The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


Contents

EC 1.1.1.314 deleted
EC 1.1.1.414 L-galactonate 5-dehydrogenase
EC 1.3.3.9 transferred
EC 1.6.1.5 transferred
EC 1.6.5.3 transferred
EC 1.6.5.8 transferred
EC 1.13.11.86 5-aminosalicylate 1,2-dioxygenase
EC 1.14.13.11 transferred
EC 1.14.13.12 transferred
EC 1.14.13.28 transferred
EC 1.14.13.30 transferred
EC 1.14.13.36 transferred
EC 1.14.13.37 transferred
EC 1.14.13.47 transferred
EC 1.14.13.52 transferred
EC 1.14.13.53 transferred
EC 1.14.13.55 transferred
EC 1.14.13.56 transferred
EC 1.14.13.57 transferred
EC 1.14.13.70 transferred
EC 1.14.13.71 transferred
EC 1.14.13.73 transferred
EC 1.14.13.75 transferred
EC 1.14.13.76 transferred
EC 1.14.13.77 transferred
EC 1.14.13.79 transferred
EC 1.14.13.85 transferred
EC 1.14.13.87 transferred
EC 1.14.13.89 transferred
EC 1.14.13.91 transferred
EC 1.14.13.93 transferred
EC 1.14.13.94 transferred
EC 1.14.13.96 transferred
EC 1.14.13.102 transferred
EC 1.14.13.103 transferred
EC 1.14.13.104 transferred
EC 1.14.13.108 transferred
EC 1.14.13.109 transferred
EC 1.14.13.110 transferred
EC 1.14.13.112 transferred
EC 1.14.13.115 transferred
EC 1.14.13.119 transferred
EC 1.14.13.120 transferred
EC 1.14.13.121 transferred
EC 1.14.13.123 transferred
EC 1.14.13.125 transferred
EC 1.14.13.133 transferred
EC 1.14.13.134 transferred
EC 1.14.13.137 transferred
EC 1.14.13.138 transferred
EC 1.14.13.139 transferred
EC 1.14.13.140 transferred
EC 1.14.13.142 transferred
EC 1.14.13.144 transferred
EC 1.14.13.145 transferred
EC 1.14.13.150 transferred
EC 1.14.13.156 transferred
EC 1.14.13.158 transferred
EC 1.14.13.162 transferred
EC 1.14.13.173 transferred
EC 1.14.13.174 transferred
EC 1.14.13.175 transferred
EC 1.14.13.176 transferred
EC 1.14.13.177 transferred
EC 1.14.13.183 transferred
EC 1.14.13.184 transferred
EC 1.14.13.185 transferred
EC 1.14.13.186 transferred
EC 1.14.13.188 transferred
EC 1.14.13.192 transferred
EC 1.14.13.193 transferred
EC 1.14.13.197 transferred
EC 1.14.13.198 transferred
EC 1.14.13.201 transferred
EC 1.14.13.202 transferred
EC 1.14.13.203 transferred
EC 1.14.13.204 transferred
EC 1.14.13.206 transferred
EC 1.14.13.213 transferred
EC 1.14.13.214 transferred
EC 1.14.14.88 isoflavone 3′-hydroxylase
EC 1.14.14.89 4′-methoxyisoflavone 2′-hydroxylase
EC 1.14.14.90 isoflavone 2′-hydroxylase
EC 1.14.14.91 trans-cinnamate 4-monooxygenase
EC 1.14.14.92 benzoate 4-monooxygenase
EC 1.14.14.93 3,9-dihydroxypterocarpan 6a-monooxygenase
EC 1.14.14.94 leukotriene-B4 20-monooxygenase
EC 1.14.14.95 germacrene A hydroxylase
EC 1.14.14.96 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase
EC 1.14.14.97 methyltetrahydroprotoberberine 14-monooxygenase
EC 1.14.14.98 protopine 6-monooxygenase
EC 1.14.14.99 (S)-limonene 3-monooxygenase
EC 1.14.14.100 dihydrosanguinarine 10-monooxygenase
EC 1.14.14.101 dihydrochelirubine 12-monooxygenase
EC 1.14.14.102 N-methylcoclaurine 3′-monooxygenase
EC 1.14.14.103 tabersonine 16-hydroxylase
EC 1.14.14.104 vinorine hydroxylase
EC 1.14.14.105 taxane 10β-hydroxylase
EC 1.14.14.106 taxane 13α-hydroxylase
EC 1.14.14.107 ent-kaurenoic acid monooxygenase
EC 1.14.14.108 2,5-diketocamphane 1,2-monooxygenase
EC 1.14.14.109 3-hydroxyindolin-2-one monooxygenase
EC 1.14.14.110 2-hydroxy-1,4-benzoxazin-3-one monooxygenase
EC 1.14.14.111 9β-pimara-7,15-diene oxidase
EC 1.14.14.112 ent-cassa-12,15-diene 11-hydroxylase
EC 1.14.14.113 α-humulene 10-hydroxylase
EC 1.14.14.114 amorpha-4,11-diene 12-monooxygenase
EC 1.14.14.115 11-oxo-β-amyrin 30-oxidase
EC 1.14.14.116 averantin hydroxylase
EC 1.14.14.117 aflatoxin B synthase
EC 1.14.14.118 tryprostatin B 6-hydroxylase
EC 1.14.14.119 fumitremorgin C monooxygenase
EC 1.14.14.120 dammarenediol 12-hydroxylase
EC 1.14.14.121 protopanaxadiol 6-hydroxylase
EC 1.14.14.122 oryzalexin E synthase
EC 1.14.14.123 oryzalexin D synthase
EC 1.14.14.124 dihydromonacolin L hydroxylase
EC 1.14.14.125 monacolin L hydroxylase
EC 1.14.14.126 β-amyrin 28-monooxygenase
EC 1.14.14.127 methyl farnesoate epoxidase
EC 1.14.14.128 farnesoate epoxidase
EC 1.14.14.129 long-chain acyl-CoA ω-monooxygenase
EC 1.14.14.130 laurate 7-monooxygenase
EC 1.14.14.131 bursehernin 5′-monooxygenase
EC 1.14.14.132 (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase
EC 1.14.14.133 1,8-cineole 2-endo-monooxygenase
EC 1.14.14.134 β-amyrin 24-hydroxylase
EC 1.14.14.135 glyceollin synthase
EC 1.14.14.136 deoxysarpagine hydroxylase
EC 1.14.14.137 (+)-abscisic acid 8′-hydroxylase
EC 1.14.14.138 lithocholate 6β-hydroxylase
EC 1.14.14.139 5β-cholestane-3α,7α-diol 12α-hydroxylase
EC 1.14.14.140 licodione synthase
EC 1.14.14.141 psoralen synthase
EC 1.14.14.142 8-dimethylallylnaringenin 2′-hydroxylase
EC 1.14.14.143 (+)-menthofuran synthase
EC 1.14.14.144 abieta-7,13-diene hydroxylase
EC 1.14.14.145 abieta-7,13-dien-18-ol hydroxylase
EC 1.14.14.146 geranylgeraniol 18-hydroxylase
EC 1.14.14.147 3-epi-6-deoxocathasterone 23-monooxygenase
EC 1.14.14.148 angelicin synthase
EC 1.14.14.149 5-epiaristolochene 1,3-dihydroxylase
EC 1.14.14.150 costunolide synthase
EC 1.14.14.151 premnaspirodiene oxygenase
EC 1.14.14.152 β-amyrin 11-oxidase
EC 1.14.14.153 indole-2-monooxygenase
EC 1.14.14.154 sterol 14α-demethylase
EC 1.14.14.155 3,6-diketocamphane 1,2-monooxygenase
EC 1.14.14.156 tryptophan N-monooxygenase
EC 1.14.14.157 indolin-2-one monooxygenase
EC 1.14.14.158 carotenoid ε hydroxylase
EC 1.14.15.31 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
EC 1.14.15.32 pentalenene oxygenase
EC 1.14.15.33 pikromycin synthase
EC 1.14.15.34 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
EC 1.14.15.35 6-deoxyerythronolide B hydroxylase
EC 1.14.19.62 secologanin synthase
EC 1.14.19.63 pseudobaptigenin synthase
EC 1.14.19.64 (S)-stylopine synthase
EC 1.14.19.65 (S)-cheilanthifoline synthase
EC 1.14.19.66 berbamunine synthase
EC 1.14.19.67 salutaridine synthase
EC 1.14.19.68 (S)-canadine synthase
EC 1.14.19.69 biflaviolin synthase
EC 1.14.19.70 mycocyclosin synthase
EC 1.14.19.71 fumitremorgin C synthase
EC 1.14.19.72 (–)-pluviatolide synthase
EC 1.14.19.73 (S)-nandinine synthase
EC 1.14.19.74 (+)-piperitol/(+)-sesamin synthase
EC 1.14.20.14 hapalindole-type alkaloid chlorinase
EC 1.14.20.15 L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
EC 1.14.21.1 transferred
EC 1.14.21.2 transferred
EC 1.14.21.3 transferred
EC 1.14.21.4 transferred
EC 1.14.21.5 transferred
EC 1.14.21.7 transferred
EC 1.14.21.8 transferred
EC 1.14.21.9 transferred
EC 1.14.21.10 transferred
EC 1.14.21.11 transferred
EC 1.14.21.12 transferred
EC 1.14.99.43 transferred
EC 1.14.99.45 transferred
EC 1.14.99.49 transferred
EC 1.14.99.61 cyclooctat-9-en-7-ol 5-monooxygenase
EC 1.14.99.62 cyclooctatin synthase
EC 1.14.99.63 β-carotene 4-ketolase
EC 1.14.99.64 zeaxanthin 4-ketolase
EC 1.17 Acting on CH or CH2 groups
EC 1.17.9.1 4-methylphenol dehydrogenase (hydroxylating)
EC 1.17.99.1 transferred
EC 1.18.1.8 transferred
EC 1.21.98.4 PqqA peptide cyclase
EC 2.1.1.349 toxoflavin synthase
EC 2.3.1.273 diglucosylglycerate octanoyltransferase
EC 2.4.1.358 acylphloroglucinol glucosyltransferase
*EC 2.5.1.17 corrinoid adenosyltransferase
EC 2.5.1.77 transferred
EC 2.5.1.147 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase
*EC 2.7.2.2 carbamate kinase
EC 2.8.5.2 L-cysteine S-thiosulfotransferase
*EC 3.4.19.9 folate γ-glutamyl hydrolase
EC 3.6.3.1 transferred
EC 3.6.3.6 transferred
EC 3.6.3.7 transferred
EC 3.6.3.14 transferred
EC 3.6.3.15 transferred
EC 3.6.3.18 transferred
EC 3.6.3.19 transferred
EC 3.6.3.21 transferred
EC 3.6.3.22 transferred
EC 3.6.3.27 transferred
EC 3.6.3.28 transferred
EC 3.6.3.44 transferred
EC 3.6.3.46 transferred
EC 3.6.4.3 transferred
EC 3.6.4.11 deleted
EC 4.1.1.3 transferred
EC 4.1.1.41 transferred
*EC 4.1.1.99 phosphomevalonate decarboxylase
EC 4.1.1.112 oxaloacetate decarboxylase
EC 4.1.99.24 L-tyrosine isonitrile synthase
EC 4.1.99.25 L-tryptophan isonitrile synthase
EC 4.3.1.32 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
EC 4.3.2.10 imidazole glycerol-phosphate synthase
EC 4.3.99.2 transferred
EC 4.4.1.6 transferred
EC 4.4.1.8 transferred
EC 5.6 Isomerases altering macromolecular conformation
EC 5.6.1 Enzymes altering polypeptide conformation or assembly
EC 5.6.1.1 microtubule-severing ATPase
*EC 6.2.1.2 medium-chain acyl-CoA ligase
EC 7 Translocases
EC 7.1 Catalysing the translocation of hydrons
EC 7.1.1 Linked to oxidoreductase reactions
EC 7.1.1.1 proton-translocating NAD(P)+ transhydrogenase
EC 7.1.1.2 NADH:ubiquinone reductase (H+-translocating)
EC 7.1 Catalysing the translocation of hydrons
EC 7.1.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.1.2.1 P-type H+-exporting transporter
EC 7.1.2.2 H+-transporting two-sector ATPase
EC 7.1 Catalysing the translocation of hydrons
EC 7.1.3 Linked to the hydrolysis of diphosphate
EC 7.1.3.1 H+-exporting diphosphatase
EC 7.2 Catalysing the translocation of inorganic cations
EC 7.2.1 Linked to oxidoreductase reactions
EC 7.2.1.1 NADH:ubiquinone reductase (Na+-transporting)
EC 7.2.1.2 ferredoxin—NAD+ oxidoreductase (Na+-transporting)
EC 7.2 Catalysing the translocation of inorganic cations
EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.2.2.1 Na+-transporting two-sector ATPase
EC 7.2.2.2 ABC-type Cd2+ transporter
EC 7.2.2.3 P-type Na+ transporter
EC 7.2.2.4 ABC-type Na+ transporter
EC 7.2 Catalysing the translocation of inorganic cations
EC 7.2.4 Linked to decarboxylation
EC 7.2.4.1 carboxybiotin decarboxylase
EC 7.2.4.2 oxaloacetate decarboxylase (Na+ extruding)
EC 7.2.4.3 (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
EC 7.3 Catalysing the translocation of inorganic anions and their chelates
EC 7.3.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.3.2.1 ABC-type phosphate transporter
EC 7.3.2.2 ABC-type phosphonate transporter
EC 7.4 Catalysing the translocation of amino acids and peptides
EC 7.4.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.4.2.1 ABC-type polar-amino-acid transporter
EC 7.4.2.2 ABC-type nonpolar-amino-acid transporter
EC 7.5 Catalysing the translocation of carbohydrates and their derivatives
EC 7.5.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.5.2.1 ABC-type maltose transporter
EC 7.5.2.2 ABC-type oligosaccharide transporter
EC 7.6 Catalysing the translocation of other compounds
EC 7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
EC 7.6.2.1 P-type phospholipid transporter
EC 7.6.2.2 ABC-type xenobiotic transporter
EC 7.6.2.3 ABC-type glutathione-S-conjugate transporter


EC 1.1.1.314
Deleted entry: germacrene A alcohol dehydrogenase. Now known to be catalyzed by EC 1.14.14.95, germacrene A hydroxylase
[EC 1.1.1.314 created 2011, deleted 2018]
 
 
EC 1.1.1.414
Accepted name: L-galactonate 5-dehydrogenase
Reaction: L-galactonate + NAD+ = D-tagaturonate + NADH + H+
Other name(s): lgoD (gene name); lgaC (gene name)
Systematic name: L-galactonate:NAD+ 5-oxidoreductase
Comments: The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Cooper, R.A. The pathway for L-galactonate catabolism in Escherichia coli K-12. FEBS Lett. 103 (1979) 216–220. [PMID: 381020]
2.  Kuivanen, J. and Richard, P. The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate. Appl. Biochem. Biotechnol. 173 (2014) 1829–1835. [PMID: 24861318]
3.  Hobbs, M.E., Williams, H.J., Hillerich, B., Almo, S.C. and Raushel, F.M. L-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota. Biochemistry 53 (2014) 4661–4670. [DOI] [PMID: 24963813]
[EC 1.1.1.414 created 2018]
 
 
EC 1.3.3.9
Transferred entry: secologanin synthase. Now EC 1.14.19.62, secologanin synthase
[EC 1.3.3.9 created 2002, deleted 2018]
 
 
EC 1.6.1.5
Transferred entry: proton-translocating NAD(P)+ transhydrogenase. Now EC 7.1.1.1, proton-translocating NAD(P)+ transhydrogenase
[EC 1.6.1.5 created 2015, deleted 2018]
 
 
EC 1.6.5.3
Transferred entry: NADH:ubiquinone reductase (H+-translocating). Now EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating)
[EC 1.6.5.3 created 1961, deleted 1965, reinstated 1983, modified 2011, modified 2013, deleted 2018]
 
 
EC 1.6.5.8
Transferred entry: NADH:ubiquinone reductase (Na+-transporting). Now EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting)
[EC 1.6.5.8 created 2011, deleted 2018]
 
 
EC 1.13.11.86
Accepted name: 5-aminosalicylate 1,2-dioxygenase
Reaction: 5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
Glossary: 5-aminosalicylate = 5-amino-2-hydroxybenzoate
Other name(s): mabB (gene name)
Systematic name: 5-aminosalicylate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Requires Fe(II). The enzyme, characterized from different bacteria, is a nonheme iron dioxygenase in the bicupin family.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Stolz, A., Nortemann, B. and Knackmuss, H.J. Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage. Biochem. J. 282 (1992) 675–680. [PMID: 1554350]
2.  Yu, H., Zhao, S. and Guo, L. Novel gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme. J. Bacteriol. 200 (2018) . [PMID: 29038259]
[EC 1.13.11.86 created 2018]
 
 
EC 1.14.13.11
Transferred entry: trans-cinnamate 4-monooxygenase. Now EC 1.14.14.91, trans-cinnamate 4-monooxygenase
[EC 1.14.13.11 created 1976, deleted 2018]
 
 
EC 1.14.13.12
Transferred entry: benzoate 4-monooxygenase. Now EC 1.14.14.92, benzoate 4-monooxygenase
[EC 1.14.13.12 created 1976, deleted 2018]
 
 
EC 1.14.13.28
Transferred entry: 3,9-dihydroxypterocarpan 6a-monooxygenase. Now EC 1.14.14.93, 3,9-dihydroxypterocarpan 6a-monooxygenase
[EC 1.14.13.28 created 1989, deleted 2018]
 
 
EC 1.14.13.30
Transferred entry: leukotriene-B4 20-monooxygenase. Now EC 1.14.14.94, leukotriene-B4 20-monooxygenase
[EC 1.14.13.30 created 1989, deleted 2018]
 
 
EC 1.14.13.36
Transferred entry: 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase. Now EC 1.14.14.96, 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase
[EC 1.14.13.36 created 1990, deleted 2018]
 
 
EC 1.14.13.37
Transferred entry: methyltetrahydroprotoberberine 14-monooxygenase. Now EC 1.14.14.97, methyltetrahydroprotoberberine 14-monooxygenase
[EC 1.14.13.37 created 1990, deleted 2018]
 
 
EC 1.14.13.47
Transferred entry: (S)-limonene 3-monooxygenase. Now EC 1.14.14.99, (S)-limonene 3-monooxygenase
[EC 1.14.13.47 created 1992, modified 2003, deleted 2018]
 
 
EC 1.14.13.52
Transferred entry: isoflavone 3′-hydroxylase. Now EC 1.14.14.88, isoflavone 3′-hydroxylase
[EC 1.14.13.52 created 1992, deleted 2018]
 
 
EC 1.14.13.53
Transferred entry: 4′-methoxyisoflavone 2′-hydroxylase. Now EC 1.14.14.89, 4′-methoxyisoflavone 2′-hydroxylase
[EC 1.14.13.53 created 1992, modified 2005, deleted 2018]
 
 
EC 1.14.13.55
Transferred entry: protopine 6-monooxygenase. Now EC 1.14.14.98, protopine 6-monooxygenase
[EC 1.14.13.55 created 1999, deleted 2018]
 
 
EC 1.14.13.56
Transferred entry: dihydrosanguinarine 10-monooxygenase. Now EC 1.14.14.100, dihydrosanguinarine 10-monooxygenase
[EC 1.14.13.56 created 1999, deleted 2018]
 
 
EC 1.14.13.57
Transferred entry: dihydrochelirubine 12-monooxygenase. Now EC 1.14.14.101, dihydrochelirubine 12-monooxygenase
[EC 1.14.13.57 created 1999, deleted 2018]
 
 
EC 1.14.13.70
Transferred entry: sterol 14α-demethylase. Now EC 1.14.14.154, sterol 14α-demethylase
[EC 1.14.13.70 created 2001, modified 2013, deleted 2018]
 
 
EC 1.14.13.71
Transferred entry: N-methylcoclaurine 3′-monooxygenase. Now EC 1.14.14.102, N-methylcoclaurine 3′-monooxygenase
[EC 1.14.13.71 created 2001, deleted 2018]
 
 
EC 1.14.13.73
Transferred entry: tabersonine 16-hydroxylase. Now EC 1.14.14.103, tabersonine 16-hydroxylase
[EC 1.14.13.73 created 2002, deleted 2018]
 
 
EC 1.14.13.75
Transferred entry: vinorine hydroxylase. Now EC 1.14.14.104, vinorine hydroxylase
[EC 1.14.13.75 created 2002, deleted 2018]
 
 
EC 1.14.13.76
Transferred entry: taxane 10β-hydroxylase. Now EC 1.14.14.105, taxane 10β-hydroxylase
[EC 1.14.13.76 created 2002, deleted 2018]
 
 
EC 1.14.13.77
Transferred entry: taxane 13α-hydroxylase. Now EC 1.14.14.106, taxane 13α-hydroxylase
[EC 1.14.13.77 created 2002, deleted 2018]
 
 
EC 1.14.13.79
Transferred entry: ent-kaurenoic acid oxidase. Now EC 1.14.14.107, ent-kaurenoic acid oxidase
[EC 1.14.13.79 created 2002, deleted 2018]
 
 
EC 1.14.13.85
Transferred entry: glyceollin synthase. Now EC 1.14.14.135, glyceollin synthase
[EC 1.14.13.85 created 2004, deleted 2018]
 
 
EC 1.14.13.87
Transferred entry: licodione synthase. Now EC 1.14.14.140, licodione synthase
[EC 1.14.13.87 created 2004, deleted 2018]
 
 
EC 1.14.13.89
Transferred entry: isoflavone 2-hydroxylase. Now EC 1.14.14.90, isoflavone 2-hydroxylase
[EC 1.14.13.89 created 2005, deleted 2018]
 
 
EC 1.14.13.91
Transferred entry: deoxysarpagine hydroxylase. Now EC 1.14.14.136, deoxysarpagine hydroxylase
[EC 1.14.13.91 created 2005, deleted 2018]
 
 
EC 1.14.13.93
Transferred entry: (+)-abscisic acid 8-hydroxylase. Now EC 1.14.14.137, (+)-abscisic acid 8-hydroxylase
[EC 1.14.13.93 created 2005, deleted 2018]
 
 
EC 1.14.13.94
Transferred entry: lithocholate 6β-hydroxylase. Now EC 1.14.14.138, lithocholate 6β-hydroxylase
[EC 1.14.13.94 created 2005, deleted 2018]
 
 
EC 1.14.13.96
Transferred entry: 5β-cholestane-3α,7α-diol 12α-hydroxylase. Now EC 1.14.14.139, 5β-cholestane-3α,7α-diol 12α-hydroxylase
[EC 1.14.13.96 created 2005, deleted 2018]
 
 
EC 1.14.13.102
Transferred entry: psoralen synthase. Now EC 1.14.14.141, psoralen synthase
[EC 1.14.13.102 created 2007, deleted 2018]
 
 
EC 1.14.13.103
Transferred entry: 8-dimethylallylnaringenin 2-hydroxylase. Now EC 1.14.14.142, 8-dimethylallylnaringenin 2-hydroxylase
[EC 1.14.13.103 created 2007, deleted 2018]
 
 
EC 1.14.13.104
Transferred entry: (+)-menthofuran synthase. Now EC 1.14.14.143, (+)-menthofuran synthase
[EC 1.14.13.104 created 2008, deleted 2018]
 
 
EC 1.14.13.108
Transferred entry: abieta-7,13-diene hydroxylase. Now EC 1.14.14.144, abieta-7,13-diene hydroxylase
[EC 1.14.13.108 created 2009, modified 2012, deleted 2018]
 
 
EC 1.14.13.109
Transferred entry: abieta-7,13-dien-18-ol hydroxylase. Now EC 1.14.14.145, abieta-7,13-dien-18-ol hydroxylase
[EC 1.14.13.109 created 2009, modified 2012, deleted 2018]
 
 
EC 1.14.13.110
Transferred entry: geranylgeraniol 18-hydroxylase. Now EC 1.14.14.146, geranylgeraniol 18-hydroxylase
[EC 1.14.13.110 created 2009, deleted 2018]
 
 
EC 1.14.13.112
Transferred entry: 3-epi-6-deoxocathasterone 23-monooxygenase. Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase
[EC 1.14.13.112 created 2010, deleted 2018]
 
 
EC 1.14.13.115
Transferred entry: angelicin synthase. Now EC 1.14.14.148, angelicin synthase
[EC 1.14.13.115 created 2010, deleted 2018]
 
 
EC 1.14.13.119
Transferred entry: 5-epiaristolochene 1,3-dihydroxylase. Now EC 1.14.14.149, 5-epiaristolochene 1,3-dihydroxylase
[EC 1.14.13.119 created 2011, deleted 2018]
 
 
EC 1.14.13.120
Transferred entry: costunolide synthase. Now EC 1.14.14.150, costunolide synthase
[EC 1.14.13.120 created 2011, deleted 2018]
 
 
EC 1.14.13.121
Transferred entry: premnaspirodiene oxygenase. Now EC 1.14.14.151, premnaspirodiene oxygenase
[EC 1.14.13.121 created 2011, deleted 2018]
 
 
EC 1.14.13.123
Transferred entry: germacrene A hydroxylase. Now EC 1.14.14.95, germacrene A hydroxylase
[EC 1.14.13.123 created 2011, deleted 2018]
 
 
EC 1.14.13.125
Transferred entry: tryptophan N-monooxygenase. Now EC 1.14.14.156, tryptophan N-monooxygenase
[EC 1.14.13.125 created 2011, deleted 2018]
 
 
EC 1.14.13.133
Transferred entry: pentalenene oxygenase. Now EC 1.14.15.32, pentalenene oxygenase
[EC 1.14.13.133 created 2011, deleted 2018]
 
 
EC 1.14.13.134
Transferred entry: β-amyrin 11-oxidase. Now EC 1.14.14.152, β-amyrin 11-oxidase
[EC 1.14.13.134 created 2011, deleted 2018]
 
 
EC 1.14.13.137
Transferred entry: indole-2-monooxygenase. Now EC 1.14.14.153, indole-2-monooxygenase
[EC 1.14.13.137 created 2012, deleted 2018]
 
 
EC 1.14.13.138
Transferred entry: indolin-2-one monooxygenase. Now EC 1.14.14.157, indolin-2-one monooxygenase
[EC 1.14.13.138 created 2012, deleted 2018]
 
 
EC 1.14.13.139
Transferred entry: 3-hydroxyindolin-2-one monooxygenase. Now EC 1.14.14.109, 3-hydroxyindolin-2-one monooxygenase
[EC 1.14.13.139 created 2012, deleted 2018]
 
 
EC 1.14.13.140
Transferred entry: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase. Now EC 1.14.14.110, 2-hydroxy-1,4-benzoxazin-3-one monooxygenase.
[EC 1.14.13.140 created 2012, deleted 2018]
 
 
EC 1.14.13.142
Transferred entry: 3-ketosteroid 9α-monooxygenase. Now EC 1.14.15.30, 3-ketosteroid 9α-monooxygenase
[EC 1.14.13.142 created 2012, deleted 2018]
 
 
EC 1.14.13.144
Transferred entry: 9β-pimara-7,15-diene oxidase. Now EC 1.14.14.111, 9β-pimara-7,15-diene oxidase.
[EC 1.14.13.144 created 2012, deleted 2018]
 
 
EC 1.14.13.145
Transferred entry: ent-cassa-12,15-diene 11-hydroxylase. Now EC 1.14.14.112, ent-cassa-12,15-diene 11-hydroxylase.
[EC 1.14.13.145 created 2012, deleted 2018]
 
 
EC 1.14.13.150
Transferred entry: α-humulene 10-hydroxylase. Now EC 1.14.14.113, α-humulene 10-hydroxylase.
[EC 1.14.13.150 created 2012, deleted 2018]
 
