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 To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.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 1.3.3.9 transferred
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 1.14.13.133 transferred
EC 1.14.13.134 transferred
EC 1.14.13.137 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 1.14.15.31 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 1.14.21.1 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 1.14.99.49 transferred
EC 1.17.9.1 4-methylphenol dehydrogenase (hydroxylating)
EC 1.17.99.1 transferred


EC 1.3.3.9 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
Transferred entry: secologanin synthase. Now EC 1.14.19.62, secologanin synthase
[EC 1.3.3.9 created 2002, deleted 2018]
 
 
EC 1.14.13.11 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
Transferred entry: germacrene A hydroxylase. Now EC 1.14.14.95, germacrene A hydroxylase
[EC 1.14.13.123 created 2011, deleted 2018]
 
 
EC 1.14.13.133 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
Transferred entry: indole-2-monooxygenase. Now EC 1.14.14.153, indole-2-monooxygenase
[EC 1.14.13.137 created 2012, deleted 2018]
 
 
EC 1.14.13.139 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 31 July 2018 [Last modified: 2018-07-03 04:43:31]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:36:44]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 10:02:44]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 10:11:02]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 26 July 2018 [Last modified: 2018-06-28 10:23:49]
Accepted name: licodione synthase
Reaction: liquiritigenin + [reduced NADPH—hemoprotein reductase] + O2 = licodione + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of licodione biosynthesis, click here
Glossary: licodione = 1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)propane-1,3-dione
Other name(s): (2S)-flavanone 2-hydroxylase; CYP93B1
Systematic name: liquiritigenin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (licodione-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The immediate product is likely 2-hydroxyliquiritigenin, which spontaneously rearranges to form licodione.
References:
1.  Otani, K., Takahashi, T., Furuya, T. and Ayabe, S. Licodione synthase, a cytochrome P450 monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol. 105 (1994) 1427–1432. [PMID: 12232298]
2.  Akashi, T., Aoki, T. and Ayabe, S. Identification of a cytochrome P450 cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431 (1998) 287–290. [DOI] [PMID: 9708921]
[EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140]
 
 
EC 1.14.14.141 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 10:32:50]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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′.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-07-13 10:03:32]
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).
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 – public review until 26 July 2018 [Last modified: 2018-07-16 04:32:52]
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-hydroxysteroid + [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.
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 1.14.15.31 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-07-12 03:30:43]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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).
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-07-10 03:26:08]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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].
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 – public review until 26 July 2018 [Last modified: 2018-07-12 03:57:43]
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
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 1.14.21.1 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 31 July 2018 [Last modified: 2018-07-03 04:44:09]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 1.14.99.49 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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 1.17.9.1 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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.
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 – public review until 26 July 2018 [Last modified: 2018-06-28 06:29:00]
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]
 
 


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