 
EC 1.14.13.156
Transferred entry: 1,8-cineole 2-endo-monooxygenase. Now EC 1.14.14.133, 1,8-cineole 2-endo-monooxygenase
[EC 1.14.13.156 created 2012, deleted 2018]
 
 
EC 1.14.13.158
Transferred entry: amorpha-4,11-diene 12-monooxygenase. Now EC 1.14.14.114, amorpha-4,11-diene 12-monooxygenase.
[EC 1.14.13.158 created 2012, deleted 2018]
 
 
EC 1.14.13.162
Transferred entry: 2,5-diketocamphane 1,2-monooxygenase. Now EC 1.14.14.108, 2,5-diketocamphane 1,2-monooxygenase
[EC 1.14.13.162 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, deleted 2018]
 
 
EC 1.14.13.173
Transferred entry: 11-oxo-β-amyrin 30-oxidase. Now EC 1.14.14.115, 11-oxo-β-amyrin 30-oxidase.
[EC 1.14.13.173 created 2013, deleted 2018]
 
 
EC 1.14.13.174
Transferred entry: averantin hydroxylase. Now EC 1.14.14.116, averantin hydroxylase
[EC 1.14.13.174 created 2013, deleted 2018]
 
 
EC 1.14.13.175
Transferred entry: aflatoxin B synthase. Now EC 1.14.14.117, aflatoxin B synthase
[EC 1.14.13.175 created 2013, deleted 2018]
 
 
EC 1.14.13.176
Transferred entry: tryprostatin B 6-hydroxylase. Now EC 1.14.14.118, tryprostatin B 6-hydroxylase
[EC 1.14.13.176 created 2013, deleted 2018]
 
 
EC 1.14.13.177
Transferred entry: fumitremorgin C monooxygenase. Now EC 1.14.14.119, fumitremorgin C monooxygenase
[EC 1.14.13.177 created 2013, deleted 2018]
 
 
EC 1.14.13.183
Transferred entry: dammarenediol 12-hydroxylase. Now EC 1.14.14.120, dammarenediol 12-hydroxylase
[EC 1.14.13.183 created 2013, deleted 2018]
 
 
EC 1.14.13.184
Transferred entry: protopanaxadiol 6-hydroxylase. Now EC 1.14.14.121, protopanaxadiol 6-hydroxylase
[EC 1.14.13.184 created 2013, deleted 2018]
 
 
EC 1.14.13.185
Transferred entry: pikromycin synthase. Now EC 1.14.15.33, pikromycin synthase
[EC 1.14.13.185 created 2014, deleted 2018]
 
 
EC 1.14.13.186
Transferred entry: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase. Now EC 1.14.15.34, 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
[EC 1.14.13.186 created 2014, deleted 2018]
 
 
EC 1.14.13.188
Transferred entry: 6-deoxyerythronolide B hydroxylase. Now EC 1.14.15.35, 6-deoxyerythronolide B hydroxylase
[EC 1.14.13.188 created 2014, deleted 2018]
 
 
EC 1.14.13.192
Transferred entry: oryzalexin E synthase. Now EC 1.14.14.122, oryzalexin E synthase
[EC 1.14.13.192 created 2014, deleted 2018]
 
 
EC 1.14.13.193
Transferred entry: oryzalexin D synthase. Now EC 1.14.14.123, oryzalexin D synthase
[EC 1.14.13.193 created 2014, deleted 2018]
 
 
EC 1.14.13.197
Transferred entry: dihydromonacolin L hydroxylase. Now EC 1.14.14.124, dihydromonacolin L hydroxylase
[EC 1.14.13.197 created 2014, deleted 2018]
 
 
EC 1.14.13.198
Transferred entry: monacolin L hydroxylase. Now EC 1.14.14.125, monacolin L hydroxylase
[EC 1.14.13.198 created 2014, deleted 2018]
 
 
EC 1.14.13.201
Transferred entry: β-amyrin 28-monooxygenase. Now EC 1.14.14.126, β-amyrin 28-monooxygenase
[EC 1.14.13.201 created 2015, deleted 2018]
 
 
EC 1.14.13.202
Transferred entry: methyl farnesoate epoxidase. Now EC 1.14.14.127, methyl farnesoate epoxidase
[EC 1.14.13.202 created 2015, deleted 2018]
 
 
EC 1.14.13.203
Transferred entry: farnesoate epoxidase. Now EC 1.14.14.128, farnesoate epoxidase
[EC 1.14.13.203 created 2015, deleted 2018]
 
 
EC 1.14.13.204
Transferred entry: long-chain acyl-CoA ω-monooxygenase. Now EC 1.14.14.129, long-chain acyl-CoA ω-monooxygenase
[EC 1.14.13.204 created 2015, deleted 2018]
 
 
EC 1.14.13.206
Transferred entry: laurate 7-monooxygenase. Now EC 1.14.14.130, laurate 7-monooxygenase
[EC 1.14.13.206 created 2015, deleted 2018]
 
 
EC 1.14.13.213
Transferred entry: bursehernin 5-monooxygenase. Now EC 1.14.14.131, bursehernin 5-monooxygenase
[EC 1.14.13.213 created 2016, deleted 2018]
 
 
EC 1.14.13.214
Transferred entry: (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase. Now EC 1.14.14.132, (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase
[EC 1.14.13.214 created 2016, deleted 2018]
 
 
EC 1.14.14.88
Accepted name: isoflavone 3′-hydroxylase
Reaction: formononetin + [reduced NADPH—hemoprotein reductase] + O2 = calycosin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of medicarpin and formononetin derivatives biosynthesis, click here
Glossary: calycosin = 3′-hydroxyformononetin
Other name(s): isoflavone 3′-monooxygenase; CYP81E9
Systematic name: formononetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Also acts on biochanin A and other isoflavones with a 4′-methoxy group. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 110183-50-1
References:
1.  Hinderer, W., Flentje, U. and Barz, W. Microsomal isoflavone 2′-hydroxylases and 3′-hydroxylases from chickpea (Cicer arietinum L) cell-suspensions induced for pterocarpan phytoalexin formation. FEBS Lett. 214 (1987) 101–106.
[EC 1.14.14.88 created 1992 as EC 1.14.13.52, transferred 2018 to EC 1.14.14.88]
 
 
EC 1.14.14.89
Accepted name: 4′-methoxyisoflavone 2′-hydroxylase
Reaction: formononetin + [reduced NADPH—hemoprotein reductase] + O2 = 2′-hydroxyformononetin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of the biosynthesis of formononetin and derivatives, click here
Other name(s): CYP81E1 (gene name); CYP81E3 (gene name); CYP81E7 (gene name); isoflavone 2′-monooxygenase (ambiguous); isoflavone 2′-hydroxylase (ambiguous)
Systematic name: formononetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Acts on isoflavones with a 4′-methoxy group, such as formononetin and biochanin A. Involved in the biosynthesis of the pterocarpin phytoalexins medicarpin and maackiain. EC 1.14.14.90, isoflavone 2′-hydroxylase, is less specific and acts on other isoflavones as well as 4′-methoxyisoflavones.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 110183-49-8
References:
1.  Hinderer, W., Flentje, U. and Barz, W. Microsomal isoflavone 2′-hydroxylases and 3′-hydroxylases from chickpea (Cicer arietinum L) cell-suspensions induced for pterocarpan phytoalexin formation. FEBS Lett. 214 (1987) 101–106.
2.  Akashi, T., Aoki, T. and Ayabe, S.-I. CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2′-hydroxylase. Biochem. Biophys. Res. Commun. 251 (1998) 67–70. [DOI] [PMID: 9790908]
3.  Liu, C.J., Huhman, D., Sumner, L.W. and Dixon, R.A. Regiospecific hydroxylation of isoflavones by cytochrome p450 81E enzymes from Medicago truncatula. Plant J. 36 (2003) 471–484. [PMID: 14617078]
[EC 1.14.14.89 created 1992 as EC 1.14.13.53, modified 2005, transferred 2018 to EC 1.14.14.89]
 
 
EC 1.14.14.90
Accepted name: isoflavone 2′-hydroxylase
Reaction: an isoflavone + [reduced NADPH—hemoprotein reductase] + O2 = a 2′-hydroxyisoflavone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of the biosynthesis of formononetin and derivatives, click here
Other name(s): isoflavone 2′-monooxygenase; CYP81E1; CYP Ge-3
Systematic name: isoflavone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Acts on daidzein, formononetin and genistein. EC 1.14.14.89, 4′-methoxyisoflavone 2′-hydroxylase, has the same reaction but is more specific as it requires a 4′-methoxyisoflavone.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 110183-49-8
References:
1.  Akashi, T., Aoki, T. and Ayabe, S.-I. CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2′-hydroxylase. Biochem. Biophys. Res. Commun. 251 (1998) 67–70. [DOI] [PMID: 9790908]
[EC 1.14.14.90 created 2005 as EC 1.14.13.89, transferred 2018 to EC 1.14.14.90]
 
 
EC 1.14.14.91
Accepted name: trans-cinnamate 4-monooxygenase
Reaction: trans-cinnamate + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxycinnamate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of chalcone and stilbene biosynthesis, click here
Other name(s): cinnamic acid 4-hydroxylase; CA4H; cytochrome P450 cinnamate 4-hydroxylase; cinnamate 4-hydroxylase; cinnamate 4-monooxygenase; cinnamate hydroxylase; cinnamic 4-hydroxylase; cinnamic acid 4-monooxygenase; cinnamic acid p-hydroxylase; t-cinnamic acid hydroxylase; trans-cinnamate 4-hydroxylase; trans-cinnamic acid 4-hydroxylase; CYP73A1 (gene name)
Systematic name: trans-cinnamate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in flavonoid biosynthesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9077-75-2
References:
1.  Potts, J.R.M., Weklych, R. and Conn, E.E. The 4-hydroxylation of cinnamic acid by sorghum microsomes and the requirement for cytochrome P-450. J. Biol. Chem. 249 (1974) 5019–5026. [PMID: 4153152]
2.  Russell, D.W. and Conn, E.E. The cinnamic acid 4-hydroxylase of pea seedlings. Arch. Biochem. Biophys. 122 (1967) 256–268. [DOI] [PMID: 4383827]
3.  Pierrel, M.A., Batard, Y., Kazmaier, M., Mignotte-Vieux, C., Durst, F. and Werck-Reichhart, D. Catalytic properties of the plant cytochrome P450 CYP73 expressed in yeast. Substrate specificity of a cinnamate hydroxylase. Eur. J. Biochem. 224 (1994) 835–844. [PMID: 7925408]
[EC 1.14.14.91 created 1976 as EC 1.14.13.11, transferred 2018 to EC 1.14.14.91]
 
 
EC 1.14.14.92
Accepted name: benzoate 4-monooxygenase
Reaction: benzoate + [reduced NADPH—hemoprotein reductase] + O2 = 4-hydroxybenzoate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of benzoate metabolism, click here
Other name(s): benzoic acid 4-hydroxylase; benzoate 4-hydroxylase; benzoic 4-hydroxylase; benzoate-p-hydroxylase; p-hydroxybenzoate hydroxylase; CYP53A1 (gene name)
Systematic name: benzoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in Aspergillus fungi.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD, CAS registry number: 39391-25-8
References:
1.  Reddy, C.C. and Vaidyanathan, C.S. Purification, properties and induction of a specific benzoate-4-hydroxylase from Aspergillus niger (UBC 814). Biochim. Biophys. Acta 384 (1975) 46–57. [DOI] [PMID: 236777]
2.  Faber, B.W., van Gorcom, R.F. and Duine, J.A. Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger. Arch. Biochem. Biophys. 394 (2001) 245–254. [PMID: 11594739]
[EC 1.14.14.92 created 1976 as EC 1.14.13.12, transferred 2018 to EC 1.14.14.92]
 
 
EC 1.14.14.93
Accepted name: 3,9-dihydroxypterocarpan 6a-monooxygenase
Reaction: (6aR,11aR)-3,9-dihydroxypterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = (6aS,11aS)-3,6a,9-trihydroxypterocarpan + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of glyceollin biosynthesis (part 2), click here
Other name(s): 3,9-dihydroxypterocarpan 6a-hydroxylase; 3,9-dihydroxypterocarpan 6α-monooxygenase (erroneous); CYP93A1 (gene name)
Systematic name: (6aR,11aR)-3,9-dihydroxypterocarpan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6a-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in soybean. The product of the reaction is the biosynthetic precursor of the glyceollin phytoalexins.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 92584-16-2
References:
1.  Hagmann, M.-L., Heller, W. and Grisebach, H. Induction of phytoalexin synthesis in soybean. Stereospecific 3,9-dihydroxypterocarpan 6a-hydroxylase from elicitor-induced soybean cell cultures. Eur. J. Biochem. 142 (1984) 127–131. [DOI] [PMID: 6540173]
2.  Schopfer, C.R., Kochs, G., Lottspeich, F. and Ebel, J. Molecular characterization and functional expression of dihydroxypterocarpan 6a-hydroxylase, an enzyme specific for pterocarpanoid phytoalexin biosynthesis in soybean (Glycine max L.). FEBS Lett. 432 (1998) 182–186. [PMID: 9720921]
[EC 1.14.14.93 created 1989 as EC 1.14.13.28, transferred 2018 to EC 1.14.14.93]
 
 
EC 1.14.14.94
Accepted name: leukotriene-B4 20-monooxygenase
Reaction: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH—hemoprotein reductase] + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): leukotriene-B4 20-hydroxylase; leucotriene-B4 ω-hydroxylase; LTB4 20-hydroxylase; LTB4 ω-hydroxylase; CYP4F2 (gene name); CYP4F3 (gene name)
Systematic name: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (20-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 90119-11-2
References:
1.  Romano, M.C., Eckardt, R.D., Bender, P.E., Leonard, T.B., Straub, K.M. and Newton, J.F. Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases. J. Biol. Chem. 262 (1987) 1590–1595. [PMID: 3027095]
2.  Shak, S. and Goldstein, I.M. Leukotriene B4 ω-hydroxylase in human polymorphonuclear leukocytes. Partial purification and identification as a cytochrome P-450. J. Clin. Invest. 76 (1985) 1218–1228. [DOI] [PMID: 4044832]
3.  Soberman, R.J., Harper, T.W., Murphy, R.C. and Austen, K.F. Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes. Proc. Natl Acad. Sci. USA 82 (1985) 2292–2295. [DOI] [PMID: 2986111]
[EC 1.14.14.94 created 1989 as EC 1.14.13.30, transferred 2018 to EC 1.14.14.94]
 
 
EC 1.14.14.95
Accepted name: germacrene A hydroxylase
Reaction: (+)-germacrene A + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = germacra-1(10),4,11(13)-trien-12-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) (+)-germacrene A + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) germacra-1(10),4,11(13)-trien-12-ol + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) germacra-1(10),4,11(13)-trien-12-al + O2 + [reduced NADPH—hemoprotein reductase] = germacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of costunolide biosynthesis, click here
Other name(s): GAO (gene name)
Systematic name: (+)-germacrene-A,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This plant enzyme catalyses three steps in a pathway that leads to the biosynthesis of many sesquiterpenoid lactones.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Nguyen, D.T., Gopfert, J.C., Ikezawa, N., Macnevin, G., Kathiresan, M., Conrad, J., Spring, O. and Ro, D.K. Biochemical conservation and evolution of germacrene A oxidase in asteraceae. J. Biol. Chem. 285 (2010) 16588–16598. [DOI] [PMID: 20351109]
2.  Liu, Q., Manzano, D., Tanic, N., Pesic, M., Bankovic, J., Pateraki, I., Ricard, L., Ferrer, A., de Vos, R., van de Krol, S. and Bouwmeester, H. Elucidation and in planta reconstitution of the parthenolide biosynthetic pathway. Metab. Eng. 23 (2014) 145–153. [PMID: 24704560]
[EC 1.14.14.95 created 2011 as EC 1.14.13.123, transferred 2018 to EC 1.14.14.95]
 
 
EC 1.14.14.96
Accepted name: 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase
Reaction: trans-5-O-(4-coumaroyl)-D-quinate + [reduced NADPH—hemoprotein reductase] + O2 = trans-5-O-caffeoyl-D-quinate + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase; coumaroylquinate(coumaroylshikimate) 3′-monooxygenase; CYP98A3 (gene name)
Systematic name: trans-5-O-(4-coumaroyl)-D-quinate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein, found in plants. It also acts on trans-5-O-(4-coumaroyl)shikimate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 112131-08-5
References:
1.  Kühnl, T., Koch, U., Heller, W. and Wellman, E. Chlorogenic acid biosynthesis: characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258 (1987) 226–232. [DOI] [PMID: 2821918]
2.  Schoch, G., Goepfert, S., Morant, M., Hehn, A., Meyer, D., Ullmann, P. and Werck-Reichhart, D. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem 276 (2001) 36566–36574. [PMID: 11429408]
3.  Franke, R., Humphreys, J.M., Hemm, M.R., Denault, J.W., Ruegger, M.O., Cusumano, J.C. and Chapple, C. The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism. Plant J. 30 (2002) 33–45. [PMID: 11967091]
4.  Matsuno, M., Compagnon, V., Schoch, G.A., Schmitt, M., Debayle, D., Bassard, J.E., Pollet, B., Hehn, A., Heintz, D., Ullmann, P., Lapierre, C., Bernier, F., Ehlting, J. and Werck-Reichhart, D. Evolution of a novel phenolic pathway for pollen development. Science 325 (2009) 1688–1692. [PMID: 19779199]
[EC 1.14.14.96 created 1990 as EC 1.14.13.36, transferred 2018 to EC 1.14.14.96]
 
 
EC 1.14.14.97
Accepted name: methyltetrahydroprotoberberine 14-monooxygenase
Reaction: (S)-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O2 = allocryptopine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of stylopine biosynthesis, click here and for diagram of canadine biosynthesis, click here
Other name(s): methyltetrahydroprotoberberine 14-hydroxylase; (S)-cis-N-methyltetrahydroberberine 14-monooxygenase; (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase; CYP82N4 (gene name)
Systematic name: (S)-N-methylcanadine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 113478-42-5
References:
1.  Rueffer, M. and Zenk, M.H. Enzymatic formation of protopines by a microsomal cytochrome-P-450 system of Corydalis vaginans. Tetrahedron Lett. 28 (1987) 5307–5310.
2.  Beaudoin, G.A. and Facchini, P.J. Isolation and characterization of a cDNA encoding (S)-cis-N-methylstylopine 14-hydroxylase from opium poppy, a key enzyme in sanguinarine biosynthesis. Biochem. Biophys. Res. Commun. 431 (2013) 597–603. [PMID: 23313486]
[EC 1.14.14.97 created 1990 as EC 1.14.13.37, transferred 2018 to EC 1.14.14.97]
 
 
EC 1.14.14.98
Accepted name: protopine 6-monooxygenase
Reaction: protopine + [reduced NADPH—hemoprotein reductase] + O2 = 6-hydroxyprotopine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of stylopine biosynthesis, click here
Other name(s): protopine 6-hydroxylase; CYP82N2 (gene name)
Systematic name: protopine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzophenanthridine alkaloid synthesis in higher plants.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 128561-60-4
References:
1.  Tanahashi, T. and Zenk, M.H. Elicitor induction and characterization of microsomal protopine-6-hydroxylase, the central enzyme in benzophenanthridine alkaloid biosynthesis. Phytochemistry 29 (1990) 1113–1122.
2.  Takemura, T., Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of a cytochrome P450 in sanguinarine biosynthesis from Eschscholzia californica cells. Phytochemistry 91 (2013) 100–108. [PMID: 22421633]
[EC 1.14.14.98 created 1999 as EC 1.14.13.55, transferred 2018 to EC 1.14.14.98]
 
 
EC 1.14.14.99
Accepted name: (S)-limonene 3-monooxygenase
Reaction: (S)-limonene + [reduced NADPH—hemoprotein reductase] + O2 = (–)-trans-isopiperitenol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of perillyl alcohol, isopiperitol and carveol biosynthesis, click here
Glossary: limonene = a monoterpenoid
(S)-limonene = (–)-limonene
Other name(s): (–)-limonene 3-hydroxylase; (–)-limonene 3-monooxygenase; CYP71D15 (gene name)
Systematic name: (S)-limonene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from peppermint (Mentha piperita).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD, CAS registry number: 138066-92-9
References:
1.  Karp, F., Mihaliak, C.A., Harris, J.L. and Croteau, R. Monoterpene biosynthesis: specificity of the hydroxylations of (-)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves. Arch. Biochem. Biophys. 276 (1990) 219–226. [DOI] [PMID: 2297225]
2.  Lupien, S., Karp, F., Wildung, M. and Croteau, R. Regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha) species: cDNA isolation, characterization, and functional expression of (–)-4S-limonene-3-hydroxylase and (–)-4S-limonene-6-hydroxylase. Arch. Biochem. Biophys. 368 (1999) 181–192. [PMID: 10415126]
3.  Wust, M., Little, D.B., Schalk, M. and Croteau, R. Hydroxylation of limonene enantiomers and analogs by recombinant (–)-limonene 3- and 6-hydroxylases from mint (Mentha) species: evidence for catalysis within sterically constrained active sites. Arch. Biochem. Biophys. 387 (2001) 125–136. [PMID: 11368174]
[EC 1.14.14.99 created 1992 as EC 1.14.13.47, modified 2003, transferred 2018 1.14.14.99]
 
 
EC 1.14.14.100
Accepted name: dihydrosanguinarine 10-monooxygenase
Reaction: dihydrosanguinarine + [reduced NADPH—hemoprotein reductase] + O2 = 10-hydroxydihydrosanguinarine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of chelirubine, macarpine and sanguinarine biosynthesis, click here
Other name(s): dihydrosanguinarine 10-hydroxylase
Systematic name: dihydrosanguinarine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzophenanthridine alkaloid synthesis in higher plants.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 144388-41-0
References:
1.  De-Eknamkul, W., Tanahashi, T. and Zenk, M.H. Enzymic 10-hydroxylation and 10-O-methylation of dihydrosanguinarine in dihydrochelirubine formation by Eschscholtzia. Phytochemistry 31 (1992) 2713–2717.
[EC 1.14.14.100 created 1999 as EC 1.14.13.56, transferred 2018 to EC 1.14.14.100]
 
 
EC 1.14.14.101
Accepted name: dihydrochelirubine 12-monooxygenase
Reaction: dihydrochelirubine + [reduced NADPH—hemoprotein reductase] + O2 = 12-hydroxydihydrochelirubine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of chelirubine, macarpine and sanguinarine biosynthesis, click here
Other name(s): dihydrochelirubine 12-hydroxylase
Systematic name: dihydrochelirubine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Thalictrum bulgaricum.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 158736-41-5
References:
1.  Kammerer, L., De-Eknamkul, W. and Zenk, M.H. Enzymic 12-hydroxylation and 12-O-methylation of dihydrochelirubine in dihydromacarpine formation by Thalictrum bulgaricum. Phytochemistry 36 (1994) 1409–1416.
[EC 1.14.14.101 created 1999 as EC 1.14.13.57, transferred 2018 to EC 1.14.14.101]
 
 
EC 1.14.14.102
Accepted name: N-methylcoclaurine 3′-monooxygenase
Reaction: (S)-N-methylcoclaurine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-3′-hydroxy-N-methylcoclaurine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reticuline biosynthesis, click here
Other name(s): N-methylcoclaurine 3′-hydroxylase; CYP80B1 (gene name)
Systematic name: (S)-N-methylcoclaurine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in benzylisoquinoline alkaloid synthesis in higher plants.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 202420-37-9
References:
1.  Pauli, H.H. and Kutchan, T.M. Molecular cloning and functional heterologous expression of two alleles encoding (S)-N-methylcoclaurine 3′-hydroxylase (CYP80B1), a new methyl jasmonate-inducible cytochrome P-450-dependent mono-oxygenase of benzylisoquinoline alkaloid biosynthesis. Plant J. 13 (1998) 793–801. [DOI] [PMID: 9681018]
[EC 1.14.14.102 created 2001 as 1.14.13.71, transferred 2018 to EC 1.14.14.102]
 
 
EC 1.14.14.103
Accepted name: tabersonine 16-hydroxylase
Reaction: tabersonine + [reduced NADPH—hemoprotein reductase] + O2 = 16-hydroxytabersonine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of vindoline biosynthesis, click here
Other name(s): tabersonine-11-hydroxylase; T11H; CYP71D12 (gene name)
Systematic name: tabersonine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (16-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Madagascar periwinkle (Catharanthus roseus).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 250378-34-8
References:
1.  St-Pierre, B. and De Luca, V. A cytochrome P-450 monooxygenase catalyzes the first step in the conversion of tabersonine to vindoline in Catharanthus roseus. Plant Physiol. 109 (1995) 131–139. [DOI] [PMID: 12228585]
2.  Besseau, S., Kellner, F., Lanoue, A., Thamm, A.M., Salim, V., Schneider, B., Geu-Flores, F., Hofer, R., Guirimand, G., Guihur, A., Oudin, A., Glevarec, G., Foureau, E., Papon, N., Clastre, M., Giglioli-Guivarc'h, N., St-Pierre, B., Werck-Reichhart, D., Burlat, V., De Luca, V., O'Connor, S.E. and Courdavault, V. A pair of tabersonine 16-hydroxylases initiates the synthesis of vindoline in an organ-dependent manner in Catharanthus roseus. Plant Physiol. 163 (2013) 1792–1803. [PMID: 24108213]
[EC 1.14.14.103 created 2002 as EC 1.14.13.73, transferred 2018 to EC 1.14.14.103]
 
 
EC 1.14.14.104
Accepted name: vinorine hydroxylase
Reaction: vinorine + [reduced NADPH—hemoprotein reductase] + O2 = vomilenine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of ajmaline, vinorine, vomilenine and raucaffricine biosynthesis, click here
Systematic name: vinorine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (21α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Rauvolfia serpentina. Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 162875-03-8
References:
1.  Falkenhagen, H. and Stöckligt, J. Enzymatic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalysed by a novel cytochrome P-450-dependent enzyme from plant cell cultures of Rauwolfia serpentina. Z. Naturforsch. C: Biosci. 50 (1995) 45–53.
[EC 1.14.14.104 created 2002 as EC 1.14.13.75, transferred 2018 to EC 1.14.14.104]
 
 
EC 1.14.14.105
Accepted name: taxane 10β-hydroxylase
Reaction: taxa-4(20),11-dien-5α-yl acetate + [reduced NADPH—hemoprotein reductase] + O2 = 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of taxadiene hydroxylation, click here
Other name(s): CYP725A1 (gene name); 5-α-taxadienol-10-β-hydroxylase
Systematic name: taxa-4(20),11-dien-5α-yl acetate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10β-hydroxylating)
Comments: This microsomal cytochrome-P-450 (heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 337514-75-7
References:
1.  Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [DOI] [PMID: 11396929]
2.  Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [DOI] [PMID: 11707604]
3.  Schoendorf, A., Rithner, C.D., Williams, R.M. and Croteau, R.B. Molecular cloning of a cytochrome P450 taxane 10β-hydroxylase cDNA from Taxus and functional expression in yeast. Proc. Natl. Acad. Sci. USA 98 (2001) 1501–1506. [DOI] [PMID: 11171980]
[EC 1.14.14.105 created 2002 as EC 1.14.13.76, transferred 2018 to EC 1.14.14.105]
 
 
EC 1.14.14.106
Accepted name: taxane 13α-hydroxylase
Reaction: taxa-4(20),11-dien-5α-ol + [reduced NADPH—hemoprotein reductase] + O2 = taxa-4(20),11-dien-5α,13α-diol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of taxadiene hydroxylation, click here
Other name(s): CYP725A2 (gene name)
Systematic name: taxa-4(20),11-dien-5α-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (13α-hydroxylating)
Comments: This cytochrome-P-450(heme-thiolate) enzyme from the plant Taxus cuspidata is involved in the biosynthesis of the diterpenoid antineoplastic drug taxol (paclitaxel).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 399030-58-1
References:
1.  Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265. [DOI] [PMID: 11396929]
2.  Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 98 (2001) 13595. [DOI] [PMID: 11707604]
[EC 1.14.14.106 created 2002 as EC 1.14.13.77, transferred 2018 to EC 1.14.14.106]
 
 
EC 1.14.14.107
Accepted name: ent-kaurenoic acid monooxygenase
Reaction: ent-kaur-16-en-19-oate + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = gibberellin A12 + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) ent-kaur-16-en-19-oate + [reduced NADPH—hemoprotein reductase] + O2 = ent-7α-hydroxykaur-16-en-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) ent-7α-hydroxykaur-16-en-19-oate + [reduced NADPH—hemoprotein reductase] + O2 = gibberellin A12 aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) gibberellin A12 aldehyde + [reduced NADPH—hemoprotein reductase] + O2 = gibberellin A12 + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of gibberellin A12 biosynthesis, click here
Other name(s): KAO1 (gene name); CYP88A3 (gene name); ent-kaurenoic acid oxidase
Systematic name: ent-kaur-16-en-19-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from plants. Catalyses three sucessive oxidations of ent-kaurenoic acid. The second step includes a ring-B contraction giving the gibbane skeleton. In pumpkin (Cucurbita maxima) ent-6α,7α-dihydroxykaur-16-en-19-oate is also formed.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 337507-95-6
References:
1.  Helliwell, C.A., Chandler, P.M., Poole, A., Dennis, E.S. and Peacock, W.J. The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway. Proc. Natl. Acad. Sci. USA 98 (2001) 2065–2070. [DOI] [PMID: 11172076]
[EC 1.14.14.107 created 2002 as EC 1.14.13.79, transferred 2018 to EC 1.14.14.107]
 
 
EC 1.14.14.108
Accepted name: 2,5-diketocamphane 1,2-monooxygenase
Reaction: (+)-bornane-2,5-dione + FMNH2 + O2 = (+)-5-oxo-1,2-campholide + FMN + H2O
For diagram of camphor catabolism, click here
Glossary: (+)-bornane-2,5-dione = 2,5-diketocamphane
Other name(s): 2,5-diketocamphane lactonizing enzyme; ketolactonase I (ambiguous); 2,5-diketocamphane 1,2-monooxygenase oxygenating component; 2,5-DKCMO; camP (gene name); camphor 1,2-monooxygenase; camphor ketolactonase I
Systematic name: (+)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (+)-camphor. Requires a dedicated NADH-FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1-3]. Can accept several bicyclic ketones including (+)- and (–)-camphor [6] and adamantanone [4]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD
References:
1.  Conrad, H.E., DuBus, R., Namtvedt, M.J. and Gunsalus, I.C. Mixed function oxidation. II. Separation and properties of the enzymes catalyzing camphor lactonizaton. J. Biol. Chem. 240 (1965) 495–503. [PMID: 14253460]
2.  Yu, C.A. and Gunsalus, I.C. Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components. J. Biol. Chem. 244 (1969) 6149–6152. [PMID: 4310834]
3.  Taylor, D.G. and Trudgill, P.W. Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453. J. Bacteriol. 165 (1986) 489–497. [DOI] [PMID: 3944058]
4.  Selifonov, S.A. Microbial oxidation of adamantanone by Pseudomonas putida carrying the camphor catabolic plasmid. Biochem. Biophys. Res. Commun. 186 (1992) 1429–1436. [DOI] [PMID: 1510672]
5.  Jones, K.H., Smith, R.T. and Trudgill, P.W. Diketocamphane enantiomer-specific ’Baeyer-Villiger’ monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J. Gen. Microbiol. 139 (1993) 797–805. [DOI] [PMID: 8515237]
6.  Kadow, M., Sass, S., Schmidt, M. and Bornscheuer, U.T. Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007. AMB Express 1:13 (2011). [DOI] [PMID: 21906366]
7.  Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282–3293. [PMID: 23524667]
[EC 1.14.14.108 created 1972 as EC 1.14.15.2, transferred 2012 to EC 1.14.13.162, transferred 2018 to EC 1.14.14.108]
 
 
EC 1.14.14.109
Accepted name: 3-hydroxyindolin-2-one monooxygenase
Reaction: 3-hydroxyindolin-2-one + [reduced NADPH—hemoprotein reductase] + O2 = 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of benzoxazinone biosynthesis, click here
Glossary: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX4 (gene name); CYP71C1 (gene name)
Systematic name: 3-hydroxyindolin-2-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxy-2H-1,4-benzoxazin-3(4H)-one-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925–930. [DOI] [PMID: 10385992]
2.  Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696–699. [DOI] [PMID: 9235894]
3.  Spiteller, P., Glawischnig, E., Gierl, A. and Steglich, W. Studies on the biosynthesis of 2-hydroxy-1,4-benzoxazin-3-one (HBOA) from 3-hydroxyindolin-2-one in Zea mays. Phytochemistry 57 (2001) 373–376. [DOI] [PMID: 11393516]
[EC 1.14.14.109 created 2012 as EC 1.14.13.139, transferred 2018 to EC 1.14.14.109]
 
 
EC 1.14.14.110
Accepted name: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase
Reaction: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one + [reduced NADPH—hemoprotein reductase] + O2 = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of benzoxazinone biosynthesis, click here
Glossary: 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one = DIBOA
2-hydroxy-2H-1,4-benzoxazin-3(4H)-one = HBOA
Other name(s): BX5 (gene name); CYP71C3 (gene name)
Systematic name: 2-hydroxy-2H-1,4-benzoxazin-3(4H)-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Bailey, B.A. and Larson, R.L. Maize microsomal benzoxazinone N-monooxygenase. Plant Physiol. 95 (1991) 792–796. [PMID: 16668055]
2.  Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925–930. [DOI] [PMID: 10385992]
[EC 1.14.14.110 created 2012 as EC 1.14.13.140, transferred 2018 to EC 1.14.14.110]
 
 
EC 1.14.14.111
Accepted name: 9β-pimara-7,15-diene oxidase
Reaction: 9β-pimara-7,15-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 9β-pimara-7,15-diene + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-ol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 9β-pimara-7,15-dien-19-ol + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-al + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) 9β-pimara-7,15-dien-19-al + O2 + [reduced NADPH—hemoprotein reductase] = 9β-pimara-7,15-dien-19-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of momilactone A biosynthesis, click here
Glossary: syn-pimara-7,15-diene = 9β-pimara-7,15-diene
Other name(s): CYP99A3; 9β-pimara-7,15-diene monooxygenase
Systematic name: 9β-pimara-7,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen 19-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the phytoalexin momilactone. It also acts similarly on 9β-stemod-13(17)-ene.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wang, Q., Hillwig, M.L. and Peters, R.J. CYP99A3: functional identification of a diterpene oxidase from the momilactone biosynthetic gene cluster in rice. Plant J. 65 (2011) 87–95. [DOI] [PMID: 21175892]
[EC 1.14.14.111 created 2012 as EC 1.14.13.144, transferred 2018 to EC 1.14.14.111]
 
 
EC 1.14.14.112
Accepted name: ent-cassa-12,15-diene 11-hydroxylase
Reaction: ent-cassa-12,15-diene + O2 + [reduced NADPH—hemoprotein reductase] = ent-11β-hydroxycassa-12,15-diene + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here
Other name(s): ent-cassadiene C11α-hydroxylase; CYP76M7
Systematic name: ent-cassa-12,15-diene,[reduced NADPH—hemoprotein reductase]:oxygen 11-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from rice (Oryza sativa) is involved in the biosynthesis of the antifungal phytocassanes.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Swaminathan, S., Morrone, D., Wang, Q., Fulton, D.B. and Peters, R.J. CYP76M7 is an ent-cassadiene C11α-hydroxylase defining a second multifunctional diterpenoid biosynthetic gene cluster in rice. Plant Cell 21 (2009) 3315–3325. [DOI] [PMID: 19825834]
[EC 1.14.14.112 created 2012 as EC 1.14.13.145, transferred 2018 to EC 1.14.14.112]
 
 
EC 1.14.14.113
Accepted name: α-humulene 10-hydroxylase
Reaction: α-humulene + O2 + [reduced NADPH—hemoprotein reductase] = 10-hydroxy-α-humulene + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of zerumbone biosynthesis, click here
Other name(s): CYP71BA1
Systematic name: α-humulene,[reduced NADPH—hemoprotein reductase]:oxygen 10-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The recommended numbering of humulene gives 10-hydroxy-α-humulene as the product rather than 8-hydroxy-α-humulene as used by the reference. See Section F: Natural Product Nomenclature.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yu, F., Okamoto, S., Harada, H., Yamasaki, K., Misawa, N. and Utsumi, R. Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. Cell. Mol. Life Sci. 68 (2011) 1033–1040. [DOI] [PMID: 20730551]
[EC 1.14.14.113 created 2012 as EC 1.14.13.150, transferred 2018 to EC 1.14.14.113]
 
 
EC 1.14.14.114
Accepted name: amorpha-4,11-diene 12-monooxygenase
Reaction: amorpha-4,11-diene + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = artemisinate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) amorpha-4,11-diene + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic alcohol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) artemisinic alcohol + O2 + [reduced NADPH—hemoprotein reductase] = artemisinic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) artemisinic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = artemisinate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of artemisinin biosynthesis, click here
Other name(s): CYP71AV1
Systematic name: amorpha-4,11-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Cloned from the plant Artemisia annua (sweet wormwood). Part of the biosynthetic pathway of artemisinin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Teoh, K.H., Polichuk, D.R., Reed, D.W., Nowak, G. and Covello, P.S. Artemisia annua L. (Asteraceae) trichome-specific cDNAs reveal CYP71AV1, a cytochrome P450 with a key role in the biosynthesis of the antimalarial sesquiterpene lactone artemisinin. FEBS Lett. 580 (2006) 1411–1416. [DOI] [PMID: 16458889]
[EC 1.14.14.114 created 2012 as EC 1.14.13.158, transferred 2018 to EC 1.14.14.114]
 
 
EC 1.14.14.115
Accepted name: 11-oxo-β-amyrin 30-oxidase
Reaction: 11-oxo-β-amyrin + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = glycyrrhetinate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) 11-oxo-β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = 30-hydroxy-11-oxo-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 30-hydroxy-11-oxo-β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = glycyrrhetaldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) glycyrrhetaldehyde + O2 + [reduced NADPH—hemoprotein reductase] = glycyrrhetinate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of glycyrrhenate biosynthesis, click here
Other name(s): CYP72A; CYP72A154; 11-oxo-β-amyrin 30-monooxygenase
Systematic name: 11-oxo-β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (30-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Glycyrrhiza uralensis (licorice) is involved in the biosynthesis of the triterpenoid saponin glycyrrhizin. The enzyme from the plant Medicago truncatula can also hydroxylate β-amyrin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Seki, H., Sawai, S., Ohyama, K., Mizutani, M., Ohnishi, T., Sudo, H., Fukushima, E.O., Akashi, T., Aoki, T., Saito, K. and Muranaka, T. Triterpene functional genomics in licorice for identification of CYP72A154 involved in the biosynthesis of glycyrrhizin. Plant Cell 23 (2011) 4112–4123. [DOI] [PMID: 22128119]
[EC 1.14.14.115 created 2013 as EC 1.14.13.173, transferred 2018 to EC 1.14.14.115]
 
 
EC 1.14.14.116
Accepted name: averantin hydroxylase
Reaction: (1) (1′S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1′S,5′S)-5′-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) (1′S)-averantin + [reduced NADPH—hemoprotein reductase] + O2 = (1′S,5′R)-5′-hydroxyaverantin + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of aflatoxin biosynthesis (part 1), click here
Glossary: averantin = 1,3,6,8-tetrahydroxy-2-[(1S)-1-hydroxyhexyl]anthracene-9,10-dione
Other name(s): AVN hydroxylase; avnA (gene name); CYP60A1
Systematic name: (1′S)-averantin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the saprophytic mold Aspergillus parasiticus. Involved in aflatoxin biosynthesis. Does not react with (1′R)-averantin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yabe, K., Matsuyama, Y., Ando, Y., Nakajima, H. and Hamasaki, T. Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic acid to averufin. Appl. Environ. Microbiol. 59 (1993) 2486–2492. [PMID: 8368836]
2.  Yu, J., Chang, P.K., Cary, J.W., Bhatnagar, D. and Cleveland, T.E. avnA, a gene encoding a cytochrome P-450 monooxygenase, is involved in the conversion of averantin to averufin in aflatoxin biosynthesis in Aspergillus parasiticus. Appl. Environ. Microbiol. 63 (1997) 1349–1356. [PMID: 9097431]
[EC 1.14.14.116 created 2013 as EC 1.14.13.174, transferred 2018 to EC 1.14.14.116]
 
 
EC 1.14.14.117
Accepted name: aflatoxin B synthase
Reaction: (1) 8-O-methylsterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B1 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
(2) 8-O-methyldihydrosterigmatocystin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = aflatoxin B2 + 2 [oxidized NADPH—hemoprotein reductase] + H2O + methanol + CO2
For diagram of aflatoxin biosynthesis (part 4), click here
Glossary: aflatoxin B1 = (6aR,9aS)-4-methoxy-2,3,6a,9a-tetrahydrocyclopenta[c]furo[3′,2′:4,5]furo[2,3-h][1]benzopyran-1,11-dione
aflatoxin B2 = (6aR,9aS)-4-methoxy-2,3,6a,8,9,9a-hexahydrocyclopenta[c]furo[3′,2′:4,5]furo[2,3-h][1]benzopyran-1,11-dione
8-O-methylsterigmatocystin = 6,8-dimethoxy-3a,12c-dihydrofuro[3′,2′:4,5]furo[2,3-c]xanthen-7-one
8-O-methyldihydrosterigmatocystin = 6,8-dimethoxy-1,2,3a,12c-tetrahydrofuro[3′,2′:4,5]furo[2,3-c]xanthen-7-one
Other name(s): ordA (gene name)
Systematic name: 8-O-methylsterigmatocystin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (aflatoxin-B forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from the mold Aspergillus parasiticus.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Bhatnagar, D., Cleveland, T.E. and Kingston, D.G. Enzymological evidence for separate pathways for aflatoxin B1 and B2 biosynthesis. Biochemistry 30 (1991) 4343–4350. [PMID: 1902378]
2.  Yu, J., Chang, P.K., Ehrlich, K.C., Cary, J.W., Montalbano, B., Dyer, J.M., Bhatnagar, D. and Cleveland, T.E. Characterization of the critical amino acids of an Aspergillus parasiticus cytochrome P-450 monooxygenase encoded by ordA that is involved in the biosynthesis of aflatoxins B1, G1, B2, and G2. Appl. Environ. Microbiol. 64 (1998) 4834–4841. [PMID: 9835571]
3.  Udwary, D.W., Casillas, L. K. and Townsend, C.A. Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a cytochrome P-450 in the final step of aflatoxin biosynthesis. J. Am. Chem. Soc. 124 (2002) 5294–5303. [DOI] [PMID: 11996570]
[EC 1.14.14.117 created 2013 as EC 1.14.13.175, transferred 2018 to EC 1.14.14.117]
 
 
EC 1.14.14.118
Accepted name: tryprostatin B 6-hydroxylase
Reaction: tryprostatin B + [reduced NADPH—hemoprotein reductase] + O2 = 6-hydroxytryprostatin B + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: tryprostatin B = (3S,8aS)-3-{[2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
6-hydroxytryprostatin B = (3S,8aS)-3-{[6-hydroxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
Other name(s): ftmC (gene name)
Systematic name: tryprostatin B,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6-hydroxytryprostatin B-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathways of several indole alkaloids such as tryprostatins, fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem. 10 (2009) 920–928. [DOI] [PMID: 19226505]
[EC 1.14.14.118 created 2013 as EC 1.14.13.176, transferred 2018 to EC 1.14.14.118]
 
 
EC 1.14.14.119
Accepted name: fumitremorgin C monooxygenase
Reaction: fumitremorgin C + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 12α,13α-dihydroxyfumitremorgin C + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
12α,13α-dihydroxyfumitremorgin = (5aR,6S,12S,14aS)-5a,6-dihydroxy-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmG (gene name)
Systematic name: fumitremorgin C,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α,13α-dihydroxyfumitremorgin C-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the indole alkaloid verruculogen.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem. 10 (2009) 920–928. [DOI] [PMID: 19226505]
[EC 1.14.14.119 created 2013 as EC 1.14.13.177, transferred 2018 to EC 1.14.14.119]
 
 
EC 1.14.14.120
Accepted name: dammarenediol 12-hydroxylase
Reaction: dammarenediol-II + [reduced NADPH—hemoprotein reductase] + O2 = protopanaxadiol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of dammarenediol II and tirucalla-7,24-dien-3β-ol biosynthesis, click here
Glossary: dammarenediol-II = dammar-24-ene-3β,20-diol
protopanaxadiol = dammar-24-ene-3β,12β,20-triol
Other name(s): protopanaxadiol synthase; CYP716A47
Systematic name: dammarenediol-II,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12β-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from ginseng (Panax ginseng). Involved in the biosynthetic pathway of ginsenosides.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Han, J.Y., Kim, H.J., Kwon, Y.S. and Choi, Y.E. The Cyt P450 enzyme CYP716A47 catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 52 (2011) 2062–2073. [DOI] [PMID: 22039120]
[EC 1.14.14.120 created 2013 as EC 1.14.13.183, transferred 2018 to EC 1.14.14.120]
 
 
EC 1.14.14.121
Accepted name: protopanaxadiol 6-hydroxylase
Reaction: protopanaxadiol + [reduced NADPH—hemoprotein reductase] + O2 = protopanaxatriol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of dammarenediol II and tirucalla-7,24-dien-3β-ol biosynthesis, click here
Glossary: protopanaxadiol = dammar-24-ene-3β,12β,20-triol
protopanaxatriol = dammar-24-ene-3β,6α,12β,20-tetrol
Other name(s): protopanaxatriol synthase; P6H; CYP716A53v2
Systematic name: protopanaxadiol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the rhizomes of ginseng (Panax ginseng). Involved in the biosynthetic pathway of ginsenosides.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yue, C.J., Zhou, X. and Zhong, J.J. Protopanaxadiol 6-hydroxylase and its role in regulating the ginsenoside heterogeneity in Panax notoginseng cells. Biotechnol. Bioeng. 100 (2008) 933–940. [DOI] [PMID: 18351680]
2.  Han, J.Y., Hwang, H.S., Choi, S.W., Kim, H.J. and Choi, Y.E. Cytochrome P450 CYP716A53v2 catalyzes the formation of protopanaxatriol from protopanaxadiol during ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 53 (2012) 1535–1545. [DOI] [PMID: 22875608]
[EC 1.14.14.121 created 2013 as EC 1.14.13.184, transferred 2018 to EC 1.14.14.121]
 
 
EC 1.14.14.122
Accepted name: oryzalexin E synthase
Reaction: ent-sandaracopimaradien-3β-ol + [reduced NADPH—hemoprotein reductase] + O2 = oryzalexin E + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of oryzalexins biosynthesis, click here
Glossary: oryzalexin E = ent-sandaracopimaradiene-3β,9α-diol = (3R,4aR,4bS,7S,10aR)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2,4b-diol
ent-sandaracopimaradien-3β-ol = (3R,4aR,4bR,7S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2-ol
Other name(s): CYP76M6
Systematic name: ent-sandaracopimaradien-3β-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (oryzalexin E forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Oryza sativa (rice). Oryzalexin E is a phytoalexin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wu, Y., Wang, Q., Hillwig, M.L. and Peters, R.J. Picking sides: distinct roles for CYP76M6 and CYP76M8 in rice oryzalexin biosynthesis. Biochem. J. 454 (2013) 209–216. [DOI] [PMID: 23795884]
[EC 1.14.14.122 created 2014 as EC 1.14.13.192, transferred 2018 to EC 1.14.14.122]
 
 
EC 1.14.14.123
Accepted name: oryzalexin D synthase
Reaction: ent-sandaracopimaradien-3β-ol + [reduced NADPH—hemoprotein reductase] + O2 = oryzalexin D + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of oryzalexins biosynthesis, click here
Glossary: oryzalexin D = ent-sandaracopimaradiene-3β,7α-diol = (3R,4aR,4bS,7S,9S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2,9-diol
ent-sandaracopimaradien-3β-ol = (3R,4aR,4bR,7S,10aS)-7-ethenyl-1,1,4a,7-tetramethyl-1,2,3,4,4a,4b,5,6,7,9,10,10a-dodecahydrophenanthren-2-ol
Other name(s): CYP76M8
Systematic name: ent-sandaracopimaradien-3β-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (oryzalexin D forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Oryza sativa (rice). Oryzalexin D is a phytoalexin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wu, Y., Wang, Q., Hillwig, M.L. and Peters, R.J. Picking sides: distinct roles for CYP76M6 and CYP76M8 in rice oryzalexin biosynthesis. Biochem. J. 454 (2013) 209–216. [DOI] [PMID: 23795884]
[EC 1.14.14.123 created 2014 as EC 1.14.13.193, transferred 2018 to EC 1.14.14.123]
 
 
EC 1.14.14.124
Accepted name: dihydromonacolin L hydroxylase
Reaction: dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin L acid + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = 3α-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 3α-hydroxy-3,5-dihydromonacolin L acid = monacolin L acid + H2O (spontaneous)
For diagram of lovastatin biosynthesis, click here
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen1yl]-3,5-dihydroxyheptanoate
monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
3α-hydroxy-3,5-dihydromonacolin L = (3R,5R)-7-[(1R,2R,3S,6R,8aR)-3-hydroxy-2,6-dimethyl-1,2,3,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovA (ambiguous)
Systematic name: dihydromonacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3α-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Treiber, L.R., Reamer, R.A., Rooney, C.S. and Ramjit, H.G. Origin of monacolin L from Aspergillus terreus cultures. J. Antibiot. (Tokyo) 42 (1989) 30–36. [PMID: 2921224]
2.  Nakamura, T., Komagata, D., Murakawa, S., Sakai, K. and Endo, A. Isolation and biosynthesis of 3α-hydroxy-3,5-dihydromonacolin L. J. Antibiot. (Tokyo) 43 (1990) 1597–1600. [PMID: 2276977]
3.  Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078–8081. [DOI] [PMID: 21495633]
[EC 1.14.14.124 created 2014 as EC 1.14.13.197, transferred 2018 to EC 1.14.14.124]
 
 
EC 1.14.14.125
Accepted name: monacolin L hydroxylase
Reaction: monacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin J acid + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of lovastatin biosynthesis, click here
Glossary: monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
Other name(s): LovA (ambiguous)
Systematic name: monacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078–8081. [DOI] [PMID: 21495633]
[EC 1.14.14.125 created 2014 as EC 1.14.13.198, transferred 2018 to EC 1.14.14.125]
 
 
EC 1.14.14.126
Accepted name: β-amyrin 28-monooxygenase
Reaction: β-amyrin + 3 O2 + 3 [reduced NADPH—hemoprotein reductase] = oleanolate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) β-amyrin + O2 + [reduced NADPH—hemoprotein reductase] = erythrodiol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) erythrodiol + O2 + [reduced NADPH—hemoprotein reductase] = oleanolic aldehyde + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) oleanolic aldehyde + O2 + [reduced NADPH—hemoprotein reductase] = oleanolate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of β-amyrin, β-seco-amyrin, 11-oxo-β-amyrin and soysapogenol biosynthesis, click here
Other name(s): CYP716A52v2; CYP716A12; CYP16A75; β-amyrin 28-oxidase
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (28-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the biosynthesis of oleanane-type triterpenoids, such as ginsenoside Ro. The enzyme from Medicago truncatula (barrel medic) (CYP716A12) can also convert α-amyrin and lupeol to ursolic acid and betulinic acid, respectively. The enzyme from Maesa lanceolata (false assegai) (CYP16A75) does not catalyse the reaction to completion, resulting in accumulation of both intermediates.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Fukushima, E.O., Seki, H., Ohyama, K., Ono, E., Umemoto, N., Mizutani, M., Saito, K. and Muranaka, T. CYP716A subfamily members are multifunctional oxidases in triterpenoid biosynthesis. Plant Cell Physiol 52 (2011) 2050–2061. [DOI] [PMID: 22039103]
2.  Han, J.Y., Kim, M.J., Ban, Y.W., Hwang, H.S. and Choi, Y.E. The involvement of β-amyrin 28-oxidase (CYP716A52v2) in oleanane-type ginsenoside biosynthesis in Panax ginseng. Plant Cell Physiol 54 (2013) 2034–2046. [DOI] [PMID: 24092881]
3.  Moses, T., Pollier, J., Faizal, A., Apers, S., Pieters, L., Thevelein, J.M., Geelen, D. and Goossens, A. Unraveling the triterpenoid saponin biosynthesis of the African shrub Maesa lanceolata. Mol. Plant 8 (2015) 122–135. [DOI] [PMID: 25578277]
[EC 1.14.14.126 created 2015 as EC 1.14.13.201, transferred 2018 to EC 1.14.14.126]
 
 
EC 1.14.14.127
Accepted name: methyl farnesoate epoxidase
Reaction: methyl (2E,6E)-farnesoate + [reduced NADPH—hemoprotein reductase] + O2 = juvenile hormone III + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of juvenile hormone biosynthesis, click here
Glossary: juvenile hormone III = methyl (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
Other name(s): CYP15A1
Systematic name: methyl (2E,6E)-farnesoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.14.128, farnesoate epoxidase) [1,2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Helvig, C., Koener, J.F., Unnithan, G.C. and Feyereisen, R. CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl farnesoate to juvenile hormone III in cockroach corpora allata. Proc. Natl. Acad. Sci. USA 101 (2004) 4024–4029. [DOI] [PMID: 15024118]
2.  Daimon, T. and Shinoda, T. Function, diversity, and application of insect juvenile hormone epoxidases (CYP15). Biotechnol. Appl. Biochem. 60 (2013) 82–91. [DOI] [PMID: 23586995]
[EC 1.14.14.127 created 2015 as EC 1.14.13.202, transferred 2018 to EC 1.14.14.127]
 
 
EC 1.14.14.128
Accepted name: farnesoate epoxidase
Reaction: (2E,6E)-farnesoate + [reduced NADPH—hemoprotein reductase] + O2 = juvenile-hormone-III carboxylate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of juvenile hormone biosynthesis, click here
Glossary: juvenile-hormone-III carboxylate = (2E,6E,10R)-10,11-epoxy-3,7,11-trimethyldodeca-2,6-dienoate
Other name(s): CYP15C1
Systematic name: (2E,6E)-farnesoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme, found in Lepidoptera (moths and butterflies), is specific for farnesoate (cf. EC 1.14.14.127, methyl farnesoate epoxidase) [1,2]. It is involved in the synthesis of juvenile hormone.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Daimon, T., Kozaki, T., Niwa, R., Kobayashi, I., Furuta, K., Namiki, T., Uchino, K., Banno, Y., Katsuma, S., Tamura, T., Mita, K., Sezutsu, H., Nakayama, M., Itoyama, K., Shimada, T. and Shinoda, T. Precocious metamorphosis in the juvenile hormone-deficient mutant of the silkworm, Bombyx mori. PLoS Genet 8:e1002486 (2012). [DOI] [PMID: 22412378]
2.  Daimon, T. and Shinoda, T. Function, diversity, and application of insect juvenile hormone epoxidases (CYP15). Biotechnol. Appl. Biochem. 60 (2013) 82–91. [DOI] [PMID: 23586995]
[EC 1.14.14.128 created 2015 as EC 1.14.13.203, transferred 2018 to EC 1.14.14.128]
 
 
EC 1.14.14.129
Accepted name: long-chain acyl-CoA ω-monooxygenase
Reaction: (1) oleoyl-CoA + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxyoleoyl-CoA + [oxidized NADPH—hemoprotein reductase] + H2O
(2) linoleoyl-CoA + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxylinoleoyl-CoA + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): long-chain acyl-CoA ω-hydroxylase; CYP86A22 (gene name); CYP52M1 (gene name)
Systematic name: long-chain acyl-CoA,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzymes from solanaceous plants are involved in the biosynthesis of stigmatic estolide, a lipid-based polyester that forms a major component of the exudate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Han, J., Clement, J.M., Li, J., King, A., Ng, S. and Jaworski, J.G. The cytochrome P450 CYP86A22 is a fatty acyl-CoA ω-hydroxylase essential for estolide synthesis in the stigma of Petunia hybrida. J. Biol. Chem. 285 (2010) 3986–3996. [DOI] [PMID: 19940120]
[EC 1.14.14.129 created 2015 as EC 1.14.13.204, transferred 2018 to EC 1.14.14.129]
 
 
EC 1.14.14.130
Accepted name: laurate 7-monooxygenase
Reaction: dodecanoate + [reduced NADPH—hemoprotein reductase] + O2 = 7-hydroxydodecanoate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: laurate = dodecanoate
Other name(s): CYP703A2 (gene name)
Systematic name: dodecanoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme is involved in the synthesis of sporopollenin - a complex polymer found at the outer layer of spores and pollen. It can also act on decanoate (C10), myristate (C14), and palmitate (C16) with lower activity. The enzyme also produces a small amount of products that are hydroxylated at neighboring positions (C-6, C-8 and C-9).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Morant, M., Jørgensen, K., Schaller, H., Pinot, F., Møller, B.L., Werck-Reichhart, D. and Bak, S. CYP703 is an ancient cytochrome P450 in land plants catalyzing in-chain hydroxylation of lauric acid to provide building blocks for sporopollenin synthesis in pollen. Plant Cell 19 (2007) 1473–1487. [DOI] [PMID: 17496121]
[EC 1.14.14.130 created 2015 as EC 1.14.13.206, transferred 2018 to EC 1.14.14.130]
 
 
EC 1.14.14.131
Accepted name: bursehernin 5′-monooxygenase
Reaction: (–)-bursehernin + [reduced NADPH—hemoprotein reductase] + O2 = (–)-5′-demethylyatein + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of podophyllotoxin biosynthesis, click here
Glossary: (–)-bursehernin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4-dimethoxyphenyl)methyl]oxolan-2-one
(–)-5′-demethylyatein = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3-hydroxy-4,5-dimethoxyphenyl)methyl]oxolan-2-one
(–)-yaetin = (3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(3,4,5-trimethoxyphenyl)methyl]oxolan-2-one
Other name(s): CYP71CU1 (gene name); bursehernin 5′-hydroxylase
Systematic name: (–)-bursehernin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum. The enzyme is involved in the biosynthetic pathway of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224–1228. [DOI] [PMID: 26359402]
[EC 1.14.14.131 created 2016 as EC 1.14.13.213, transferred 2018 to EC 1.14.14.131]
 
 
EC 1.14.14.132
Accepted name: (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase
Reaction: (–)-4′-demethyldeoxypodophyllotoxin + [reduced NADPH—hemoprotein reductase] + O2 = (–)-4′-demethylepipodophyllotoxin + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: (–)-4′-demethyldeoxypodophyllotoxin = (5R,5aR,8aR)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3′,4′:6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
(–)-4′-demethylepipodophyllotoxin = (5R,5aR,8aR,9S)-9-hydroxy-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3′,4′:6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
Other name(s): CYP82D61 (gene name)
Systematic name: (–)-deoxypodophyllotoxin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein characterized from the plant Sinopodophyllum hexandrum. The enzyme produces the direct precursor to etoposide, a potent anticancer drug. It can also act on (–)-deoxypodophyllotoxin with lower efficiency.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Lau, W. and Sattely, E.S. Six enzymes from mayapple that complete the biosynthetic pathway to the etoposide aglycone. Science 349 (2015) 1224–1228. [DOI] [PMID: 26359402]
[EC 1.14.14.132 created 2016 as EC 1.14.13.214, transferred 2018 to EC 1.14.14.132]
 
 
EC 1.14.14.133
Accepted name: 1,8-cineole 2-endo-monooxygenase
Reaction: 1,8-cineole + [reduced flavodoxin] + O2 = 2-endo-hydroxy-1,8-cineole + [oxidized flavodoxin] + H2O
For diagram of 1,8-cineole catabolism, click here
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
2-endo-hydroxy-1,8-cineole = (1R,4S,6R)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-ol
Other name(s): P450cin; CYP176A; CYP176A1
Systematic name: 1,8-cineole,[reduced flavodoxin]:oxygen oxidoreductase (2-endo-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein that uses a flavodoxin-like redox partner to reduce the heme iron. Isolated from the bacterium Citrobacter braakii, which can use 1,8-cineole as the sole source of carbon.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hawkes, D.B., Adams, G.W., Burlingame, A.L., Ortiz de Montellano, P.R. and De Voss, J.J. Cytochrome P450cin (CYP176A), isolation, expression, and characterization. J. Biol. Chem. 277 (2002) 27725–27732. [DOI] [PMID: 12016226]
2.  Meharenna, Y.T., Li, H., Hawkes, D.B., Pearson, A.G., De Voss, J. and Poulos, T.L. Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam. Biochemistry 43 (2004) 9487–9494. [DOI] [PMID: 15260491]
3.  Kimmich, N., Das, A., Sevrioukova, I., Meharenna, Y., Sligar, S.G. and Poulos, T.L. Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin. J. Biol. Chem. 282 (2007) 27006–27011. [DOI] [PMID: 17606612]
4.  Meharenna, Y.T., Slessor, K.E., Cavaignac, S.M., Poulos, T.L. and De Voss, J.J. The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin. J. Biol. Chem. 283 (2008) 10804–10812. [DOI] [PMID: 18270198]
[EC 1.14.14.133 created 2012 as EC 1.14.13.156, transferred 2018 to EC 1.14.14.133]
 
 
EC 1.14.14.134
Accepted name: β-amyrin 24-hydroxylase
Reaction: (1) β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 24-hydroxy-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(2) sophoradiol + [reduced NADPH—hemoprotein reductase] + O2 = 24-hydroxysophoradiol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of soyasapogenol biosynthesis, click here
Glossary: 24-hydroxy-β-amyrin = olean-12-ene-3β,24-diol
24-hydroxysophoradiol = soyasapogenol B
Other name(s): sophoradiol 24-hydroxylase; CYP93E1
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (24-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Found in plants and participates in the biosynthesis of soybean saponins.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Shibuya, M., Hoshino, M., Katsube, Y., Hayashi, H., Kushiro, T. and Ebizuka, Y. Identification of β-amyrin and sophoradiol 24-hydroxylase by expressed sequence tag mining and functional expression assay. FEBS J. 273 (2006) 948–959. [DOI] [PMID: 16478469]
[EC 1.14.14.134 created 2011 as EC 1.14.99.43, transferred 2018 to EC 1.14.14.134]
 
 
EC 1.14.14.135
Accepted name: glyceollin synthase
Reaction: (1) 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin II + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(2) 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin III + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(3) 4-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan + [reduced NADPH—hemoprotein reductase] + O2 = glyceollin I + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of glyceollin biosynthesis (part 2), click here
Other name(s): dimethylallyl-3,6a,9-trihydroxypterocarpan cyclase
Systematic name: 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (cyclizing)
Comments: A cytochrome P-450 (heme-thiolate) protein purified from soybean.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Welle, R. and Grisebach, H. Induction of phytoalexin synthesis in soybean: enzymatic cyclization of prenylated pterocarpans to glyceollin isomers. Arch. Biochem. Biophys. 263 (1988) 191–198. [DOI] [PMID: 3369863]
[EC 1.14.14.135 created 2004 as EC 1.14.13.85, transferred 2018 to EC 1.14.14.135]
 
 
EC 1.14.14.136
Accepted name: deoxysarpagine hydroxylase
Reaction: 10-deoxysarpagine + [reduced NADPH—hemoprotein reductase] + O2 = sarpagine + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of geissoschizine and sarpagine biosynthesis, click here
Other name(s): DOSH
Systematic name: 10-deoxysarpagine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (10-hydroxylating)
Comments: A cytohrome P-450 (heme-thiolate) protein isolated from the plant Rauvolfia serpentina.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yu, B., Ruppert, M. and Stöckigt, J. Deoxysarpagine hydroxylase — a novel enzyme closing a short side pathway of alkaloid biosynthesis in Rauvolfia. Bioorg. Med. Chem. 10 (2002) 2479–2483. [DOI] [PMID: 12057637]
[EC 1.14.14.136 created 2005 as EC 1.14.13.91, transferred 2018 to EC 1.14.14.136]
 
 
EC 1.14.14.137
Accepted name: (+)-abscisic acid 8′-hydroxylase
Reaction: (+)-abscisate + [reduced NADPH—hemoprotein reductase] + O2 = 8′-hydroxyabscisate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abscisic-acid biosynthesis, click here
Other name(s): (+)-ABA 8′-hydroxylase; ABA 8′-hydroxylase; CYP707A1 (gene name)
Systematic name: abscisate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8′-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Catalyses the first step in the oxidative degradation of abscisic acid and is considered to be the pivotal enzyme in controlling the rate of degradation of this plant hormone [1]. CO inhibits the reaction, but its effects can be reversed by the presence of blue light [1]. The 8′-hydroxyabscisate formed can be converted into (–)-phaseic acid, most probably spontaneously.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 153190-37-5
References:
1.  Cutler, A.J., Squires, T.M., Loewen, M.K. and Balsevich, J.J. Induction of (+)-abscisic acid 8′ hydroxylase by (+)-abscisic acid in cultured maize cells. J. Exp. Bot. 48 (1997) 1787–1795.
2.  Krochko, J.E., Abrams, G.D., Loewen, M.K., Abrams, S.R. and Cutler, A.J. (+)-Abscisic acid 8′-hydroxylase is a cytochrome P450 monooxygenase. Plant Physiol. 118 (1998) 849–860. [PMID: 9808729]
3.  Saito, S., Hirai, N., Matsumoto, C., Ohigashi, H., Ohta, D., Sakata, K. and Mizutani, M. Arabidopsis CYP707As encode (+)-abscisic acid 8′-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid. Plant Physiol. 134 (2004) 1439–1449. [PMID: 15064374]
[EC 1.14.14.137 created 2005 as EC 1.14.13.93, transferred 2018 EC 1.14.14.137]
 
 
EC 1.14.14.138
Accepted name: lithocholate 6β-hydroxylase
Reaction: lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = 6β-hydroxylithocholate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of the reaction of deoxycholate and related bile acids, click here
Glossary: lithocholate = 3α-hydroxy-5β-cholan-24-oate
6β-hydroxylithocholate = murideoxycholate = 3α,6β-dihydroxy-5β-cholan-24-oate
Other name(s): lithocholate 6β-monooxygenase; CYP3A10; 6β-hydroxylase; cytochrome P450 3A10; lithocholic acid 6β-hydroxylase
Systematic name: lithocholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6β-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from Mesocricetus auratus (golden hamster). Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9075-83-6
References:
1.  Teixeira, J. and Gil, G. Cloning, expression, and regulation of lithocholic acid 6β-hydroxylase. J. Biol. Chem. 266 (1991) 21030–21036. [PMID: 1840595]
2.  Chang, T.K., Teixeira, J., Gil, G. and Waxman, D.J. The lithocholic acid 6beta-hydroxylase cytochrome P-450, CYP 3A10, is an active catalyst of steroid-hormone 6β-hydroxylation. Biochem. J. 291 (1993) 429–433. [PMID: 8484723]
3.  Subramanian, A., Wang, J. and Gil, G. STAT 5 and NF-Y are involved in expression and growth hormone-mediated sexually dimorphic regulation of cytochrome P450 3A10/lithocholic acid 6β-hydroxylase. Nucleic Acids Res. 26 (1998) 2173–2178. [DOI] [PMID: 9547277]
4.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC 1.14.14.138 created 2005 as EC 1.14.13.94, transferred 2018 to EC 1.14.14.138]
 
 
EC 1.14.14.139
Accepted name: 5β-cholestane-3α,7α-diol 12α-hydroxylase
Reaction: 5β-cholestane-3α,7α-diol + [reduced NADPH—hemoprotein reductase] + O2 = 5β-cholestane-3α,7α,12α-triol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of cholesterol catabolism (rings A, B and C), click here
Other name(s): 5β-cholestane-3α,7α-diol 12α-monooxygenase; sterol 12α-hydroxylase (ambiguous); CYP8B1; cytochrome P450 8B1
Systematic name: 5β-cholestane-3α,7α-diol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals. This is the key enzyme in the biosynthesis of the bile acid cholic acid (3α,7α,12α-trihydroxy-5β-cholanoic acid). The activity of this enzyme determines the biosynthetic ratio between cholic acid and chenodeoxycholic acid [3]. The enzyme can also hydroxylate the substrate at the 25 and 26 position, but to a lesser extent [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12α-hydroxylation of 5β-cholestane-3α,7α-diol. Eur. J. Biochem. 125 (1982) 423–429. [DOI] [PMID: 6811268]
2.  Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis and metabolism of bile acids. Catalytic properties of different forms of cytochrome P-450. J. Biol. Chem. 255 (1980) 1643–1649. [PMID: 6766451]
3.  Lundell, K. and Wikvall, K. Gene structure of pig sterol 12α-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21). Biochim. Biophys. Acta 1634 (2003) 86–96. [DOI] [PMID: 14643796]
4.  del Castillo-Olivares, A. and Gil, G. α1-Fetoprotein transcription factor is required for the expression of sterol 12α -hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription. J. Biol. Chem. 275 (2000) 17793–17799. [DOI] [PMID: 10747975]
5.  Yang, Y., Zhang, M., Eggertsen, G. and Chiang, J.Y. On the mechanism of bile acid inhibition of rat sterol 12α-hydroxylase gene (CYP8B1) transcription: roles of α-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha. Biochim. Biophys. Acta 1583 (2002) 63–73. [DOI] [PMID: 12069850]
6.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC 1.14.14.139 created 2005 as EC 1.14.13.96, transferred 2018 to EC 1.14.14.139]
 
 
EC 1.14.14.140 – public review until 01 September 2018 [Last modified: 2018-08-04 12:45:47]
Transferred entry: licodione synthase. Now included with EC 1.14.14.162, flavanone 2-hydroxylase
[EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162, deleted 2018]
 
 
EC 1.14.14.141
Accepted name: psoralen synthase
Reaction: (+)-marmesin + [reduced NADPH—hemoprotein reductase] + O2 = psoralen + [oxidized NADPH—hemoprotein reductase] + acetone + 2 H2O
For diagram of reaction, click here
Glossary: (+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
psoralen = 7H-furo[3,2-g]chromen-7-one
Other name(s): CYP71AJ1
Systematic name: (+)-marmesin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This microsomal cytochrome P-450 (heme-thiolate) enzyme is rather specific for (+)-marmesin, although it can also accept 5-hydroxymarmesin to a much lesser extent. Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-Columbianetin, the angular furanocoumarin analogue of the linear furanocoumarin (+)-marmesin, acts as a competitive inhibitor even though it is not a substrate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Larbat, R., Kellner, S., Specker, S., Hehn, A., Gontier, E., Hans, J., Bourgaud, F. and Matern, U. Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis. J. Biol. Chem. 282 (2007) 542–554. [DOI] [PMID: 17068340]
[EC 1.14.14.141 created 2007 as EC 1.14.13.102, transferred 2018 to EC 1.14.14.141]
 
 
EC 1.14.14.142
Accepted name: 8-dimethylallylnaringenin 2′-hydroxylase
Reaction: sophoraflavanone B + [reduced NADPH—hemoprotein reductase] + O2 = leachianone G + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of sophoraflavanone G biosynthesis, click here
Glossary: sophoraflavanone B = (–)-(2S)-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-enyl)chroman-4-one
leachianone G = (–)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-8-(2-hydroxy-3-methylbut-2-enyl)-2-(4-hydroxyphenyl)chroman-4-one
Other name(s): 8-DMAN 2′-hydroxylase
Systematic name: sophoraflavanone-B,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2′-hydroxylating)
Comments: A membrane-bound cytochrome P-450 (heme-thiolate) protein that is associated with the endoplasmic reticulum [1,2]. This enzyme is specific for sophoraflavanone B as substrate. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone G biosynthetic pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yamamoto, H., Yatou, A. and Inoue, K. 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58 (2001) 671–676. [DOI] [PMID: 11672730]
2.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337]
[EC 1.14.14.142 created 2007 asEC 1.14.13.103, transferred 2018 to EC 1.14.14.142]
 
 
EC 1.14.14.143
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + [reduced NADPH—hemoprotein reductase] + O2 = (+)-menthofuran + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of (–)-carvone, perillyl aldehyde and pulegone biosynthesis, click here and for mechanism of reaction, click here
Other name(s): menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase
Systematic name: (+)-pulegone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (9-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan [1]. This is the second cytochrome P-450-mediated step of monoterpene metabolism in peppermint, with the other step being catalysed by EC 1.14.14.99, (S)-limonene 3-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279–286. [DOI] [PMID: 11396930]
2.  Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481–14486. [DOI] [PMID: 14623962]
[EC 1.14.14.143 created 2008 as EC 1.14.13.104, transferred 2018 to EC 1.14.14.143]
 
 
EC 1.14.14.144
Accepted name: abieta-7,13-diene hydroxylase
Reaction: abieta-7,13-diene + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-ol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here
Glossary: abieta-7,13-diene = (4aS,4bR,10aS)-7-isopropyl-1,1,4a-trimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene
abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
Other name(s): abietadiene hydroxylase (ambiguous)
Systematic name: abieta-7,13-diene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). Activity is induced by wounding of the plant tissue [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [DOI] [PMID: 8311462]
2.  Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380]
[EC 1.14.14.144 created 2009 as EC 1.14.13.108, modified 2012, transferred 2018 to EC 1.14.14.144]
 
 
EC 1.14.14.145
Accepted name: abieta-7,13-dien-18-ol hydroxylase
Reaction: abieta-7,13-dien-18-ol + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = abieta-7,13-dien-18-oate + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) abieta-7,13-dien-18-ol + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18,18-diol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) abieta-7,13-dien-18,18-diol = abieta-7,13-dien-18-al + H2O (spontaneous)
(1c) abieta-7,13-dien-18-al + [reduced NADPH—hemoprotein reductase] + O2 = abieta-7,13-dien-18-oate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of abietadiene, abietate, isopimaradiene, labdadienol and sclareol biosynthesis, click here
Glossary: abieta-7,13-dien-18-ol = ((1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthren-1-yl)methanol
abieta-7,13-dien-18-al = (1R,4aR,4bR,10aR)-7-isopropyl-1,4a-dimethyl-1,2,3,4,4a,4b,5,6,10,10a-decahydrophenanthrene-1-carbaldehyde
Other name(s): CYP720B1; PtAO; abietadienol hydroxylase (ambiguous)
Systematic name: abieta-7,13-dien-18-ol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine) [1], and the gene encoding the enzyme has been identified in Pinus taeda (loblolly pine) [3]. The recombinant enzyme catalyses the oxidation of multiple diterpene alcohol and aldehydes, including levopimaradienol, isopimara-7,15-dienol, isopimara-7,15-dienal, dehydroabietadienol and dehydroabietadienal. It is not able to oxidize abietadiene.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Funk, C. and Croteau, R. Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis. Arch. Biochem. Biophys. 308 (1994) 258–266. [DOI] [PMID: 8311462]
2.  Funk, C., Lewinsohn, E., Vogel, B.S., Steele, C.L. and Croteau, R. Regulation of oleoresinosis in grand fir (Abies grandis) (coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding). Plant Physiol. 106 (1994) 999–1005. [PMID: 12232380]
3.  Ro, D.K., Arimura, G., Lau, S.Y., Piers, E. and Bohlmann, J. Loblolly pine abietadienol/abietadienal oxidase PtAO (CYP720B1) is a multifunctional, multisubstrate cytochrome P450 monooxygenase. Proc. Natl. Acad. Sci. USA 102 (2005) 8060–8065. [DOI] [PMID: 15911762]
[EC 1.14.14.145 created 2009 as EC 1.14.13.109, modified 2012, transferred 2018 to EC 1.14.14.145]
 
 
EC 1.14.14.146
Accepted name: geranylgeraniol 18-hydroxylase
Reaction: geranylgeraniol + [reduced NADPH—hemoprotein reductase] + O2 = 18-hydroxygeranylgeraniol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of acyclic diterpenoid biosynthesis, click here
Glossary: plaunotol = 18-hydroxygeranylgeraniol
Other name(s): GGOH-18-hydroxylase
Systematic name: geranylgeraniol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (18-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the plant Croton sublyratus.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Tansakul, P. and De-Eknamkul, W. Geranylgeraniol-18-hydroxylase: the last enzyme in the plaunotol biosynthetic pathway in Croton sublyratus. Phytochemistry 47 (1998) 1241–1246.
[EC 1.14.14.146 created 2009 as EC 1.14.13.110, transferred 2018 to EC 1.14.14.146]
 
 
EC 1.14.14.147
Accepted name: 3-epi-6-deoxocathasterone 23-monooxygenase
Reaction: (1) 3-epi-6-deoxocathasterone + [reduced NADPH—hemoprotein reductase] + O2 = 6-deoxotyphasterol + [oxidized NADPH—hemoprotein reductase] + H2O
(2) (22S,24R)-22-hydroxy-5α-ergostan-3-one + [reduced NADPH—hemoprotein reductase] + O2 = 3-dehydro-6-deoxoteasterone + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): cytochrome P450 90C1; CYP90D1; CYP90C1
Systematic name: 3-epi-6-deoxocathasterone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-23-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in brassinosteroid biosynthesis. C-23 hydroxylation shortcuts bypass campestanol, 6-deoxocathasterone, and 6-deoxoteasterone and lead directly from (22S,24R)-22-hydroxy-5α-ergostan-3-one and 3-epi-6-deoxocathasterone to 3-dehydro-6-deoxoteasterone and 6-deoxotyphasterol [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ohnishi, T., Szatmari, A.M., Watanabe, B., Fujita, S., Bancos, S., Koncz, C., Lafos, M., Shibata, K., Yokota, T., Sakata, K., Szekeres, M. and Mizutani, M. C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel shortcut in brassinosteroid biosynthesis. Plant Cell 18 (2006) 3275–3288. [DOI] [PMID: 17138693]
[EC 1.14.14.147 created 2010 as EC 1.14.13.112, transferred 2018 to EC 1.14.14.147]
 
 
EC 1.14.14.148
Accepted name: angelicin synthase
Reaction: (+)-columbianetin + [reduced NADPH—hemoprotein reductase] + O2 = angelicin + [oxidized NADPH—hemoprotein reductase] + acetone + 2 H2O
For diagram of psoralen biosynthesis, click here
Other name(s): CYP71AJ4 (gene name)
Systematic name: (+)-columbianetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This cytochrome P-450 (heme-thiolate) enzyme from wild parsnip is involved in the formation of angular furanocoumarins. Attacks its substrate by syn-elimination of hydrogen from C-3′.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Larbat, R., Hehn, A., Hans, J., Schneider, S., Jugde, H., Schneider, B., Matern, U. and Bourgaud, F. Isolation and functional characterization of CYP71AJ4 encoding for the first P450 monooxygenase of angular furanocoumarin biosynthesis. J. Biol. Chem. 284 (2009) 4776–4785. [DOI] [PMID: 19098286]
[EC 1.14.14.148 created 2010 as EC 1.14.13.115, transferred 2018 to EC 1.14.14.148]
 
 
EC 1.14.14.149
Accepted name: 5-epiaristolochene 1,3-dihydroxylase
Reaction: 5-epiaristolochene + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = capsidiol + 2 [oxidized NADPH—hemoprotein reductase] + 2 H2O
click here
Other name(s): 5-epi-aristolochene 1,3-dihydroxylase; EAH; CYP71D20
Systematic name: 5-epiaristolochene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (1- and 3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Kinetic studies suggest that 1β-hydroxyepiaristolochene is mainly formed first followed by hydroxylation at C-3. However the reverse order via 3α-hydroxyepiaristolochene does occur.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ralston, L., Kwon, S.T., Schoenbeck, M., Ralston, J., Schenk, D.J., Coates, R.M. and Chappell, J. Cloning, heterologous expression, and functional characterization of 5-epi-aristolochene-1,3-dihydroxylase from tobacco (Nicotiana tabacum). Arch. Biochem. Biophys. 393 (2001) 222–235. [DOI] [PMID: 11556809]
2.  Takahashi, S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Kinetic and molecular analysis of 5-epiaristolochene 1,3-dihydroxylase, a cytochrome P450 enzyme catalyzing successive hydroxylations of sesquiterpenes. J. Biol. Chem. 280 (2005) 3686–3696. [DOI] [PMID: 15522862]
[EC 1.14.14.149 created 2011 as EC 1.14.13.119, transferred 2018 to EC 1.14.14.149]
 
 
EC 1.14.14.150
Accepted name: costunolide synthase
Reaction: germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = (+)-costunolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) germacra-1(10),4,11(13)-trien-12-oate + [reduced NADPH—hemoprotein reductase] + O2 = 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate = (+)-costunolide + H2O (spontaneous)
click here
Other name(s): CYP71BL2
Systematic name: germacra-1(10),4,11(13)-trien-12-oate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from chicory plants. The enzyme hydroxylates carbon C-6 of germacra-1(10),4,11(13)-trien-12-oate to give 6α-hydroxygermacra-1(10),4,11(13)-trien-12-oate, which spontaneously cyclises to form the lactone ring.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  de Kraker, J.W., Franssen, M.C., Joerink, M., de Groot, A. and Bouwmeester, H.J. Biosynthesis of costunolide, dihydrocostunolide, and leucodin. Demonstration of cytochrome p450-catalyzed formation of the lactone ring present in sesquiterpene lactones of chicory. Plant Physiol. 129 (2002) 257–268. [DOI] [PMID: 12011356]
[EC 1.14.14.150 created 2011 as EC 1.14.13.120, transferred 2018 to EC 1.14.14.150]
 
 
EC 1.14.14.151
Accepted name: premnaspirodiene oxygenase
Reaction: (–)-vetispiradiene + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = solavetivone + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) (–)-vetispiradiene + [reduced NADPH—hemoprotein reductase] + O2 = solavetivol + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) solavetivol + [reduced NADPH—hemoprotein reductase] + O2 = solavetivone + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of solavetivone biosynthesis, click here
Glossary: (–)-premnaspirodiene = (–)-vetispiradiene
Other name(s): HPO; Hyoscymus muticus premnaspirodiene oxygenase; CYP71D55
Systematic name: (–)-vetispiradiene,[reduced NADPH—hemoprotein reductase]:oxygen 2α-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plant Hyoscymus muticus also hydroxylates valencene at C-2 to give the α-hydroxy compound, nootkatol, and this is converted into nootkatone. 5-Epiaristolochene and epieremophilene are hydroxylated at C-2 to give a 2β-hydroxy derivatives that are not oxidized further.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Takahashi, S., Yeo, Y.S., Zhao, Y., O'Maille, P.E., Greenhagen, B.T., Noel, J.P., Coates, R.M. and Chappell, J. Functional characterization of premnaspirodiene oxygenase, a cytochrome P450 catalyzing regio- and stereo-specific hydroxylations of diverse sesquiterpene substrates. J. Biol. Chem. 282 (2007) 31744–31754. [DOI] [PMID: 17715131]
[EC 1.14.14.151 created 2011 as EC 1.14.13.121, transferred 2018 to EC 1.14.14.151]
 
 
EC 1.14.14.152
Accepted name: β-amyrin 11-oxidase
Reaction: β-amyrin + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = 11-oxo-β-amyrin + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 11α-hydroxy-β-amyrin + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 11α-hydroxy-β-amyrin + [reduced NADPH—hemoprotein reductase] + O2 = 11-oxo-β-amyrin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of glycyrrhenate biosynthesis, click here
Other name(s): CYP88D6
Systematic name: β-amyrin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Glycyrrhiza uralensis (Chinese licorice) that participates in the glycyrrhizin biosynthesis pathway. The enzyme is also able to oxidize 30-hydroxy-β-amyrin to 11α,30-dihydroxy-β-amyrin but this is not thought to be part of glycyrrhizin biosynthesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Seki, H., Ohyama, K., Sawai, S., Mizutani, M., Ohnishi, T., Sudo, H., Akashi, T., Aoki, T., Saito, K. and Muranaka, T. Licorice β-amyrin 11-oxidase, a cytochrome P450 with a key role in the biosynthesis of the triterpene sweetener glycyrrhizin. Proc. Natl. Acad. Sci. USA 105 (2008) 14204–14209. [DOI] [PMID: 18779566]
[EC 1.14.14.152 created 2011 as EC 1.14.13.134, transferred 2018 to EC 1.14.14.152]
 
 
EC 1.14.14.153
Accepted name: indole-2-monooxygenase
Reaction: indole + [reduced NADPH—hemoprotein reductase] + O2 = indolin-2-one + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of benzoxazinone biosynthesis, click here
Other name(s): BX2 (gene name); CYP71C4 (gene name)
Systematic name: indole,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696–699. [DOI] [PMID: 9235894]
2.  Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925–930. [DOI] [PMID: 10385992]
[EC 1.14.14.153 created 2012 as EC 1.14.13.137, transferred 2018 to EC 1.14.14.153]
 
 
EC 1.14.14.154
Accepted name: sterol 14α-demethylase
Reaction: a 14α-methylsteroid + 3 [reduced NADPH—hemoprotein reductase] + 3 O2 = a Δ14-steroid + formate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H2O (overall reaction)
(1a) a 14α-methylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-hydroxymethylsteroid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) a 14α-hydroxysteroid + [reduced NADPH—hemoprotein reductase] + O2 = a 14α-formylsteroid + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(1c) a 14α-formylsteroid + [reduced NADPH—hemoprotein reductase] + O2 = a Δ14-steroid + formate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of sterol ring B, C, D modification, click here
Glossary: obtusifoliol = 4α,14α-dimethyl-5α-ergosta-8,24(28)-dien-3β-ol or 4α,14α-dimethyl-24-methylene-5α-cholesta-8-en-3β-ol
Other name(s): obtusufoliol 14-demethylase; lanosterol 14-demethylase; lanosterol 14α-demethylase; sterol 14-demethylase; CYP51
Systematic name: sterol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (14-methyl cleaving)
Comments: This cytochrome P-450 (heme-thiolate) enzyme acts on a range of steroids with a 14α-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses a hydroxylation and a reduction of the 14α-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 60063-87-8
References:
1.  Alexander, K., Akhtar, M., Boar, R.B., McGhie, J.F. and Barton, D.H.R. The removal of the 32-carbon atom as formic acid in cholesterol biosynthesis. J. Chem. Soc. Chem. Commun. (1972) 383–385.
2.  Aoyama, Y. and Yoshida, Y. Different substrate specificities of lanosterol 14α-demethylase (P-45014DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol. Biochem. Biophys. Res. Commun. 178 (1991) 1064–1071. [DOI] [PMID: 1872829]
3.  Aoyama, Y. and Yoshida, Y. The 4β-methyl group of substrate does not affect the activity of lanosterol 14α-demethylase (P45014DM) of yeast: differences between the substrate recognition by yeast and plant sterol 14α-demethylases. Biochem. Biophys. Res. Commun. 183 (1992) 1266–1272. [DOI] [PMID: 1567403]
4.  Bak, S., Kahn, R.A., Olsen, C.E. and Halkier, B.A. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11 (1997) 191–201. [DOI] [PMID: 9076987]
[EC 1.14.14.154 created 2001 as EC 1.14.13.70, modified 2013, transferred 2018 EC 1.14.14.154]
 
 
EC 1.14.14.155
Accepted name: 3,6-diketocamphane 1,2-monooxygenase
Reaction: (–)-bornane-2,5-dione + O2 + FMNH2 = (–)-5-oxo-1,2-campholide + FMN + H2O
Glossary: (–)-bornane-2,5-dione = 3,6-diketocamphane
Other name(s): 3,6-diketocamphane lactonizing enzyme; 3,6-DKCMO
Systematic name: (–)-bornane-2,5-dione,FMNH2:oxygen oxidoreductase (1,2-lactonizing)
Comments: A Baeyer-Villiger monooxygenase isolated from camphor-grown strains of Pseudomonas putida and encoded on the cam plasmid. Involved in the degradation of (–)-camphor. Requires a dedicated NADH—FMN reductase [cf. EC 1.5.1.42, FMN reductase (NADH)] [1,2]. The product spontaneously converts to [(1R)-2,2,3-trimethyl-5-oxocyclopent-3-enyl]acetate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD
References:
1.  Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y. and Lau, P.C. Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79 (2013) 3282–3293. [PMID: 23524667]
2.  Isupov, M.N., Schroder, E., Gibson, R.P., Beecher, J., Donadio, G., Saneei, V., Dcunha, S.A., McGhie, E.J., Sayer, C., Davenport, C.F., Lau, P.C., Hasegawa, Y., Iwaki, H., Kadow, M., Balke, K., Bornscheuer, U.T., Bourenkov, G. and Littlechild, J.A. The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 2344–2353. [PMID: 26527149]
[EC 1.14.14.155 created 2018]
 
 
EC 1.14.14.156
Accepted name: tryptophan N-monooxygenase
Reaction: L-tryptophan + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-indol-3-ylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) N-hydroxy-L-tryptophan + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-tryptophan + [oxidized NADPH—hemoprotein reductase] + H2O
(1c) N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O
Other name(s): tryptophan N-hydroxylase; CYP79B1; CYP79B2; CYP79B3
Systematic name: L-tryptophan,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein from the plant Arabidopsis thaliana. This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Mikkelsen, M.D., Hansen, C.H., Wittstock, U. and Halkier, B.A. Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid. J. Biol. Chem. 275 (2000) 33712–33717. [DOI] [PMID: 10922360]
2.  Hull, A.K., Vij, R. and Celenza, J.L. Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 2379–2384. [DOI] [PMID: 10681464]
3.  Zhao, Y., Hull, A.K., Gupta, N.R., Goss, K.A., Alonso, J., Ecker, J.R., Normanly, J., Chory, J. and Celenza, J.L. Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3. Genes Dev. 16 (2002) 3100–3112. [DOI] [PMID: 12464638]
4.  Naur, P., Hansen, C.H., Bak, S., Hansen, B.G., Jensen, N.B., Nielsen, H.L. and Halkier, B.A. CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime. Arch. Biochem. Biophys. 409 (2003) 235–241. [DOI] [PMID: 12464264]
[EC 1.14.14.156 created 2011 as EC 1.14.13.125, transferred 2018 to EC 1.14.14.156]
 
 
EC 1.14.14.157
Accepted name: indolin-2-one monooxygenase
Reaction: indolin-2-one + [reduced NADPH—hemoprotein reductase] + O2 = 3-hydroxyindolin-2-one + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of benzoxazinone biosynthesis, click here
Other name(s): BX3 (gene name); CYP71C2 (gene name)
Systematic name: indolin-2-one,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme is involved in the biosynthesis of protective and allelophatic benzoxazinoids in some plants, most commonly from the family of Poaceae (grasses).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Frey, M., Chomet, P., Glawischnig, E., Stettner, C., Grün, S., Winklmair, A., Eisenreich, W., Bacher, A., Meeley, R.B., Briggs, S.P., Simcox, K. and Gierl, A. Analysis of a chemical plant defense mechanism in grasses. Science 277 (1997) 696–699. [DOI] [PMID: 9235894]
2.  Glawischnig, E., Grun, S., Frey, M. and Gierl, A. Cytochrome P450 monooxygenases of DIBOA biosynthesis: specificity and conservation among grasses. Phytochemistry 50 (1999) 925–930. [DOI] [PMID: 10385992]
[EC 1.14.14.157 created 2012 as EC 1.14.13.138, transferred 2018 to EC 1.14.14.157]
 
 
EC 1.14.14.158
Accepted name: carotenoid ε hydroxylase
Reaction: (1) α-carotene + [reduced NADPH-hemoprotein reductase] + O2 = α-cryptoxanthin + [oxidized NADPH-hemoprotein reductase] + H2O
(2) zeinoxanthin + [reduced NADPH-hemoprotein reductase] + O2 = lutein + [oxidized NADPH-hemoprotein reductase] + H2O
For diagram of lutein biosynthesis, click here
Other name(s): CYP97C1; LUT1; CYP97C; carotene ε-monooxygenase
Systematic name: α-carotene,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Pogson, B., McDonald, K.A., Truong, M., Britton, G. and DellaPenna, D. Arabidopsis carotenoid mutants demonstrate that lutein is not essential for photosynthesis in higher plants. Plant Cell 8 (1996) 1627–1639. [DOI] [PMID: 8837513]
2.  Tian, L., Musetti, V., Kim, J., Magallanes-Lundback, M. and DellaPenna, D. The Arabidopsis LUT1 locus encodes a member of the cytochrome P450 family that is required for carotenoid ε-ring hydroxylation activity. Proc. Natl. Acad. Sci. USA 101 (2004) 402–407. [DOI] [PMID: 14709673]
3.  Stigliani, A.L., Giorio, G. and D'Ambrosio, C. Characterization of P450 carotenoid β- and ε-hydroxylases of tomato and transcriptional regulation of xanthophyll biosynthesis in root, leaf, petal and fruit. Plant Cell Physiol 52 (2011) 851–865. [PMID: 21450689]
4.  Chang, S., Berman, J., Sheng, Y., Wang, Y., Capell, T., Shi, L., Ni, X., Sandmann, G., Christou, P. and Zhu, C. Cloning and functional characterization of the maize (Zea mays L.) carotenoid ε hydroxylase gene. PLoS One 10:e0128758 (2015). [PMID: 26030746]
5.  Reddy, C.S., Lee, S.H., Yoon, J.S., Kim, J.K., Lee, S.W., Hur, M., Koo, S.C., Meilan, J., Lee, W.M., Jang, J.K., Hur, Y., Park, S.U. and Kim, A.YB. Molecular cloning and characterization of carotenoid pathway genes and carotenoid content in Ixeris dentata var. albiflora. Molecules 22 (2017) . [DOI] [PMID: 28858245]
[EC 1.14.14.158 created 2011 as EC 1.14.99.45, transferred 2018 to EC 1.14.14.158]
 
 
EC 1.14.15.31
Accepted name: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
Reaction: 2-hydroxy-5-methyl-1-naphthoate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 2,7-dihydroxy-5-methyl-1-naphthoate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of neocarzinostatin biosynthesis, click here
Other name(s): NcsB3
Systematic name: 2-hydroxy-5-methyl-1-naphthoate,reduced ferredoxin:oxygen oxidoreductase (7-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hang, V.T.T., Oh, T.J., Yamaguchi, T. and Sohng, J.K. In vivo characterization of NcsB3 to establish the complete biosynthesis of the naphthoic acid moiety of the neocarzinostatin chromophore. FEMS Microbiol. Lett. 311 (2010) 119–125. [DOI] [PMID: 20735485]
[EC 1.14.15.31 created 2014 as EC 1.14.99.49, transferred 2018 to EC 1.14.15.31]
 
 
EC 1.14.15.32
Accepted name: pentalenene oxygenase
Reaction: pentalenene + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = pentalen-13-al + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O (overall reaction)
(1a) pentalenene + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-ol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1b) pentalen-13-ol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pentalen-13-al + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of humulene-based sequiterpenoid biosynthesis, click here
Other name(s): PtlI
Systematic name: pentalenene,reduced ferredoxin:oxygen 13-oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein found in the bacterium Streptomyces avermitilis. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Quaderer, R., Omura, S., Ikeda, H. and Cane, D.E. Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilis. J. Am. Chem. Soc. 128 (2006) 13036–13037. [DOI] [PMID: 17017767]
[EC 1.14.15.32 created 2011 as EC 1.14.13.133, transferred 2018 to EC 1.14.15.32]
 
 
EC 1.14.15.33
Accepted name: pikromycin synthase
Reaction: (1) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = pikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(2) narbomycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neopikromycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(3) narbomycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novapikromyin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(4) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = methymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(5) 10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = neomethymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(6) 10-deoxymethymycin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + 2 O2 = novamethymycin + 4 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of pikromycin biosynthesis, click here
Other name(s): PikC; CYP107L1
Systematic name: narbomycin,reduced ferredoxin:oxygen oxidoreductase (pikromycin-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthesis of a number of bacterial macrolide antibiotics containing a desosamine glycoside unit. With narbomycin it hydroxylates at either C-12 to give pikromycin or C-14 to give neopikromycin or both positions to give narvopikromycin. With 10-deoxymethymycin it hydroxylates at either C-10 to give methymycin or C-12 to give neomethymycin or both positions to give novamethymycin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Xue, Y., Wilson, D., Zhao, L., Liu Hw and Sherman, D.H. Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae. Chem. Biol. 5 (1998) 661–667. [DOI] [PMID: 9831532]
2.  Sherman, D.H., Li, S., Yermalitskaya, L.V., Kim, Y., Smith, J.A., Waterman, M.R. and Podust, L.M. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J. Biol. Chem. 281 (2006) 26289–26297. [DOI] [PMID: 16825192]
3.  Li, S., Ouellet, H., Sherman, D.H. and Podust, L.M. Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae. J. Biol. Chem. 284 (2009) 5723–5730. [DOI] [PMID: 19124459]
[EC 1.14.15.33 created 2014 as EC 1.14.13.185, transferred 2018 to EC 1.14.15.33]
 
 
EC 1.14.15.34
Accepted name: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase
Reaction: 20-oxo-5-O-β-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 5-O-β-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of tylosin biosynthesis, click here
Glossary: tylactone = (4R,5S,6S,7S,9R,11E,13E,15S,16R)-7,16-diethyl-4,6-dihydroxy-5,9,13,15-tetramethyl-1-oxacyclohexadeca-11,13-diene-2,10-dione
α-D-mycaminose = 3-dimethylamino-3,6-dideoxy-α-D-glucopyranose
tylonolide = 2-[(4R,5S,6S,7R,9R,11E,13E,15R,16R)-16-ethyl-4,6-dihydroxy-15-(hydroxymethyl)-5,9,13-trimethyl-2,10-dioxo-1-oxacyclohexadeca-11,13-dien-7-yl]acetaldehyde
Other name(s): tylH1 (gene name)
Systematic name: 20-oxo-5-O-β-mycaminosyltylactone,reduced ferredoxin:oxygen oxidoreductase (23-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. Involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Baltz, R.H. and Seno, E.T. Properties of Streptomyces fradiae mutants blocked in biosynthesis of the macrolide antibiotic tylosin. Antimicrob. Agents Chemother. 20 (1981) 214–225. [PMID: 7283418]
2.  Reeves, C.D., Ward, S.L., Revill, W.P., Suzuki, H., Marcus, M., Petrakovsky, O.V., Marquez, S., Fu, H., Dong, S.D. and Katz, L. Production of hybrid 16-membered macrolides by expressing combinations of polyketide synthase genes in engineered Streptomyces fradiae hosts. Chem. Biol. 11 (2004) 1465–1472. [DOI] [PMID: 15489173]
[EC 1.14.15.34 created 2014 as EC 1.14.13.186, transferred 2018 to EC 1.14.15.34]
 
 
EC 1.14.15.35
Accepted name: 6-deoxyerythronolide B hydroxylase
Reaction: 6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
For diagram of erythromycin biosynthesis, click here
Other name(s): DEB hydroxylase; eryF (gene name); P450(eryF); CYP107A1
Systematic name: 6-deoxyerythronolide-B,reduced ferredoxin:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea. The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Weber, J.M., Leung, J.O., Swanson, S.J., Idler, K.B. and McAlpine, J.B. An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea. Science 252 (1991) 114–117. [DOI] [PMID: 2011746]
2.  Shafiee, A. and Hutchinson, C.R. Macrolide antibiotic biosynthesis: isolation and properties of two forms of 6-deoxyerythronolide B hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus). Biochemistry 26 (1987) 6204–6210. [PMID: 2446657]
3.  Cupp-Vickery, J.R., Li, H. and Poulos, T.L. Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF. Proteins: Struct., Funct., Bioinf. 20 (1994) 197–201. [DOI] [PMID: 7846029]
4.  Nagano, S., Cupp-Vickery, J.R. and Poulos, T.L. Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF. J. Biol. Chem. 280 (2005) 22102–22107. [DOI] [PMID: 15824115]
[EC 1.14.15.35 created 2014 as EC 1.14.13.188, transferred 2018 to EC 1.14.15.35]
 
 
EC 1.14.19.62
Accepted name: secologanin synthase
Reaction: loganin + [reduced NADPH—hemoprotein reductase] + O2 = secologanin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of secologanin biosynthesis, click here
Systematic name: loganin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ring-cleaving)
Comments: A cytochrome P-450 (heme-thiolate) protein. Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 258339-71-8
References:
1.  Yamamoto, H., Katano, N., Ooi, Y. and Inoue, K. Transformation of loganin and 7-deoxyloganin into secologanin by Lonicera japonica cell suspension cultures. Phytochemistry 50 (1999) 417–422.
2.  Yamamoto, H., Katano, N., Ooi, A. and Inoue, K. Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P-450. Phytochemistry 53 (2000) 7–12. [DOI] [PMID: 10656401]
3.  Irmler, S., Schroder, G., St-Pierre, B., Crouch, N.P., Hotze, M., Schmidt, J., Strack, D., Matern, U. and Schroder, J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P-450 CYP72A1 as secologanin synthase. Plant J. 24 (2000) 797–804. [DOI] [PMID: 11135113]
[EC 1.14.19.62 created 2002 as EC 1.3.3.9, transferred 2018 to EC 1.14.19.62]
 
 
EC 1.14.19.63
Accepted name: pseudobaptigenin synthase
Reaction: (1) calycosin + [reduced NADPH—hemoprotein reductase] + O2 = pseudobaptigenin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
(2) pratensein + [reduced NADPH-hemoprotein reductase] + O2 = 5-hydroxypseudobaptigenin + [oxidized NADPH—hemoprotein reductase] + 2 H2O
Glossary: calycosin = 3′-hydroxyformononetin
pratensein = 3′-hydroxybiochanin A
Systematic name: calycosin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A cytochrome P-450 (heme-thiolate) enzyme catalysing an oxidative reaction that does not incorporate oxygen into the product. Catalyses a step in the biosynthesis of (–)-maackiain, the main pterocarpan phytoalexin in chickpea (Cicer arietinum).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Clemens S., Barz W. Cytochrome P450-dependent methylenedioxy bridge formation in Cicer arietinum. Phytochemistry 41 (1996) 457–460.
[EC 1.14.19.63 created 2011 as EC 1.14.21.8, transferred 2018 to EC 1.14.19.63]
 
 
EC 1.14.19.64
Accepted name: (S)-stylopine synthase
Reaction: (S)-cheilanthifoline + [reduced NADPH—hemoprotein reductase] + O2 = (S)-stylopine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of stylopine biosynthesis, click here
Other name(s): (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-cheilanthifoline,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 138791-29-4
References:
1.  Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953–2961.
[EC 1.14.19.64 created 1999 as EC 1.1.3.32, transferred 2002 to EC 1.14.21.1, transferred 2018 to EC 1.14.19.64]
 
 
EC 1.14.19.65
Accepted name: (S)-cheilanthifoline synthase
Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-cheilanthifoline + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of stylopine biosynthesis, click here
Other name(s): CYP719A14 (gene name); (S)-scoulerine oxidase (methylenedioxy-bridge-forming) (ambiguous)
Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-cheilanthifoline-forming]
Comments: A cytochrome P-450 (heme-thiolate) protein catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline by the oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine. cf. EC 1.14.19.73, (S)-nandinine synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-nandinine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 138791-27-2
References:
1.  Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953–2961.
2.  Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186–193. [DOI] [PMID: 21094631]
[EC 1.14.19.65 created 1999 as EC 1.1.3.33, transferred 2002 to EC 1.14.21.2, modified 2016, transferred 2018 to EC 1.14.19.65]
 
 
EC 1.14.19.66
Accepted name: berbamunine synthase
Reaction: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + [reduced NADPH—hemoprotein reductase] + O2 = berbamunine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of reaction, click here
Other name(s): (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Systematic name: (S)-N-methylcoclaurine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-O phenol-coupling)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 144941-42-4
References:
1.  Stadler, R. and Zenk, M.H. The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolifera plant cell cultures. J. Biol. Chem. 268 (1993) 823–831. [PMID: 8380416]
[EC 1.14.19.66 created 1999 as EC 1.1.3.34, transferred 2002 to EC 1.14.21.3, transferred 2018 to EC 1.14.19.66]
 
 
EC 1.14.19.67
Accepted name: salutaridine synthase
Reaction: (R)-reticuline + [reduced NADPH—hemoprotein reductase] + O2 = salutaridine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of thebaine biosynthesis, click here
Other name(s): (R)-reticuline oxidase (C-C phenol-coupling)
Systematic name: (R)-reticuline,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (C-C phenol-coupling)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 149433-84-1
References:
1.  Gerady, R. and Zenk, M.H. Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum. Phytochemistry 32 (1993) 79–86.
[EC 1.14.19.67 created 1999 as EC 1.1.3.35, transferred 2002 to EC 1.14.21.4, transferred 2018 to EC 1.14.19.67]
 
 
EC 1.14.19.68
Accepted name: (S)-canadine synthase
Reaction: (S)-tetrahydrocolumbamine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-canadine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of canadine biosynthesis, click here
Other name(s): (S)-tetrahydroberberine synthase; (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming); CYP719A (gene name)
Systematic name: (S)-tetrahydrocolumbamine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein found in plants. The enzyme catalyses an oxidative reaction that does not incorporate oxygen into the product. Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 114308-22-4
References:
1.  Rueffer, M. and Zenk, M.H. Canadine synthase from Thalictrum tuberosum cell cultures catalyses the formation of the methylenedioxy bridge in berberine synthesis. Phytochemistry 36 (1994) 1219–1223.
2.  Ikezawa, N., Tanaka, M., Nagayoshi, M., Shinkyo, R., Sakaki, T., Inouye, K. and Sato, F. Molecular cloning and characterization of CYP719, a methylenedioxy bridge-forming enzyme that belongs to a novel P450 family, from cultured Coptis japonica cells. J. Biol. Chem 278 (2003) 38557–38565. [PMID: 12732624]
3.  Dang, T.T. and Facchini, P.J. Cloning and characterization of canadine synthase involved in noscapine biosynthesis in opium poppy. FEBS Lett. 588 (2014) 198–204. [PMID: 24316226]
[EC 1.14.19.68 created 1999 as EC 1.1.3.36, transferred 2002 to EC 1.14.21.5, transferred 2018 to EC 1.14.19.68]
 
 
EC 1.14.19.69
Accepted name: biflaviolin synthase
Reaction: (1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,3′-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 3,8′-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of flaviolin metabolism, click here
Glossary: flaviolin = 4,5,7-trihydroxynaphthalene-1,2-dione
3,3′-biflaviolin = 3,3′,6,6′,8,8′-hexahydroxy-2,2′-binaphthalene-1,1′,4,4′-tetraone
3,8′-biflaviolin = 2,3′,4,6′,7,8′-hexahydroxy-1,2′-binaphthalene-1′,4′,5,8-tetraone
Other name(s): CYP158A2 (gene name); cytochrome P450 158A2
Systematic name: flaviolin,reduced ferredoxin:oxygen oxidoreductase
Comments: This cytochrome-P-450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyses a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product [1,3]. The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zhao, B., Guengerich, F.P., Bellamine, A., Lamb, D.C., Izumikawa, M., Lei, L., Podust, L.M., Sundaramoorthy, M., Kalaitzis, J.A., Reddy, L.M., Kelly, S.L., Moore, B.S., Stec, D., Voehler, M., Falck, J.R., Shimada, T. and Waterman, M.R. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J. Biol. Chem. 280 (2005) 11599–11607. [DOI] [PMID: 15659395]
2.  Zhao, B., Guengerich, F.P., Voehler, M. and Waterman, M.R. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J. Biol. Chem. 280 (2005) 42188–42197. [DOI] [PMID: 16239228]
3.  Zhao, B., Lamb, D.C., Lei, L., Kelly, S.L., Yuan, H., Hachey, D.L. and Waterman, M.R. Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 (2007) 8725–8733. [DOI] [PMID: 17614370]
[EC 1.14.19.69 created 2008 as EC 1.14.21.7, transferred 2018 to EC 1.14.19.69]
 
 
EC 1.14.19.70
Accepted name: mycocyclosin synthase
Reaction: cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
For diagram of cyclic dipeptide biosynthesis, click here
Glossary: mycocyclosin = (1S,14S)-6,9-dihydroxy-15,17-diazatetracyclo[12.2.2.13,7.18,12]icosa-3(20),4,6,8(19),9,11-hexaene-16,18-dione
Other name(s): CYP121; rv2276 (locus name)
Systematic name: cyclo(L-tyrosyl-L-tyrosyl),reduced ferredoxin:oxygen oxidoreductase (diarylbridge-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein from the bacterium Mycobacterium tuberculosis catalysing an oxidative reaction that does not incorporate oxygen into the product.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Belin, P., Le Du, M.H., Fielding, A., Lequin, O., Jacquet, M., Charbonnier, J.B., Lecoq, A., Thai, R., Courcon, M., Masson, C., Dugave, C., Genet, R., Pernodet, J.L. and Gondry, M. Identification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 106 (2009) 7426–7431. [DOI] [PMID: 19416919]
[EC 1.14.19.70 created 2013 as EC 1.14.21.9, transferred 2018 to EC 1.14.19.70]
 
 
EC 1.14.19.71
Accepted name: fumitremorgin C synthase
Reaction: tryprostatin A + [reduced NADPH—hemoprotein reductase] + O2 = fumitremorgin C + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of fumitremorgin alkaloid biosynthesis (part 1), click here
Glossary: tryprostatin A = (3S,8aS)-3-{[6-methoxy-2-(3-methylbut-2-en-1-yl)-1H-indol-3-yl]methyl}hexahydropyrrolo[1,2-a]pyrazine-1,4-dione
fumitremorgin C = (5aS,12S,14aS)-9-methoxy-12-(2-methylprop-1-en-1-yl)-1,2,3,5a,6,11,12,14a-octahydro-5H,14H-pyrrolo[1′′,2′′:4′,5′]pyrazino[1′,2′:1,6]pyrido[3,4-b]indole-5,14-dione
Other name(s): ftmE (gene name)
Systematic name: tryprostatin A,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: A cytochrome P-450 (heme-thiolate) protein. The protein from the fungus Aspergillus fumigatus also has activity with tryprostatin B forming demethoxyfumitremorgin C. Involved in the biosynthetic pathways of several indole alkaloids such as fumitremorgins and verruculogen.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kato, N., Suzuki, H., Takagi, H., Asami, Y., Kakeya, H., Uramoto, M., Usui, T., Takahashi, S., Sugimoto, Y. and Osada, H. Identification of cytochrome P450s required for fumitremorgin biosynthesis in Aspergillus fumigatus. ChemBioChem. 10 (2009) 920–928. [DOI] [PMID: 19226505]
[EC 1.14.19.71 created 2013 as EC 1.14.21.10, transferred 2018 to EC 1.14.19.71]
 
 
EC 1.14.19.72
Accepted name: (–)-pluviatolide synthase
Reaction: (–)-matairesinol + [reduced NADPH—hemoprotein reductase] + O2 = (–)-pluviatolide + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of podophyllotoxin biosynthesis, click here
Glossary: (–)-matairesinol = 3R,4R)-3,4-bis[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one
(–)-pluviatolide = ((3R,4R)-4-(2H-1,3-benzodioxol-5-ylmethyl)-3-[(4-hydroxy-3-methoxyphenyl)methyl]oxolan-2-one
Other name(s): CYP719A23 (gene name)
Systematic name: (–)-matairesinol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from the plants Sinopodophyllum hexandrum and Podophyllum peltatum catalyses the formation of a methylenedioxy-bridge. It is involved in the biosynthesis of podophyllotoxin, a non-alkaloid toxin lignan whose derivatives are important anticancer drugs.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Marques, J.V., Kim, K.W., Lee, C., Costa, M.A., May, G.D., Crow, J.A., Davin, L.B. and Lewis, N.G. Next generation sequencing in predicting gene function in podophyllotoxin biosynthesis. J. Biol. Chem. 288 (2013) 466–479. [DOI] [PMID: 23161544]
[EC 1.14.19.72 created 2016 as EC 1.14.21.11, transferred 2018 to EC 1.14.19.72]
 
 
EC 1.14.19.73
Accepted name: (S)-nandinine synthase
Reaction: (S)-scoulerine + [reduced NADPH—hemoprotein reductase] + O2 = (S)-nandinine + [oxidized NADPH—hemoprotein reductase] + 2 H2O
For diagram of nandinine biosynthesis, click here
Glossary: (S)-scoulerine = (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol
(S)-cheilanthifoline = (6aS)-9-methoxy-6,11,12,14-tetrahydro-2H,6aH-[1,3]dioxolo[4,5-h]isoquino[2,1-b]isoquinolin-8-ol
Other name(s): CYP719A3
Systematic name: (S)-scoulerine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(S)-nandinine-forming]
Comments: A cytochrome P-450 (heme-thiolate) enzyme found in plants. The enzyme catalyses an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid (S)-nandinine by the oxidative ring closure of adjacent phenolic and methoxy groups of (S)-scoulerine. cf. EC 1.14.19.65, (S)-cheilanthifoline synthase, which catalyses a similar reaction at the other side of the (S)-scoulerine molecule, forming (S)-cheilanthifoline.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ikezawa, N., Iwasa, K. and Sato, F. Molecular cloning and characterization of methylenedioxy bridge-forming enzymes involved in stylopine biosynthesis in Eschscholzia californica. FEBS J. 274 (2007) 1019–1035. [DOI] [PMID: 17250743]
2.  Diaz Chavez, M.L., Rolf, M., Gesell, A. and Kutchan, T.M. Characterization of two methylenedioxy bridge-forming cytochrome P450-dependent enzymes of alkaloid formation in the Mexican prickly poppy Argemone mexicana. Arch. Biochem. Biophys. 507 (2011) 186–193. [DOI] [PMID: 21094631]
[EC 1.14.19.73 created 2016 as EC 1.14.21.12, transferred 2018 to EC 1.14.19.73]
 
 
EC 1.14.19.74
Accepted name: (+)-piperitol/(+)-sesamin synthase
Reaction: (1) (+)-pinoresinol + [reduced NADPH-hemoprotein reductase]l + O2 = (+)-piperitol + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(2) (+)-piperitol + [reduced NADPH-hemoprotein reductase] + O2 = (+)-sesamin + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Other name(s): CYP81Q1; CYP81Q2; PS; PSS; SS; piperitol synthase; sesamin synthase
Systematic name: (+)-pinoresinol,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (cyclizing)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from Sesamum indicum (sesame) and S. radiatum (black sesame).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ono, E., Nakai, M., Fukui, Y., Tomimori, N., Fukuchi-Mizutani, M., Saito, M., Satake, H., Tanaka, T., Katsuta, M., Umezawa, T. and Tanaka, Y. Formation of two methylenedioxy bridges by a Sesamum CYP81Q protein yielding a furofuran lignan, (+)-sesamin. Proc. Natl Acad. Sci. USA 103 (2006) 10116–10121. [PMID: 16785429]
[EC 1.14.19.74 created 2018]
 
 
EC 1.14.20.14
Accepted name: hapalindole-type alkaloid chlorinase
Reaction: (1) hapalindole U + 2-oxoglutarate + O2 + chloride = hapalindole G + succinate + CO2 + H2O
(2)12-epi-fischerindole U + 2-oxoglutarate + O2 + chloride = 12-epi-fischerindole G + succinate + CO2 + H2O
Glossary: 12-epi-fischerindole U = (6aS,9S,10R,10aS)-9-ethenyl-10-isocyano-6,6,9-trimethyl-5,6,6a,7,8,9,10,10a-octahydroindeno[2,1-b]indole
12-epi-fischerindole G = (6aR,8R,9S,10R,10aS)-8-chloro-9-ethenyl-10-isocyano-6,6,9-trimethyl-5,6,6a,7,8,9,10,10a-octahydroindeno[2,1-b]indole
Other name(s): ambO5 (gene name); welO5 (gene name)
Systematic name: 12-epi-fischerindole U,2-oxoglutarate:oxygen oxidoreductase (13-halogenating)
Comments: The enzyme, characterized from hapalindole-type alkaloids-producing cyanobacteria, is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrates in a reaction that requires oxygen, chloride ions, iron(II) and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hillwig, M.L. and Liu, X. A new family of iron-dependent halogenases acts on freestanding substrates. Nat. Chem. Biol. 10 (2014) 921–923. [PMID: 25218740]
2.  Zhu, Q., Hillwig, M.L., Doi, Y. and Liu, X. Aliphatic halogenase enables late-stage C-H functionalization: selective synthesis of a brominated fischerindole alkaloid with enhanced antibacterial activity. Chembiochem 17 (2016) 466–470. [PMID: 26749394]
3.  Hillwig, M.L., Zhu, Q., Ittiamornkul, K. and Liu, X. Discovery of a promiscuous non-heme iron halogenase in ambiguine alkaloid biogenesis: implication for an evolvable enzyme family for late-stage halogenation of aliphatic carbons in small molecules. Angew. Chem. Int. Ed. Engl. 55 (2016) 5780–5784. [PMID: 27027281]
[EC 1.14.20.14 created 2018]
 
 
EC 1.14.20.15
Accepted name: L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
Reaction: an L-threonyl-[L-threonyl-carrier protein] + 2-oxoglutarate + O2 + Cl- = a 4-chloro-L-threonyl-[L-threonyl-carrier protein] + succinate + CO2 + H2O
Other name(s): syrB2 (gene name)
Systematic name: L-threonyl-[L-threonyl-carrier protein],2-oxoglutarate:oxygen oxidoreductase (4-halogenating)
Comments: The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis. The enzyme is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Vaillancourt, F.H., Yin, J. and Walsh, C.T. SyrB2 in syringomycin E biosynthesis is a nonheme FeII α-ketoglutarate- and O2-dependent halogenase. Proc. Natl Acad. Sci. USA 102 (2005) 10111–10116. [PMID: 16002467]
[EC 1.14.20.15 created 2018]
 
 
EC 1.14.21.1
Transferred entry: (S)-stylopine synthase. Now EC 1.14.19.64, (S)-stylopine synthase
[EC 1.14.21.1 created 2002, deleted 2018]
 
 
EC 1.14.21.2
Transferred entry: (S)-cheilanthifoline synthase. Now EC 1.14.19.65, (S)-cheilanthifoline synthase
[EC 1.14.21.2 created 2002, modified 2016, deleted 2018]
 
 
EC 1.14.21.3
Transferred entry: berbamunine synthase. Now EC 1.14.19.66, berbamunine synthase
[EC 1.14.21.3 created 2002, deleted 2018]
 
 
EC 1.14.21.4
Transferred entry: salutaridine synthase. Now EC 1.14.19.67, salutaridine synthase
[EC 1.14.21.4 created 2002, deleted 2018]
 
 
EC 1.14.21.5
Transferred entry: (S)-canadine synthase. Now EC 1.14.19.68, (S)-canadine synthase
[EC 1.14.21.5 created 2002, deleted 2018]
 
 
EC 1.14.21.7
Transferred entry: biflaviolin synthase. Now EC 1.14.19.69, biflaviolin synthase
[EC 1.14.21.7 created 2008, deleted 2018]
 
 
EC 1.14.21.8
Transferred entry: pseudobaptigenin synthase. Now EC 1.14.19.63, pseudobaptigenin synthase.
[EC 1.14.21.8 created 2011, deleted 2018]
 
 
EC 1.14.21.9
Transferred entry: mycocyclosin synthase. Now EC 1.14.19.70, mycocyclosin synthase
[EC 1.14.21.9 created 2013, deleted 2018]
 
 
EC 1.14.21.10
Transferred entry: fumitremorgin C synthase. Now EC 1.14.19.71, fumitremorgin C synthase
[EC 1.14.21.10 created 2013, deleted 2018]
 
 
EC 1.14.21.11
Transferred entry: (–)-pluviatolide synthase. Now EC 1.14.19.72, (–)-pluviatolide synthase
[EC 1.14.21.11 created 2016, deleted 2018]
 
 
EC 1.14.21.12
Transferred entry: (S)-nandinine synthase. Now EC 1.14.19.73, (S)-nandinine synthase
[EC 1.14.21.12 created 2016, deleted 2018]
 
 
EC 1.14.99.43
Transferred entry: β-amyrin 24-hydroxylase. Now EC 1.14.14.134, β-amyrin 24-hydroxylase
[EC 1.14.99.43 created 2011, deleted 2018]
 
 
EC 1.14.99.45
Transferred entry: carotene ε-monooxygenase. Now EC 1.14.14.158, carotene ε-monooxygenase
[EC 1.14.99.45 created 2011, deleted 2018]
 
 
EC 1.14.99.49
Transferred entry: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase. Now EC 1.14.15.31, 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase
[EC 1.14.99.49 created 2014, deleted 2018]
 
 
EC 1.14.99.61
Accepted name: cyclooctat-9-en-7-ol 5-monooxygenase
Reaction: cyclooctat-9-en-7-ol + reduced acceptor + O2 = cyclooctat-9-ene-5,7-diol + acceptor + H2O
Glossary: cyclooctat-9-en-7-ol = (1S,3aS,4R,7S,9aS,10aS)-1,4,9a-trimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,7,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulen-4-ol
cyclooctat-9-ene-5,7-diol = (1S,3R,3aS,4R,7S,9aS,10aS)-1,4,9a-trimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,7,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulene-3,4-diol
Other name(s): CotB3
Systematic name: cyclooctat-9-en-7-ol,hydrogen-donor:oxygen oxidoreductase (5-hydroxylating)
Comments: Isolated from the bacterium Streptomyces melanosporofaciens M1614-43f2. Involved in the biosynthesis of cyclooctatin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kim, S.Y., Zhao, P., Igarashi, M., Sawa, R., Tomita, T., Nishiyama, M. and Kuzuyama, T. Cloning and heterologous expression of the cyclooctatin biosynthetic gene cluster afford a diterpene cyclase and two P450 hydroxylases. Chem. Biol. 16 (2009) 736–743. [DOI] [PMID: 19635410]
2.  Gorner, C., Schrepfer, P., Redai, V., Wallrapp, F., Loll, B., Eisenreich, W., Haslbeck, M. and Bruck, T. Identification, characterization and molecular adaptation of class I redox systems for the production of hydroxylated diterpenoids. Microb. Cell Fact. 15:86 (2016). [PMID: 27216162]
[EC 1.14.99.61 created 2018]
 
 
EC 1.14.99.62
Accepted name: cyclooctatin synthase
Reaction: cyclooctat-9-ene-5,7-diol + reduced acceptor + O2 = cyclooctatin + acceptor + H2O
Glossary: cyclooctat-9-ene-5,7-diol = (1S,3R,3aS,4R,7S,9aS,10aS)-1,4,9a-trimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,7,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulene-3,4-diol
cyclooctatin = cycloctat-9-ene-5,7,18-triol = (1R,3R,3aS,4R,7S,9aS,10aS)-1-(hydroxymethyl-)4,9a-dimethyl-7-(propan-2-yl)-1,2,3,3a,4,5,7,8,9,9a,10,10a-dodecahydrodicyclopenta[a,d][8]annulene-3,4-diol
Other name(s): CotB4
Systematic name: cyclooctat-9-ene-5,7-diol,hydrogen-donor:oxygen oxidoreductase (18-hydroxylating)
Comments: Isolated from the bacterium Streptomyces melanosporofaciens M1614-43f2.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kim, S.Y., Zhao, P., Igarashi, M., Sawa, R., Tomita, T., Nishiyama, M. and Kuzuyama, T. Cloning and heterologous expression of the cyclooctatin biosynthetic gene cluster afford a diterpene cyclase and two P450 hydroxylases. Chem. Biol. 16 (2009) 736–743. [DOI] [PMID: 19635410]
2.  Gorner, C., Schrepfer, P., Redai, V., Wallrapp, F., Loll, B., Eisenreich, W., Haslbeck, M. and Bruck, T. Identification, characterization and molecular adaptation of class I redox systems for the production of hydroxylated diterpenoids. Microb. Cell Fact. 15:86 (2016). [PMID: 27216162]
[EC 1.14.99.62 created 2018]
 
 
EC 1.14.99.63
Accepted name: β-carotene 4-ketolase
Reaction: (1) β-carotene + 2 reduced acceptor + 2 O2 = echinenone + 2 acceptor + 3 H2O
(2) echinenone + 2 reduced acceptor + 2 O2 = canthaxanthin + 2 acceptor + 3 H2O
Glossary: echinenone = β,β-caroten-4-one
canthaxanthin = β,β-carotene-4,4′-dione
zeaxanthin = β,β-carotene-3,3′-diol
astaxanthin = 3,3′-dihydroxy-β,β-carotene-4,4′-dione
Other name(s): BKT (ambiguous); β-C-4 oxygenase; β-carotene ketolase; crtS (gene name); crtW (gene name)
Systematic name: β-carotene,donor:oxygen oxidoreductase (echinenone-forming)
Comments: The enzyme, studied from algae, plants, fungi, and bacteria, adds an oxo group at position 4 of a carotenoid β ring. It is involved in the biosynthesis of carotenoids such as astaxanthin and flexixanthin. The enzyme does not act on β rings that are hydroxylated at position 3, such as in zeaxanthin (cf. EC 1.14.99.64, zeaxanthin 4-ketolase). The enzyme from the yeast Xanthophyllomyces dendrorhous is bifuntional and also catalyses the activity of EC 1.14.15.24, β-carotene 3-hydroxylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Lotan, T. and Hirschberg, J. Cloning and expression in Escherichia coli of the gene encoding β-C-4-oxygenase, that converts β-carotene to the ketocarotenoid canthaxanthin in Haematococcus pluvialis. FEBS Lett. 364 (1995) 125–128. [PMID: 7750556]
2.  Breitenbach, J., Misawa, N., Kajiwara, S. and Sandmann, G. Expression in Escherichia coli and properties of the carotene ketolase from Haematococcus pluvialis. FEMS Microbiol. Lett. 140 (1996) 241–246. [PMID: 8764486]
3.  Steiger, S. and Sandmann, G. Cloning of two carotenoid ketolase genes from Nostoc punctiforme for the heterologous production of canthaxanthin and astaxanthin. Biotechnol. Lett. 26 (2004) 813–817. [PMID: 15269553]
4.  Ojima, K., Breitenbach, J., Visser, H., Setoguchi, Y., Tabata, K., Hoshino, T., van den Berg, J. and Sandmann, G. Cloning of the astaxanthin synthase gene from Xanthophyllomyces dendrorhous (Phaffia rhodozyma) and its assignment as a β-carotene 3-hydroxylase/4-ketolase. Mol. Genet. Genomics 275 (2006) 148–158. [PMID: 16416328]
5.  Tao, L., Yao, H., Kasai, H., Misawa, N. and Cheng, Q. A carotenoid synthesis gene cluster from Algoriphagus sp. KK10202C with a novel fusion-type lycopene β-cyclase gene. Mol. Genet. Genomics 276 (2006) 79–86. [PMID: 16625353]
6.  Kathiresan, S., Chandrashekar, A., Ravishankar, G.A. and Sarada, R. Regulation of astaxanthin and its intermediates through cloning and genetic transformation of β-carotene ketolase in Haematococcus pluvialis. J. Biotechnol. 196-197 (2015) 33–41. [PMID: 25612872]
[EC 1.14.99.63 created 2018]
 
 
EC 1.14.99.64
Accepted name: zeaxanthin 4-ketolase
Reaction: (1) zeaxanthin + 2 reduced acceptor + 2 O2 = adonixanthin + 2 acceptor + 3 H2O
(2) adonixanthin + 2 reduced acceptor + 2 O2 = (3S,3′S)-astaxanthin + 2 acceptor + 3 H2O
Glossary: zeaxanthin = β,β-carotene-3,3′-diol
adonixanthin = 3,3′-dihydroxy-β,β-carotene-4-one
(3S,3′S)-astaxanthin = (3S,3′S)-3,3′-dihydroxy-β,β-carotene-4,4′-dione
Other name(s): BKT (ambiguous); crtW148 (gene name)
Systematic name: zeaxanthin,donor:oxygen oxidoreductase (adonixanthin-forming)
Comments: The enzyme has a similar activity to that of EC 1.14.99.63, β-carotene 4-ketolase, but unlike that enzyme is able to also act on zeaxanthin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zhong, Y.J., Huang, J.C., Liu, J., Li, Y., Jiang, Y., Xu, Z.F., Sandmann, G. and Chen, F. Functional characterization of various algal carotenoid ketolases reveals that ketolating zeaxanthin efficiently is essential for high production of astaxanthin in transgenic Arabidopsis. J. Exp. Bot. 62 (2011) 3659–3669. [PMID: 21398427]
2.  Huang, J., Zhong, Y., Sandmann, G., Liu, J. and Chen, F. Cloning and selection of carotenoid ketolase genes for the engineering of high-yield astaxanthin in plants. Planta 236 (2012) 691–699. [PMID: 22526507]
[EC 1.14.99.64 created 2018]
 
 
EC 1.17 Acting on CH or CH2 groups
 
EC 1.17.9.1
Accepted name: 4-methylphenol dehydrogenase (hydroxylating)
Reaction: 4-methylphenol + 4 oxidized azurin + H2O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H+ (overall reaction)
(1a) 4-methylphenol + 2 oxidized azurin + H2O = 4-hydroxybenzyl alcohol + 2 reduced azurin + 2 H+
(1b) 4-hydroxybenzyl alcohol + 2 oxidized azurin = 4-hydroxybenzaldehyde + 2 reduced azurin + 2 H+
Glossary: 4-methylphenol = 4-cresol = p-cresol
Other name(s): pchCF (gene names); p-cresol-(acceptor) oxidoreductase (hydroxylating); p-cresol methylhydroxylase; 4-cresol dehydrogenase (hydroxylating)
Systematic name: 4-methylphenol:oxidized azurin oxidoreductase (methyl-hydroxylating)
Comments: This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, UM-BBD, CAS registry number: 66772-07-4
References:
1.  Hopper, D.J. and Taylor, D.G. The purification and properties of p-cresol-(acceptor) oxidoreductase (hydroxylating), a flavocytochrome from Pseudomonas putida. Biochem. J. 167 (1977) 155–162. [PMID: 588247]
2.  McIntire, W., Edmondson, D.E. and Singer, T.P. 8α-O-Tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase. J. Biol. Chem. 255 (1980) 6553–6555. [PMID: 7391034]
3.  Hopper, D.J., Jones, M.R. and Causer, M.J. Periplasmic location of p-cresol methylhydroxylase in Pseudomonas putida. FEBS Lett. 182 (1985) 485–488. [PMID: 3920077]
4.  Bossert, I.D., Whited, G., Gibson, D.T. and Young, L.Y. Anaerobic oxidation of p-cresol mediated by a partially purified methylhydroxylase from a denitrifying bacterium. J. Bacteriol. 171 (1989) 2956–2962. [DOI] [PMID: 2722739]
5.  Reeve, C.D., Carver, M.A. and Hopper, D.J. Stereochemical aspects of the oxidation of 4-ethylphenol by the bacterial enzyme 4-ethylphenol methylenehydroxylase. Biochem. J. 269 (1990) 815–819. [PMID: 1697166]
6.  Peters, F., Heintz, D., Johannes, J., van Dorsselaer, A. and Boll, M. Genes, enzymes, and regulation of para-cresol metabolism in Geobacter metallireducens. J. Bacteriol. 189 (2007) 4729–4738. [PMID: 17449613]
7.  Johannes, J., Bluschke, A., Jehmlich, N., von Bergen, M. and Boll, M. Purification and characterization of active-site components of the putative p-cresol methylhydroxylase membrane complex from Geobacter metallireducens. J. Bacteriol. 190 (2008) 6493–6500. [PMID: 18658262]
[EC 1.17.9.1 created 1983 as EC 1.17.99.1, modified 2001, modified 2011, modified 2015, transferred 2018 to EC 1.17.9.1]
 
 
EC 1.17.99.1
Transferred entry: 4-methylphenol dehydrogenase (hydroxylating). Now EC 1.17.9.1, 4-methylphenol dehydrogenase (hydroxylating)
[EC 1.17.99.1 created 1983, modified 2001, modified 2011, modified 2015, deleted 2018]
 
 
EC 1.18.1.8
Transferred entry: ferredoxin-NAD+ oxidoreductase (Na+-transporting). Now EC 7.2.1.2, ferredoxin—NAD+ oxidoreductase (Na+-transporting)
[EC 1.18.1.8 created 2015, deleted 2018]
 
 
EC 1.21.98.4
Accepted name: PqqA peptide cyclase
Reaction: a PqqA peptide + S-adenosyl-L-methionine = a PqqA peptide with linked Glu-Tyr residues + 5′-deoxyadenosine + L-methionine
Glossary: PqqA peptide = pyrroloquinoline quinone biosynthesis protein A, a small peptide that provides the precursor for the biosynthesis of the cofactor pyrroloquinoline quinone
Other name(s): pqqE (gene name)
Systematic name: PqqA peptide:S-adenosyl-L-methionine oxidoreductase (cyclizing)
Comments: This bacterial enzyme, which is a member of the radical SAM protein family, catalyses the formation of a C-C bond between C-4 of glutamate and C-3 of tyrosine residues of the PqqA protein (which are separated by three amino acid residues). This is the first enzymic step in the biosynthesis of the bacterial enzyme cofactor pyrroloquinoline quinone (PQQ). The reaction is dependent on the presence of a reductant (flavodoxin) and the accessory protein PqqD.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wecksler, S.R., Stoll, S., Iavarone, A.T., Imsand, E.M., Tran, H., Britt, R.D. and Klinman, J.P. Interaction of PqqE and PqqD in the pyrroloquinoline quinone (PQQ) biosynthetic pathway links PqqD to the radical SAM superfamily. Chem. Commun. (Camb.) 46 (2010) 7031–7033. [PMID: 20737074]
2.  Latham, J.A., Iavarone, A.T., Barr, I., Juthani, P.V. and Klinman, J.P. PqqD is a novel peptide chaperone that forms a ternary complex with the radical S-adenosylmethionine protein PqqE in the pyrroloquinoline quinone biosynthetic pathway. J. Biol. Chem. 290 (2015) 12908–12918. [PMID: 25817994]
3.  Barr, I., Latham, J.A., Iavarone, A.T., Chantarojsiri, T., Hwang, J.D. and Klinman, J.P. Demonstration that the radical S-adenosylmethionine (SAM) enzyme PqqE catalyzes de novo carbon-carbon cross-linking within a peptide substrate PqqA in the presence of the peptide chaperone PqqD. J. Biol. Chem. 291 (2016) 8877–8884. [PMID: 26961875]
[EC 1.21.98.4 created 2018]
 
 
EC 2.1.1.349
Accepted name: toxoflavin synthase
Reaction: (1) S-adenosyl-L-methionine + 1,6-didemethyltoxoflavin = S-adenosyl-L-homocysteine + reumycin
(2) S-adenosyl-L-methionine + reumycin = S-adenosyl-L-homocysteine + toxoflavin
Glossary: reumycin = 1-demethyltoxoflavin
toxoflavin = 1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Other name(s): toxA (gene name)
Systematic name: S-adenosyl-L-methionine:1,6-didemethyltoxoflavin N1,N6-dimethyltransferase (toxoflavin-forming)
Comments: The enzyme is a dual-specificity methyltransferase that catalyses the last two steps of toxoflavin biosynthesis. Toxoflavin is a major virulence factor of several bacterial crop pathogens.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Fenwick, M.K., Philmus, B., Begley, T.P. and Ealick, S.E. Burkholderia glumae ToxA Is a dual-specificity methyltransferase that catalyzes the last two steps of toxoflavin biosynthesis. Biochemistry 55 (2016) 2748–2759. [PMID: 27070241]
[EC 2.1.1.349 created 2018]
 
 
EC 2.3.1.273
Accepted name: diglucosylglycerate octanoyltransferase
Reaction: octanoyl-CoA + 2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate. = 2-O-[6-O-octanoyl-α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate. + CoA
Other name(s): octT (gene name); DGG octanoyltransferase
Systematic name: octanoyl-CoA:2-O-[α-D-glucopyranosyl-(1→6)-α-D-glucopyranosyl]-D-glycerate octanoyltransferase
Comments: The enzyme, characterized from mycobacteria, is involved in the biosynthesis of methylglucose lipopolysaccharide (MGLP). The enzyme can also act on 2-O-(α-D-glucopyranosyl)-D-glycerate, but with lower activity.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Maranha, A., Moynihan, P.J., Miranda, V., Correia Lourenco, E., Nunes-Costa, D., Fraga, J.S., Jose Barbosa Pereira, P., Macedo-Ribeiro, S., Ventura, M.R., Clarke, A.J. and Empadinhas, N. Octanoylation of early intermediates of mycobacterial methylglucose lipopolysaccharides. Sci Rep 5:13610 (2015). [PMID: 26324178]
[EC 2.3.1.273 created 2018]
 
 
EC 2.4.1.358
Accepted name: acylphloroglucinol glucosyltransferase
Reaction: UDP-α-D-glucose + 2-acylphloroglucinol = UDP + 2-acylphloroglucinol 1-O-β-D-glucoside
Glossary: phlorisobutyrophenone = 2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one
phlorisovalerophenone = 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
Other name(s): UGT71K3
Systematic name: UDP-α-D-glucose:2-acylphloroglucinol 1-O-β-glucosyltransferase
Comments: Isolated from strawberries (Fragaria X ananassa). Acts best on phloroisovalerophenone and phlorobutyrophenone but will also glycosylate many other phenolic compounds. A minor product of the reaction is the 5-O-β-D-glucoside.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Song, C., Zhao, S., Hong, X., Liu, J., Schulenburg, K. and Schwab, W. A UDP-glucosyltransferase functions in both acylphloroglucinol glucoside and anthocyanin biosynthesis in strawberry (Fragaria x ananassa). Plant J. 85 (2016) 730–742. [PMID: 26859691]
[EC 2.4.1.358 created 2018]
 
 
*EC 2.5.1.17
Accepted name: corrinoid adenosyltransferase
Reaction: (1) 2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein (overall reaction)
(1a) 2 cob(II)alamin + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)alamin
(1b) a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)alamin = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)alamin (spontaneous)
(1c) 2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)alamin = 2 triphosphate + 2 adenosylcob(III)alamin + 2 [corrinoid adenosyltransferase]
(2) 2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein (overall reaction)
(2a) 2 cob(II)yrinic acid a,c-diamide + 2 [corrinoid adenosyltransferase] = 2 [corrinoid adenosyltransferase]-cob(II)yrinic acid a,c-diamide
(2b) a reduced flavoprotein + 2 [corrinoid adenosyltransferase]-cob(II)yrinic acid a,c-diamide = an oxidized flavoprotein + 2 [corrinoid adenosyltransferase]-cob(I)yrinic acid a,c-diamide (spontaneous)
(2c) 2 ATP + 2 [corrinoid adenosyltransferase]-cob(I)yrinic acid a,c-diamide = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + 2 [corrinoid adenosyltransferase]
For diagram of corrin biosynthesis (part 5), click here and for diagram of the cobinamide salvage pathways, click here
Other name(s): MMAB (gene name); cobA (gene name); cobO (gene name); pduO (gene name); ATP:corrinoid adenosyltransferase; cob(I)alamin adenosyltransferase; aquacob(I)alamin adenosyltransferase; aquocob(I)alamin vitamin B12s adenosyltransferase; ATP:cob(I)alamin Coβ-adenosyltransferase; ATP:cob(I)yrinic acid-a,c-diamide Coβ-adenosyltransferase; cob(I)yrinic acid a,c-diamide adenosyltransferase
Systematic name: ATP:cob(II)alamin Coβ-adenosyltransferase
Comments: The corrinoid adenosylation pathway comprises three steps: (i) reduction of Co(III) within the corrinoid to Co(II) by a one-electron transfer. This can occur non-enzymically in the presence of dihydroflavin nucleotides or reduced flavoproteins [3]. (ii) Co(II) is bound by corrinoid adenosyltransferase, resulting in displacement of the lower axial ligand by an aromatic residue. The reduction potential of the 4-coordinate Co(II) intermediate is raised by ~250 mV compared with the free compound, bringing it to within physiological range. This is followed by a second single-electron transfer from either free dihydroflavins or the reduced flavin cofactor of flavoproteins, resulting in reduction to Co(I) [7]. (iii) the Co(I) conducts a nucleophilic attack on the adenosyl moiety of ATP, resulting in transfer of the deoxyadenosyl group and oxidation of the cobalt atom to Co(III) state. Three types of corrinoid adenosyltransferases, not related by sequence, have been described. In the anaerobic bacterium Salmonella enterica they are encoded by the cobA gene (a housekeeping enzyme involved in both the de novo biosynthesis and the salvage of adenosylcobalamin), the pduO gene (involved in (S)-propane-1,2-diol utilization), and the eutT gene (involved in ethanolamine utilization). Since EutT hydrolyses triphosphate to diphosphate and phosphate during catalysis, it is classified as a separate enzyme. The mammalian enzyme belongs to the PduO type. The enzyme can act on other corrinoids, such as cob(II)inamide.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37277-84-2
References:
1.  Vitols, E., Walker, G.A. and Huennekens, F.M. Enzymatic conversion of vitamin B12s to a cobamide coenzyme, α-(5,6-dimethylbenzimidazolyl)deoxyadenosylcobamide (adenosyl-B12). J. Biol. Chem. 241 (1966) 1455–1461. [PMID: 5946606]
2.  Bauer, C.B., Fonseca, M.V., Holden, H.M., Thoden, J.B., Thompson, T.B., Escalante-Semerena, J.C. and Rayment, I. Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP. Biochemistry 40 (2001) 361–374. [DOI] [PMID: 11148030]
3.  Fonseca, M.V. and Escalante-Semerena, J.C. Reduction of Cob(III)alamin to Cob(II)alamin in Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 182 (2000) 4304–4309. [PMID: 10894741]
4.  Fonseca, M.V. and Escalante-Semerena, J.C. An in vitro reducing system for the enzymic conversion of cobalamin to adenosylcobalamin. J. Biol. Chem. 276 (2001) 32101–32108. [DOI] [PMID: 11408479]
5.  Suh, S. and Escalante-Semerena, J.C. Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium. J. Bacteriol. 177 (1995) 921–925. [DOI] [PMID: 7860601]
6.  Mera, P.E., St Maurice, M., Rayment, I. and Escalante-Semerena, J.C. Residue Phe112 of the human-type corrinoid adenosyltransferase (PduO) enzyme of Lactobacillus reuteri is critical to the formation of the four-coordinate Co(II) corrinoid substrate and to the activity of the enzyme. Biochemistry 48 (2009) 3138–3145. [PMID: 19236001]
7.  Mera, P.E. and Escalante-Semerena, J.C. Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins. J. Biol. Chem. 285 (2010) 2911–2917. [PMID: 19933577]
[EC 2.5.1.17 created 1972, modified 2004, modified 2018]
 
 
EC 2.5.1.77
Transferred entry: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase.
[EC 2.5.1.77 created 2010, deleted 2018]
 
 
EC 2.5.1.147
Accepted name: 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase
Reaction: 5-amino-6-(D-ribitylamino)uracil + L-tyrosine + S-adenosyl-L-methionine = 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + 2-iminoacetate + L-methionine + 5′-deoxyadenosine
Glossary: 5-amino-6-(D-ribitylamino)uracil = 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione
Other name(s): cofH (gene name); cbiF (gene name) (ambiguous)
Systematic name: 5-amino-6-(D-ribitylamino)uracil:L-tyrosine, 4-hydroxyphenyl transferase
Comments: The enzyme is involved in the production of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO), the precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. FO is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, is a radical SAM enzyme that uses the 5′-deoxyadenosyl radical to initiate the reaction.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Decamps, L., Philmus, B., Benjdia, A., White, R., Begley, T.P. and Berteau, O. Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. J. Am. Chem. Soc. 134 (2012) 18173–18176. [DOI] [PMID: 23072415]
2.  Philmus, B., Decamps, L., Berteau, O. and Begley, T.P. Biosynthetic versatility and coordinated action of 5′-deoxyadenosyl radicals in deazaflavin biosynthesis. J. Am. Chem. Soc. 137 (2015) 5406–5413. [DOI] [PMID: 25781338]
[EC 2.5.1.147 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 2.5.1.147]
 
 
*EC 2.7.2.2
Accepted name: carbamate kinase
Reaction: ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O (overall reaction)
(1a) ATP + carbamate = ADP + carbamoyl phosphate
(1b) NH3 + hydrogencarbonate = carbamate + H2O (spontaneous)
For diagram of AMP catabolism, click here
Other name(s): CKase; carbamoyl phosphokinase; carbamyl phosphokinase
Systematic name: ATP:carbamate phosphotransferase
Comments: The enzyme catalyses the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyses to ammonia and hydrogencarbonate. The physiological role of the enzyme is to generate ATP.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, PDB, CAS registry number: 9026-69-1
References:
1.  Jones, M.E., Spector, L. and Lipmann, F. Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis. J. Am. Chem. Soc. 77 (1955) 819–820.
2.  Davis, R.H. Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase. Biochim. Biophys. Acta 107 (1965) 44–53. [DOI] [PMID: 5857367]
3.  Glasziou, K.T. The metabolism of arginine in Serratia marcescens. II. Carbamyladenosine diphosphate phosphoferase. Aust. J. Biol. Sci. 9 (1956) 253–262.
4.  Bishop, S.H. and Grisolia, S. Crystalline carbamate kinase. Biochim. Biophys. Acta 118 (1966) 211–215. [PMID: 4959296]
5.  Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532–9541. [PMID: 6895223]
[EC 2.7.2.2 created 1961, modified 2018]
 
 
EC 2.8.5.2
Accepted name: L-cysteine S-thiosulfotransferase
Reaction: (1) [SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
(2) [SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
Other name(s): SoxXA
Systematic name: thiosulfate:[SoxY protein]-L-cysteine thiosufotransferase
Comments: The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Friedrich, C.G., Quentmeier, A., Bardischewsky, F., Rother, D., Kraft, R., Kostka, S. and Prinz, H. Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17. J. Bacteriol. 182 (2000) 4677–4687. [PMID: 10940005]
2.  Cheesman, M.R., Little, P.J. and Berks, B.C. Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum. Biochemistry 40 (2001) 10562–10569. [PMID: 11523998]
3.  Rother, D. and Friedrich, C.G. The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system. Biochim. Biophys. Acta 1598 (2002) 65–73. [PMID: 12147345]
4.  Bamford, V.A., Bruno, S., Rasmussen, T., Appia-Ayme, C., Cheesman, M.R., Berks, B.C. and Hemmings, A.M. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme. EMBO J. 21 (2002) 5599–5610. [PMID: 12411478]
5.  Dambe, T., Quentmeier, A., Rother, D., Friedrich, C. and Scheidig, A.J. Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation. J. Struct. Biol. 152 (2005) 229–234. [PMID: 16297640]
6.  Hensen, D., Sperling, D., Truper, H.G., Brune, D.C. and Dahl, C. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62 (2006) 794–810. [PMID: 16995898]
7.  Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12:e0173395 (2017). [DOI] [PMID: 28257465]
[EC 2.8.5.2 created 2018]
 
 
*EC 3.4.19.9
Accepted name: folate γ-glutamyl hydrolase
Reaction: tetrahydropteroyl-(γ-glutamyl)n + (n-1) H2O = 5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Other name(s): GGH (gene name); conjugase; folate conjugase; lysosomal γ-glutamyl carboxypeptidase; γ-Glu-X carboxypeptidase; pteroyl-poly-γ-glutamate hydrolase; carboxypeptidase G; folic acid conjugase; poly(γ-glutamic acid) endohydrolase; polyglutamate hydrolase; poly(glutamic acid) hydrolase II; pteroylpoly-γ-glutamyl hydrolase; γ-glutamyl hydrolase
Systematic name: tetrahydropteroyl-poly-γ-glutamyl γ-glutamyl hydrolase
Comments: The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase. It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu). The initial cleavage may release either monoglutamate or poly-γ-glutamate of two or more residues, depending on the specific enzyme. For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates. The enzyme is lysosomal (and secreted) in animals and vacuolar in plants.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  McGuire, J.J. and Coward, J.K. Pteroylpolyglutamates: biosynthesis, degradation and function.. In: Blakley, R.L. and Benkovic, S.J. (Eds), Folates and Pterins, John Wiley and Sons, New York, 1984, pp. 135–191.
2.  Wang, Y., Nimec, Z., Ryan, T.J., Dias, J.A. and Galivan, J. The properties of the secreted γ-glutamyl hydrolases from H35 hepatoma cells. Biochim. Biophys. Acta 1164 (1993) 227–235. [DOI] [PMID: 8343522]
3.  Yao, R., Rhee, M.S. and Galivan, J. Effects of γ-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells. Mol. Pharmacol. 48 (1995) 505–511. [PMID: 7565632]
4.  Yao, R., Schneider, E., Ryan, T.J. and Galivan, J. Human γ-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro. Proc. Natl. Acad. Sci. USA 93 (1996) 10134–10138. [DOI] [PMID: 8816764]
5.  Yao, R., Nimec, Z., Ryan, T.J. and Galivan, J. Identification, cloning, and sequencing of a cDNA coding for rat γ-glutamyl hydrolase. J. Biol. Chem. 271 (1996) 8525–8528. [DOI] [PMID: 8621474]
6.  Orsomando, G., de la Garza, R.D., Green, B.J., Peng, M., Rea, P.A., Ryan, T.J., Gregory, J.F., 3rd and Hanson, A.D. Plant γ-glutamyl hydrolases and folate polyglutamates: characterization, compartmentation, and co-occurrence in vacuoles. J. Biol. Chem. 280 (2005) 28877–28884. [PMID: 15961386]
7.  Akhtar, T.A., McQuinn, R.P., Naponelli, V., Gregory, J.F., 3rd, Giovannoni, J.J. and Hanson, A.D. Tomato γ-glutamylhydrolases: expression, characterization, and evidence for heterodimer formation. Plant Physiol. 148 (2008) 775–785. [PMID: 18757550]
[EC 3.4.19.9 created 1972 as EC 3.4.12.10, transferred 1978 to EC 3.4.22.12, transferred 1992 to EC 3.4.19.9, modified 1997, modified 2018]
 
 
EC 3.6.3.1
Transferred entry: phospholipid-translocating ATPase. Now EC 7.6.2.1, P-type phospholipid transporter
[EC 3.6.3.1 created 2000 (EC 3.6.3.13 created 2000, incorporated 2001), deleted 2018]
 
 
EC 3.6.3.6
Transferred entry: H+-exporting ATPase. Now EC 7.1.2.1, P-type H+-exporting transporter
[EC 3.6.3.6 created 1984 as EC 3.6.1.35, transferred 2000 to EC 3.6.3.6, deleted 2018]
 
 
EC 3.6.3.7
Transferred entry: Na+-exporting ATPase. Now EC 7.2.2.3, P-type Na+ transporter
[EC 3.6.3.7 created 2000, modified 2001, transferred 2018 to EC 7.2.2.3, deleted 2018]
 
 
EC 3.6.3.14
Transferred entry: H+-transporting two-sector ATPase. Now EC 7.1.2.2, H+-transporting two-sector ATPase
[EC 3.6.3.14 created 1984 as EC 3.6.1.34, transferred 2000 to EC 3.6.3.14, deleted 2018]
 
 
EC 3.6.3.15
Transferred entry: Na+-transporting two-sector ATPase. Now EC 7.2.2.1, Na+-transporting two-sector ATPase
[EC 3.6.3.15 created 2000, transferred 2018 to EC 7.2.2.1, deleted 2018]
 
 
EC 3.6.3.18
Transferred entry: oligosaccharide-transporting ATPase. Now EC 7.5.2.2, ABC-type oligosaccharide transporter
[EC 3.6.3.18 created 2000, deleted 2018]
 
 
EC 3.6.3.19
Transferred entry: maltose-transporting ATPase. Now EC 7.5.2.1, ABC-type maltose transporter
[EC 3.6.3.19 created 2000, deleted 2018]
 
 
EC 3.6.3.21
Transferred entry: polar-amino-acid-transporting ATPase. Now EC 7.4.2.1, ABC-type polar-amino-acid transporter
[EC 3.6.3.21 created 2000, deleted 2018]
 
 
EC 3.6.3.22
Transferred entry: nonpolar-amino-acid-transporting ATPase. Now EC 7.4.2.2, ABC-type nonpolar-amino-acid transporter
[EC 3.6.3.22 created 2000, deleted 2018]
 
 
EC 3.6.3.27
Transferred entry: phosphate-transporting ATPase. Now EC 7.3.2.1, ABC-type phosphate transporter
[EC 3.6.3.27 created 2000, deleted 2018]
 
 
EC 3.6.3.28
Transferred entry: phosphonate-transporting ATPase. Now EC 7.3.2.2, ABC-type phosphonate transporter
[EC 3.6.3.28 created 2000, deleted 2018]
 
 
EC 3.6.3.44
Transferred entry: xenobiotic-transporting ATPase. Now EC 7.6.2.2, ABC-type xenobiotic transporter
[EC 3.6.3.44 created 2000 (EC 3.6.3.45 incorporated 2006), modified 2006, deleted 2018]
 
 
EC 3.6.3.46
Transferred entry: cadmium-transporting ATPase. Now EC 7.2.2.2, ABC-type Cd2+ transporter
[EC 3.6.3.46 created 2000, transferred 2018 to EC 7.2.2.2, deleted 2018]
 
 
EC 3.6.4.3
Transferred entry: microtubule-severing ATPase. Now EC 5.6.1.1, microtubule-severing ATPase
[EC 3.6.4.3 created 2000 as 3.6.4.3, deleted 2018]
 
 
EC 3.6.4.11
Deleted entry: nucleoplasmin ATPase. The activity has been shown not to take place.
[EC 3.6.4.11 created 2000, deleted 2018]
 
 
EC 4.1.1.3
Transferred entry: oxaloacetate decarboxylase. Now recognized to be two enzymes EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 4.1.1.112 (oxaloacetate decarboxylase).
[EC 4.1.1.3 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, deleted 2018]
 
 
EC 4.1.1.41
Transferred entry: (S)-methylmalonyl-CoA decarboxylase. Now EC 7.2.4.3, (S)-methylmalonyl-CoA decarboxylase
[EC 4.1.1.41 created 1972, modified 1983, modified 1986, deleted 2018]
 
 
*EC 4.1.1.99
Accepted name: phosphomevalonate decarboxylase
Reaction: ATP + (R)-5-phosphomevalonate = ADP + phosphate + isopentenyl phosphate + CO2
For diagram of the archaeal mevalonate pathway, click here
Systematic name: ATP:(R)-5-phosphomevalonate carboxy-lyase (adding ATP; isopentenyl-phosphate-forming)
Comments: The enzyme participates in a mevalonate pathway that occurs in archaea other than the extreme acidophiles of the Thermoplasmatales order. cf. EC 4.1.1.110, bisphosphomevalonate decarboxylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Vannice, J.C., Skaff, D.A., Keightley, A., Addo, J.K., Wyckoff, G.J. and Miziorko, H.M. Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway. J. Bacteriol. 196 (2014) 1055–1063. [DOI] [PMID: 24375100]
[EC 4.1.1.99 created 2014, modified 2018]
 
 
EC 4.1.1.112
Accepted name: oxaloacetate decarboxylase
Reaction: oxaloacetate = pyruvate + CO2
Other name(s): oxaloacetate β-decarboxylase; oxalacetic acid decarboxylase; oxalate β-decarboxylase; oxaloacetate carboxy-lyase
Systematic name: oxaloacetate carboxy-lyase (pyruvate-forming)
Comments: Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme’s involvement in Na+ transport.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9024-98-0
References:
1.  Schmitt, A., Bottke, I. and Siebert, G. Eigenschaften einer Oxaloacetat-Decarboxylase aus Dorschmuskulatur. Hoppe-Seyler's Z. Physiol. Chem. 347 (1966) 18–34. [PMID: 5972993]
2.  Herbert, D. Oxalacetic carboxylase of Micrococcus lysodeikticus. Methods Enzymol. 1 (1955) 753–757.
3.  Horton, A.A. and Kornberg, H.L. Oxaloacetate 4-carboxy-lyase from Pseudomonas ovalis chester. Biochim. Biophys. Acta 89 (1964) 381–383. [PMID: 14205502]
4.  Sender, P.D., Martin, M.G., Peiru, S. and Magni, C. Characterization of an oxaloacetate decarboxylase that belongs to the malic enzyme family. FEBS Lett. 570 (2004) 217–222. [PMID: 15251467]
5.  Narayanan, B.C., Niu, W., Han, Y., Zou, J., Mariano, P.S., Dunaway-Mariano, D. and Herzberg, O. Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily. Biochemistry 47 (2008) 167–182. [PMID: 18081320]
[EC 4.1.1.112 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, part transferred 2018 to EC 4.1.1.112]
 
 
EC 4.1.99.24
Accepted name: L-tyrosine isonitrile synthase
Reaction: L-tyrosine + D-ribulose 5-phosphate = (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate + hydroxyacetone + formaldehyde + phosphate + H2O
Glossary: (2S)-3-(4-hydroxyphenyl)-2-isocyanopropanoate = L-tyrosine isonitrile
paerucumarin = 6,7-dihydroxy-3-isocyanochromen-2-one
rhabduscin = N-[(2S,3S,4R,5S,6R)-4,5-dihydroxy-6-{4-[(E)-2-isocyanoethenyl]phenoxy}-2-methyloxan-3-yl]acetamide
Other name(s): pvcA (gene name)
Systematic name: L-tyrosine:D-ribulose-5-phosphate lyase (isonitrile-forming)
Comments: The enzymes from the bacteria Pseudomonas aeruginosa and Xenorhabdus nematophila are involved in the biosynthesis of paerucumarin and rhabduscin, respectively. According to the proposed mechanism, the enzyme forms an imine intermediate composed of linked L-tyrosine and D-ribulose 5-phosphate, followed by loss of the phosphate group and formation of a β-keto imine and keto-enol tautomerization. This is followed by a C-C bond cleavage, the release of hydroxyacetone, and a retro aldol type reaction that releases formaldehyde and forms the final product [3]. cf. EC 4.1.99.25, L-tryptophan isonitrile synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Clarke-Pearson, M.F. and Brady, S.F. Paerucumarin, a new metabolite produced by the pvc gene cluster from Pseudomonas aeruginosa. J. Bacteriol. 190 (2008) 6927–6930. [DOI] [PMID: 18689486]
2.  Drake, E.J. and Gulick, A.M. Three-dimensional structures of Pseudomonas aeruginosa PvcA and PvcB, two proteins involved in the synthesis of 2-isocyano-6,7-dihydroxycoumarin. J. Mol. Biol. 384 (2008) 193–205. [DOI] [PMID: 18824174]
3.  Chang, W.C., Sanyal, D., Huang, J.L., Ittiamornkul, K., Zhu, Q. and Liu, X. In vitro stepwise reconstitution of amino acid derived vinyl isocyanide biosynthesis: detection of an elusive intermediate. Org. Lett. 19 (2017) 1208–1211. [DOI] [PMID: 28212039]
[EC 4.1.99.24 created 2018]
 
 
EC 4.1.99.25
Accepted name: L-tryptophan isonitrile synthase
Reaction: L-tryptophan + D-ribulose 5-phosphate = (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate + hydroxyacetone + formaldehyde + phosphate + H2O
Glossary: (2S)-3-(1H-indol-3-yl)-2-isocyanopropanoate = L-tryptophan isonitrile
hydroxyacetone = 1-hydroxypropan-2-one
Other name(s): isnA (gene name); ambI1 (gene name); well1 (gene name)
Systematic name: L-tryptophan:D-ribulose-5-phosphate lyase (isonitrile-forming)
Comments: The enzymes from cyanobacteria that belong to the Nostocales order participate in the biosynthesis of hapalindole-type alkaloids. According to the proposed mechanism, the enzyme forms an imine intermediate composed of linked L-tryptophan and D-ribulose 5-phosphate, followed by loss of the phosphate group and formation of a β-keto imine and keto-enol tautomerization. This is followed by a C-C bond cleavage, the release of hydroxyacetone, and a retro aldol type reaction that releases formaldehyde and forms the final product [3]. cf. EC 4.1.99.24, L-tyrosine isonitrile synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Brady, S.F. and Clardy, J. Cloning and heterologous expression of isocyanide biosynthetic genes from environmental DNA. Angew. Chem. Int. Ed. Engl. 44 (2005) 7063–7065. [PMID: 16206308]
2.  Brady, S.F. and Clardy, J. Systematic investigation of the Escherichia coli metabolome for the biosynthetic origin of an isocyanide carbon atom. Angew. Chem. Int. Ed. Engl. 44 (2005) 7045–7048. [PMID: 16217820]
3.  Hillwig, M.L., Zhu, Q. and Liu, X. Biosynthesis of ambiguine indole alkaloids in cyanobacterium Fischerella ambigua. ACS Chem. Biol. 9 (2014) 372–377. [DOI] [PMID: 24180436]
4.  Chang, W.C., Sanyal, D., Huang, J.L., Ittiamornkul, K., Zhu, Q. and Liu, X. In vitro stepwise reconstitution of amino acid derived vinyl isocyanide biosynthesis: detection of an elusive intermediate. Org. Lett. 19 (2017) 1208–1211. [DOI] [PMID: 28212039]
[EC 4.1.99.25 created 2018]
 
 
EC 4.3.1.32
Accepted name: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
Reaction: 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil + S-adenosyl-L-methionine = 7,8-didemethyl-8-hydroxy-5-deazariboflavin + NH3 + L-methionine + 5′-deoxyadenosine
Other name(s): FO synthase; fbiC (gene name) (ambiguous); cofG (gene name)
Systematic name: 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil ammonia-lyase (7,8-didemethyl-8-hydroxy-5-deazariboflavin-forming)
Comments: The enzyme produces the 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) precursor of the redox cofactor coenzyme F420, which is found in methanogens and in various actinobacteria. FO is also produced by some cyanobacteria and eukaryotes. The enzyme, which forms a complex with EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase, is a radical SAM enzyme that uses the 5′-deoxyadenosyl radical to catalyse the condensation reaction.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Decamps, L., Philmus, B., Benjdia, A., White, R., Begley, T.P. and Berteau, O. Biosynthesis of F0, precursor of the F420 cofactor, requires a unique two radical-SAM domain enzyme and tyrosine as substrate. J. Am. Chem. Soc. 134 (2012) 18173–18176. [DOI] [PMID: 23072415]
2.  Philmus, B., Decamps, L., Berteau, O. and Begley, T.P. Biosynthetic versatility and coordinated action of 5′-deoxyadenosyl radicals in deazaflavin biosynthesis. J. Am. Chem. Soc. 137 (2015) 5406–5413. [DOI] [PMID: 25781338]
[EC 4.3.1.32 created 2010 as EC 2.5.1.77, part transferred 2018 to EC 4.3.1.32]
 
 
EC 4.3.2.10
Accepted name: imidazole glycerol-phosphate synthase
Reaction: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + L-glutamate (overall reaction)
(1a) L-glutamine + H2O = L-glutamate + NH3
(1b) 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + NH3 = 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H2O
Other name(s): IGP synthase; hisFH (gene names); HIS7 (gene name)
Systematic name: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate-lyase (L-glutamine-hydrolysing; 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide-forming)
Comments: The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 Å tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Klem, T.J. and Davisson, V.J. Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Biochemistry 32 (1993) 5177–5186. [PMID: 8494895]
2.  Fujimori, K. and Ohta, D. An Arabidopsis cDNA encoding a bifunctional glutamine amidotransferase/cyclase suppresses the histidine auxotrophy of a Saccharomyces cerevisiae his7 mutant. FEBS Lett. 428 (1998) 229–234. [PMID: 9654139]
3.  Beismann-Driemeyer, S. and Sterner, R. Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex. J. Biol. Chem 276 (2001) 20387–20396. [PMID: 11264293]
4.  Douangamath, A., Walker, M., Beismann-Driemeyer, S., Vega-Fernandez, M.C., Sterner, R. and Wilmanns, M. Structural evidence for ammonia tunneling across the (β α)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure 10 (2002) 185–193. [PMID: 11839304]
5.  Chaudhuri, B.N., Lange, S.C., Myers, R.S., Davisson, V.J. and Smith, J.L. Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme. Biochemistry 42 (2003) 7003–7012. [PMID: 12795595]
[EC 4.3.2.10 created 2018]
 
 
EC 4.3.99.2
Transferred entry: carboxybiotin decarboxylase. Now EC 7.2.4.1, carboxybiotin decarboxylase
[EC 4.3.99.2 created 2008, deleted 2018]
 
 
EC 4.4.1.6
Transferred entry: S-alkylcysteine lyase. Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase
[EC 4.4.1.6 created 1965, deleted 1972, reinstated 1976, deleted 2018]
 
 
EC 4.4.1.8
Transferred entry: cystathionine β-lyase. Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase
[EC 4.4.1.8 created 1972, deleted 2018]
 
 
EC 5.6 Isomerases altering macromolecular conformation
 
EC 5.6.1 Enzymes altering polypeptide conformation or assembly
 
EC 5.6.1.1
Accepted name: microtubule-severing ATPase
Reaction: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) α/β tubulin heterodimers
Other name(s): katanin
Systematic name: ATP phosphohydrolase (tubulin-dimerizing)
Comments: A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  McNally, F.J. and Vale, R.D. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 75 (1993) 419–429. [DOI] [PMID: 8221885]
2.  Hartman, J.J., Mahr, J., McNally, K., Okawa, K., Iwamatsu, A., Thomas, S., Cheesman, S., Heuser, J., Vale, R.D. and McNally, F.J. Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit. Cell 93 (1998) 277–287. [DOI] [PMID: 9568719]
[EC 5.6.1.1 created 2000 as 3.6.4.3, transferred 2018 to EC 5.6.1.1]
 
 
*EC 6.2.1.2
Accepted name: medium-chain acyl-CoA ligase
Reaction: ATP + a medium-chain fatty acid + CoA = AMP + diphosphate + a medium-chain acyl-CoA
Other name(s): fadK (gene name); lvaE (gene name); butyryl-CoA synthetase; fatty acid thiokinase (medium chain); acyl-activating enzyme; fatty acid elongase; fatty acid activating enzyme; fatty acyl coenzyme A synthetase; butyrate—CoA ligase; butyryl-coenzyme A synthetase; L-(+)-3-hydroxybutyryl CoA ligase; short-chain acyl-CoA synthetase; medium-chain acyl-CoA synthetase; butanoate:CoA ligase (AMP-forming)
Systematic name: medium-chain fatty acid:CoA ligase (AMP-forming)
Comments: Acts on fatty acids from C4 to C11 and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids. The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives.
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9080-51-7
References:
1.  Mahler, H.R., Wakil, S.J. and Bock, R.M. Studies on fatty acid oxidation. I. Enzymatic activation of fatty acids. J. Biol. Chem. 204 (1953) 453–468. [PMID: 13084616]
2.  Massaro, E.J. and Lennarz, W.J. The partial purification and characterization of a bacterial fatty acyl coenzyme A synthetase. Biochemistry 4 (1965) 85–90. [PMID: 14285249]
3.  Websterlt, J.R., Gerowin, L.D. and Rakita, L. Purification and characteristics of a butyryl coenzyme A synthetase from bovine heart mitochondria. J. Biol. Chem. 240 (1965) 29–33. [PMID: 14253428]
4.  Morgan-Kiss, R.M. and Cronan, J.E. The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase. J. Biol. Chem. 279 (2004) 37324–37333. [PMID: 15213221]
5.  Rand, J.M., Pisithkul, T., Clark, R.L., Thiede, J.M., Mehrer, C.R., Agnew, D.E., Campbell, C.E., Markley, A.L., Price, M.N., Ray, J., Wetmore, K.M., Suh, Y., Arkin, A.P., Deutschbauer, A.M., Amador-Noguez, D. and Pfleger, B.F. A metabolic pathway for catabolizing levulinic acid in bacteria. Nat Microbiol 2 (2017) 1624–1634. [PMID: 28947739]
[EC 6.2.1.2 created 1961, modified 2011, modified 2018]
 
 
EC 7 Translocases
 
EC 7.1 Catalysing the translocation of hydrons
 
EC 7.1.1 Linked to oxidoreductase reactions
 
EC 7.1.1.1
Accepted name: proton-translocating NAD(P)+ transhydrogenase
Reaction: NADPH + NAD+ + H+[side 1] = NADP+ + NADH + H+[side 2]
Other name(s): pntA (gene name); pntB (gene name); NNT (gene name)
Systematic name: NADPH:NAD+ oxidoreductase (H+-transporting)
Comments: The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Clarke, D.M. and Bragg, P.D. Cloning and expression of the transhydrogenase gene of Escherichia coli. J. Bacteriol. 162 (1985) 367–373. [PMID: 3884596]
2.  Clarke, D.M. and Bragg, P.D. Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 149 (1985) 517–523. [DOI] [PMID: 3891338]
3.  Glavas, N.A., Hou, C. and Bragg, P.D. Involvement of histidine-91 of the β subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 34 (1995) 7694–7702. [PMID: 7779816]
4.  Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. and Fischer, E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613–6619. [DOI] [PMID: 14660605]
5.  Bizouarn, T., Fjellstrom, O., Meuller, J., Axelsson, M., Bergkvist, A., Johansson, C., Goran Karlsson, B. and Rydstrom, J. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim. Biophys. Acta 1457 (2000) 211–228. [DOI] [PMID: 10773166]
6.  White, S.A., Peake, S.J., McSweeney, S., Leonard, G., Cotton, N.P. and Jackson, J.B. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure 8 (2000) 1–12. [PMID: 10673423]
7.  Johansson, T., Oswald, C., Pedersen, A., Tornroth, S., Okvist, M., Karlsson, B.G., Rydstrom, J. and Krengel, U. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 352 (2005) 299–312. [DOI] [PMID: 16083909]
8.  Meimaridou, E., Kowalczyk, J., Guasti, L., Hughes, C.R., Wagner, F., Frommolt, P., Nurnberg, P., Mann, N.P., Banerjee, R., Saka, H.N., Chapple, J.P., King, P.J., Clark, A.J. and Metherell, L.A. Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency. Nat. Genet. 44 (2012) 740–742. [DOI] [PMID: 22634753]
[EC 7.1.1.1 created 2015 as EC 1.6.1.5, transferred 2018 to EC 7.1.1.1]
 
 
EC 7.1.1.2
Accepted name: NADH:ubiquinone reductase (H+-translocating)
Reaction: NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]
Other name(s): ubiquinone reductase (ambiguous); type 1 dehydrogenase; complex 1 dehydrogenase; coenzyme Q reductase (ambiguous); complex I (electron transport chain); complex I (mitochondrial electron transport); complex I (NADH:Q1 oxidoreductase); dihydronicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); DPNH-coenzyme Q reductase (ambiguous); DPNH-ubiquinone reductase (ambiguous); mitochondrial electron transport complex 1; mitochondrial electron transport complex I; NADH coenzyme Q1 reductase; NADH-coenzyme Q oxidoreductase (ambiguous); NADH-coenzyme Q reductase (ambiguous); NADH-CoQ oxidoreductase (ambiguous); NADH-CoQ reductase (ambiguous); NADH-ubiquinone reductase (ambiguous); NADH-ubiquinone oxidoreductase (ambiguous); NADH-ubiquinone-1 reductase; reduced nicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); NADH:ubiquinone oxidoreductase complex; NADH-Q6 oxidoreductase (ambiguous); electron transfer complex I; NADH2 dehydrogenase (ubiquinone)
Systematic name: NADH:ubiquinone oxidoreductase
Comments: A flavoprotein (FMN) containing iron-sulfur clusters. The complex is present in mitochondria and aerobic bacteria. Breakdown of the complex can release EC 1.6.99.3, NADH dehydrogenase. In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD+ to NADH.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9028-04-0
References:
1.  Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1–70.
2.  Herter, S.M., Kortluke, C.M. and Drews, G. Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169 (1998) 98–105. [PMID: 9446680]
3.  Hunte, C., Zickermann, V. and Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329 (2010) 448–451. [DOI] [PMID: 20595580]
4.  Efremov, R.G., Baradaran, R. and Sazanov, L.A. The architecture of respiratory complex I. Nature 465 (2010) 441–445. [DOI] [PMID: 20505720]
5.  Wikstrom, M. and Hummer, G. Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications. Proc. Natl. Acad. Sci. USA 109 (2012) 4431–4436. [DOI] [PMID: 22392981]
[EC 7.1.1.2 created 1961 as EC 1.6.5.3, deleted 1965, reinstated 1983, modified 2011, modified 2013, transferred 2018 to EC 7.1.1.2]
 
 
EC 7.1 Catalysing the translocation of hydrons
 
EC 7.1.2 Linked to the hydrolysis of a nucleoside triphosphate
 
EC 7.1.2.1
Accepted name: P-type H+-exporting transporter
Reaction: ATP + H2O + H+[side 1] = ADP + phosphate + H+[side 2]
Other name(s): proton-translocating ATPase; yeast plasma membrane H+-ATPase; yeast plasma membrane ATPase; ATP phosphohydrolase (ambiguous); proton-exporting ATPase; proton transport ATPase; proton-translocating P-type ATPase; H+-transporting ATPase
Systematic name: ATP phosphohydrolase (P-type, H+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Goffeau, A. and Slayman, C. The proton-translocating ATPase of the fungal plasma membrane. Biochim. Biophys. Acta 639 (1981) 197–223. [PMID: 6461354]
2.  Serrano, R., Kielland-Brandt, M.C. and Fink, G.R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+)-, K+-and Ca2+-ATPases. Nature 319 (1986) 689–693. [DOI] [PMID: 3005867]
3.  Serrano, R. and Portillo, F. Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018 (1990) 195–199. [DOI] [PMID: 2144186]
4.  Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53–61. [PMID: 2425739]
[EC 7.1.2.1 created 1984 as EC 3.6.1.35, transferred 2000 to EC 3.6.3.6, transferred 2018 to EC 7.1.2.1]
 
 
EC 7.1.2.2
Accepted name: H+-transporting two-sector ATPase
Reaction: ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]
Glossary: In Fo, the "o" refers to oligomycin. F0 is incorrect
Other name(s): ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (Fo, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase
Systematic name: ATP phosphohydrolase (two-sector, H+-transporting)
Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53–61. [PMID: 2425739]
2.  Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215–250. [DOI] [PMID: 8417777]
3.  Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621–628. [DOI] [PMID: 8065448]
4.  Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17–32. [DOI] [PMID: 8581162]
5.  Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299–302. [DOI] [PMID: 9069291]
6.  Turina, P., Samoray, D. and Graber, P. H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes. EMBO J. 22 (2003) 418–426. [PMID: 12554643]
[EC 7.1.2.2 created 1984 as EC 3.6.1.34, transferred 2000 to EC 3.6.3.14, transferred 2018 to EC 7.1.2.2]
 
 
EC 7.1 Catalysing the translocation of hydrons
 
EC 7.1.3 Linked to the hydrolysis of diphosphate
 
EC 7.1.3.1
Accepted name: H+-exporting diphosphatase
Reaction: diphosphate + H2O + H+[side 1] = 2 phosphate + H+[side 2]
Other name(s): H+-PPase; proton-pumping pyrophosphatase; vacuolar H+-pyrophosphatase; hydrogen-translocating pyrophosphatase; proton-pumping dihosphatase
Systematic name: diphosphate phosphohydrolase (H+-transporting)
Comments: This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Rea, P.A. and Poole, R.J. Chromatographic resolution of H+-translocating pyrophosphatase from H+-translocating ATPase of higher plant tonoplast. Plant Physiol. 81 (1986) 126–129. [PMID: 16664761]
2.  Sarafian, V. and Poole, R.J. Purification of an H+-translocating inorganic pyrophosphatase from vacuole membranes of red beet. Plant Physiol. 91 (1989) 34–38. [PMID: 16667022]
3.  Hedrich, R., Kurkdjian, A., Guern, J. and Flugge, U.I. Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J. 8 (1989) 2835–2841. [PMID: 2479537]
4.  Segami, S., Tomoyama, T., Sakamoto, S., Gunji, S., Fukuda, M., Kinoshita, S., Mitsuda, N., Ferjani, A. and Maeshima, M. Vacuolar H+-pyrophosphatase and cytosolic soluble pyrophosphatases cooperatively regulate pyrophosphate levels in Arabidopsis thaliana. Plant Cell 30 (2018) 1040–1061. [PMID: 29691313]
[EC 7.1.3.1 created 2018]
 
 
EC 7.2 Catalysing the translocation of inorganic cations
 
EC 7.2.1 Linked to oxidoreductase reactions
 
EC 7.2.1.1
Accepted name: NADH:ubiquinone reductase (Na+-transporting)
Reaction: NADH + H+ + ubiquinone + n Na+[side 1] = NAD+ + ubiquinol + n Na+[side 2]
Other name(s): Na+-translocating NADH-quinone reductase; Na+-NQR
Systematic name: NADH:ubiquinone oxidoreductase (Na+-translocating)
Comments: An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Beattie, P., Tan, K., Bourne, R.M., Leach, D., Rich, P.R. and Ward, F.B. Cloning and sequencing of four structural genes for the Na+-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 356 (1994) 333–338. [DOI] [PMID: 7805867]
2.  Nakayama, Y., Hayashi, M. and Unemoto, T. Identification of six subunits constituting Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. FEBS Lett. 422 (1998) 240–242. [DOI] [PMID: 9490015]
3.  Bogachev, A.V., Bertsova, Y.V., Barquera, B. and Verkhovsky, M.I. Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry 40 (2001) 7318–7323. [DOI] [PMID: 11401580]
4.  Barquera, B., Hellwig, P., Zhou, W., Morgan, J.E., Hase, C.C., Gosink, K.K., Nilges, M., Bruesehoff, P.J., Roth, A., Lancaster, C.R. and Gennis, R.B. Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry 41 (2002) 3781–3789. [DOI] [PMID: 11888296]
5.  Barquera, B., Nilges, M.J., Morgan, J.E., Ramirez-Silva, L., Zhou, W. and Gennis, R.B. Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Biochemistry 43 (2004) 12322–12330. [DOI] [PMID: 15379571]
[EC 7.2.1.1 created 2011 as EC 1.6.5.8, transferred 2018 to EC 7.2.1.1]
 
 
EC 7.2.1.2
Accepted name: ferredoxin—NAD+ oxidoreductase (Na+-transporting)
Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]
Other name(s): Rnf complex (ambiguous); Na+-translocating ferredoxin:NAD+ oxidoreductase
Systematic name: ferredoxin:NAD+ oxidoreductase (Na+-transporting)
Comments: This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Biegel, E., Schmidt, S. and Muller, V. Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii. Environ Microbiol 11 (2009) 1438–1443. [DOI] [PMID: 19222539]
2.  Biegel, E. and Muller, V. Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase. Proc. Natl. Acad. Sci. USA 107 (2010) 18138–18142. [DOI] [PMID: 20921383]
3.  Hess, V., Schuchmann, K. and Muller, V. The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential. J. Biol. Chem. 288 (2013) 31496–31502. [DOI] [PMID: 24045950]
[EC 7.2.1.2 created 2015 as EC 1.18.1.8, transferred 2018 to EC 7.2.1.2]
 
 
EC 7.2 Catalysing the translocation of inorganic cations
 
EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
 
*EC 7.2.2.1 – public review until 30 November 2018 [Last modified: 2018-09-29 07:04:44]
Accepted name: Na+-transporting two-sector ATPase
Reaction: ATP + H2O + n Na+[side 1] = ADP + phosphate + n Na+[side 2]
Other name(s): sodium-transporting two-sector ATPase; Na+-translocating ATPase; Na+-translocating FoF1-ATPase; sodium ion specific ATP synthase
Systematic name: ATP phosphohydrolase (two-sector, Na+-transporting)
Comments: A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H+-transporting two-sector ATPase) but pumps Na+ rather than H+. By analogy to EC 7.1.2.2, it is likely that the enzyme pumps 4 sodium ions for every ATP molecule that is hydrolysed. cf. EC 7.2.2.3, P-type Na+ transporter and EC 7.2.2.4, ABC-type Na+ transporter.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Solioz, M. and Davies, K. Operon of vacuolar-type Na+-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453–9459. [PMID: 8144530]
2.  Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037–11044. [PMID: 8157629]
3.  Rahlfs, S. and Müller, V. Sequence of subunit c of the Na+-translocating F1Fo-ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269–271. [DOI] [PMID: 9119076]
[EC 7.2.2.1 created 2000 as EC 3.6.3.15, transferred 2018 to EC 7.2.2.1, modified 2018]
 
 
EC 7.2.2.2
Accepted name: ABC-type Cd2+ transporter
Reaction: ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2]
Other name(s): cadmium-transporting ATPase (ambiguous); ABC-type cadmium-transporter
Systematic name: ATP phosphohydrolase (ABC-type, heavy-metal-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509–6517. [DOI] [PMID: 8626454]
2.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.2.2.2 created 2000 as EC 3.6.3.46, transferred 2018 to EC 7.2.2.2]
 
 
EC 7.2.2.3
Accepted name: P-type Na+ transporter
Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]
Other name(s): Na+-exporting ATPase (ambiguous); ENA1 (gene name); ENA2 (gene name); ENA5 (gene name); sodium transport ATPase (ambiguous); sodium-translocating P-type ATPase
Systematic name: ATP phosphohydrolase (P-type, Na+-exporting)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed. Some forms can also export Li+ ions. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.4, ABC-type Na+ transporter.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wieland, J., Nitsche, A.M., Strayle, J., Steiner, H. and Rudolph, H.K. The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane. EMBO J. 14 (1995) 3870–3882. [PMID: 7664728]
2.  Catty, P., de Kerchove d'Exaerde, A. and Goffeau, A. The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett. 409 (1997) 325–332. [DOI] [PMID: 9224683]
3.  Benito, B., Quintero, F.J. and Rodriguez-Navarro, A. Overexpression of the sodium ATPase of Saccharomyces cerevisiae: conditions for phosphorylation from ATP and Pi. Biochim. Biophys. Acta 1328 (1997) 214–226. [PMID: 9315618]
4.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.2.2.3 created 2000, as EC 3.6.3.7, modified 2001, transferred 20018 to EC 7.2.2.3]
 
 
EC 7.2.2.4
Accepted name: ABC-type Na+ transporter
Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]
Other name(s): natAB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, Na+-exporting)
Comments: ABC-type (ATP-binding cassette-type) transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This bacterial enzyme, characterized from Bacillus subtilis, exports Na+ ions out of the cell. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.3, P-type Na+ transporter.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Cheng, J., Guffanti, A.A. and Krulwich, T.A. A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23 (1997) 1107–1120. [DOI] [PMID: 9106203]
2.  Ogura, M., Tsukahara, K., Hayashi, K. and Tanaka, T. The Bacillus subtilis NatK-NatR two-component system regulates expression of the natAB operon encoding an ABC transporter for sodium ion extrusion. Microbiology 153 (2007) 667–675. [PMID: 17322186]
[EC 7.2.2.4 created 2018]
 
 
EC 7.2 Catalysing the translocation of inorganic cations
 
EC 7.2.4 Linked to decarboxylation
 
EC 7.2.4.1
Accepted name: carboxybiotin decarboxylase
Reaction: a carboxybiotinyl-[protein] + n Na+[side 1] + H+[side 2] = CO2 + a biotinyl-[protein] + n Na+[side 2] (n = 1–2)
For diagram of the reactions involved in the multienzyme complex malonate decarboxylase, click here
Other name(s): MadB; carboxybiotin protein decarboxylase
Systematic name: carboxybiotinyl-[protein] carboxy-lyase
Comments: The integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 7.2.4.3 [(S)-methylmalonyl-CoA decarboxylase (sodium-transporting)] [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103–115. [DOI] [PMID: 9128730]
2.  Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3–10. [DOI] [PMID: 11902724]
[EC 7.2.4.1 created 2008 as EC 4.3.99.2, transferred 2018 to EC 7.2.4.1]
 
 
EC 7.2.4.2
Accepted name: oxaloacetate decarboxylase (Na+ extruding)
Reaction: oxaloacetate + 2 Na+[side 1] = pyruvate + CO2 + 2 Na+[side 2]
Other name(s): oxaloacetate β-decarboxylase (ambiguous); oxalacetic acid decarboxylase (ambiguous); oxalate β-decarboxylase (ambiguous); oxaloacetate carboxy-lyase (ambiguous)
Systematic name: oxaloacetate carboxy-lyase (pyruvate-forming; Na+-extruding)
Comments: The enzyme from the bacterium Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+. Differs from EC 4.1.1.112 (oxaloacetate decarboxylase) for which there is no evidence for involvement in Na+ transport.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9024-98-0
References:
1.  Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353–358. [DOI] [PMID: 7016536]
2.  Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435–441. [DOI] [PMID: 7037395]
[EC 7.2.4.2 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, transferred 2018 to EC 7.2.4.2]
 
 
EC 7.2.4.3
Accepted name: (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
Reaction: (S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]
Other name(s): methylmalonyl-coenzyme A decarboxylase (ambiguous); (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase (ambiguous)
Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)
Comments: This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37289-44-4
References:
1.  Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253–1261. [PMID: 5646172]
2.  Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584–585. [PMID: 7070502]
3.  Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645–650. [DOI] [PMID: 2920730]
4.  Huder, J.B. and Dimroth, P. Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli. J. Bacteriol. 177 (1995) 3623–3630. [PMID: 7601825]
5.  Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. and Dimroth, P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250 (1997) 590–599. [PMID: 9428714]
[EC 7.2.4.3 created 1972 as EC 4.1.1.41, modified 1983, modified 1986, transferred 2018 to EC 7.2.4.3]
 
 
EC 7.3 Catalysing the translocation of inorganic anions and their chelates
 
EC 7.3.2 Linked to the hydrolysis of a nucleoside triphosphate
 
EC 7.3.2.1
Accepted name: ABC-type phosphate transporter
Reaction: ATP + H2O + phosphate-[phosphate-binding protein][side 1] = ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
Other name(s): phosphate ABC transporter; phosphate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, phosphate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions. Unlike P-type ATPases, it does not undergo phosphorylation during the transport process.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Webb, D.C., Rosenberg, H. and Cox, G.B. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices. J. Biol. Chem. 267 (1992) 24661–24668. [PMID: 1447208]
2.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.  Braibant, M., LeFevre, P., de Wit, L., Ooms, J., Peirs, P., Huygen, K., Wattiez, R. and Content, J. Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter. FEBS Lett. 394 (1996) 206–212. [DOI] [PMID: 8843165]
4.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
5.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.3.2.1 created 2000 as EC 3.6.3.27, transferred 2018 to EC 7.3.2.1]
 
 
EC 7.3.2.2
Accepted name: ABC-type phosphonate transporter
Reaction: ATP + H2O + phosphonate-[phosphonate-binding protein][side 1] = ADP + phosphate + phosphonate[side 2] + [phosphonate-binding protein][side 1]
Other name(s): phosphonate-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (ABC-type, phosphonate-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of phosphonate and organophosphate anions.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wanner, B.L. and Metcalf, W.W. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79 (1992) 133–139. [PMID: 1335942]
2.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.3.2.2 created 2000 as EC 3.6.3.28, transferred 2018 to EC 7.3.2.2]
 
 
EC 7.4 Catalysing the translocation of amino acids and peptides
 
EC 7.4.2 Linked to the hydrolysis of a nucleoside triphosphate
 
EC 7.4.2.1
Accepted name: ABC-type polar-amino-acid transporter
Reaction: ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1] = ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
Glossary: nopaline = N-{(1R)-1-carboxy-4-[(diaminomethylene)amino]butyl}-L-glutamate
Other name(s): histidine permease; polar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polar-amino-acid-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.  Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745–27752. [DOI] [PMID: 9346917]
3.  Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397–401. [DOI] [PMID: 9315727]
4.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.4.2.1 created 2000 as EC 3.6.3.21, transferred 2018 to EC 7.4.2.1]
 
 
EC 7.4.2.2
Accepted name: ABC-type nonpolar-amino-acid transporter
Reaction: ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1] = ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
Other name(s): nonpolar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, nonpolar-amino-acid-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein. This entry comprises enzymes that import Leu, Ile and Val.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
3.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.4.2.2 created 2000 as EC 3.6.3.22, transferred 2018 to EC 7.4.2.2]
 
 
EC 7.5 Catalysing the translocation of carbohydrates and their derivatives
 
EC 7.5.2 Linked to the hydrolysis of a nucleoside triphosphate
 
EC 7.5.2.1
Accepted name: ABC-type maltose transporter
Reaction: ATP + H2O + maltose-[maltose-binding protein][side 1] = ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Other name(s): maltose ABC transporter; maltose-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, maltose-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of maltose and maltose oligosaccharides.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67–113. [DOI] [PMID: 1282354]
2.  Dassa, E. and Muir, S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7 (1993) 29–38. [DOI] [PMID: 8437518]
3.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
4.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
5.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.5.2.1 created 2000 as EC 3.6.3.19, transferred 2018 to EC 7.5.2.1]
 
 
EC 7.5.2.2
Accepted name: ABC-type oligosaccharide transporter
Reaction: ATP + H2O + oligosaccharide-[oligosaccharide-binding protein][side 1] = ADP + phosphate + oligosaccharide[side 2] + [oligosaccharide-binding protein][side 1]
Other name(s): oligosaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, oligosaccharide-importing)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of lactose, melibiose and raffinose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67–113. [DOI] [PMID: 1282354]
2.  Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755–1768. [DOI] [PMID: 1630315]
3.  Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320–346. [PMID: 8336670]
4.  Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
5.  Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
[EC 7.5.2.2 created 2000 as EC 3.6.3.18, transferred 2018 to EC 7.5.2.2]
 
 
EC 7.6 Catalysing the translocation of other compounds
 
EC 7.6.2 Linked to the hydrolysis of a nucleoside triphosphate
 
EC 7.6.2.1
Accepted name: P-type phospholipid transporter
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous); phospholipid-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme moves phospholipids such as phosphatidylcholine, phosphatidylserine, and phosphatidylethanolamine from one membrane face to the other (’flippase’).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823–832. [PMID: 8136700]
2.  Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95–102. [PMID: 8839453]
3.  Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429–10434. [DOI] [PMID: 9099684]
4.  Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938–10942. [DOI] [PMID: 7971987]
5.  Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632–1642. [DOI] [PMID: 16452632]
6.  Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791–801. [DOI] [PMID: 20053675]
[EC 7.6.2.1 created 2000 as EC 3.6.3.1 (EC 3.6.3.13 created 2000, incorporated 2001), transferred 2018 to EC 7.6.2.1]
 
 
EC 7.6.2.2
Accepted name: ABC-type xenobiotic transporter
Reaction: ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
Other name(s): xenobiotic-transporting ATPase; multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting)
Systematic name: ATP phosphohydrolase (ABC-type, xenobiotic-exporting)
Comments: An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione—drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some ’flippase’ activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161–183. [DOI] [PMID: 8725386]
2.  Frijters, C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzyme Regul. 36 (1996) 351–363. [DOI] [PMID: 8869755]
3.  Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321–333. [DOI] [PMID: 9381978]
4.  Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130–5136. [PMID: 9823323]
5.  van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31–36. [DOI] [PMID: 9693718]
6.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
7.  Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320–329. [PMID: 7614555]
8.  Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536–1543. [DOI] [PMID: 7883711]
9.  Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271 (1996) 25167–25172. [DOI] [PMID: 8810273]
[EC 7.6.2.2 created 2000 as EC 3.6.3.44 (EC 3.6.3.45 incorporated 2006), modified 2006, transferred 2018 to EC 7.6.2.2]
 
 
EC 7.6.2.3
Accepted name: ABC-type glutathione-S-conjugate transporter
Reaction: ATP + H2O + glutathione-S-conjugate[side 1] = ADP + phosphate + glutathione-S-conjugate[side 2]
Other name(s): multidrug resistance-associated protein 1; glutathione-S-conjugate-translocating ATPase; MRP; MRP1; ABCC1 (gene name); YBT1 (gene name); YCF1 (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, glutathione-S-conjugate-exporting)
Comments: A eukaryotic ATP-binding cassette (ABC) type transporter that mediates the transport of glutathione-S-conjugates. The mammalian enzyme, which also transports some glucuronides, exports the substrates out of the cell, while plant and fungal transporters export them into the vacuole. Over-expression confers resistance to anticancer drugs by their efficient exportation in glutathione-S-conjugate form.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zaman, G.J., Flens, M.J., van Leusden, M.R., de Haas, M., Mulder, H.S., Lankelma, J., Pinedo, H.M., Scheper, R.J., Baas, F., Broxterman, H.J. and et al. The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump. Proc. Natl Acad. Sci. USA 91 (1994) 8822–8826. [PMID: 7916458]
2.  Lautier, D., Canitrot, Y., Deeley, R.G. and Cole, S.P. Multidrug resistance mediated by the multidrug resistance protein (MRP) gene. Biochem. Pharmacol. 52 (1996) 967–977. [PMID: 8831715]
3.  Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509–6517. [DOI] [PMID: 8626454]
4.  Lu, Y.P., Li, Z.S. and Rea, P.A. AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl Acad. Sci. USA 94 (1997) 8243–8248. [PMID: 9223346]
5.  Cole, S.P. Multidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter. J. Biol. Chem 289 (2014) 30880–30888. [PMID: 25281745]
6.  Cordente, A.G., Capone, D.L. and Curtin, C.D. Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one. Appl. Microbiol. Biotechnol. 99 (2015) 9709–9722. [PMID: 26227410]
[EC 7.6.2.3 created 2018]
 
 


Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald