The Enzyme Database

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

Proposed Changes to the Enzyme List

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 To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

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


Contents

*EC 1.1.1.44 phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)
EC 1.1.1.158 transferred
*EC 1.1.1.272 D-2-hydroxyacid dehydrogenase (NADP+)
*EC 1.1.1.274 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
EC 1.1.1.343 phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
EC 1.1.1.344 dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+]
EC 1.1.1.345 D-2-hydroxyacid dehydrogenase (NAD+)
EC 1.1.1.346 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
EC 1.3.1.26 transferred
EC 1.3.1.98 UDP-N-acetylmuramate dehydrogenase
EC 1.3.1.99 iridoid synthase
EC 1.5.1.46 agroclavine dehydrogenase
EC 1.7.3.4 transferred
EC 1.7.3.6 hydroxylamine oxidase (cytochrome)
*EC 1.11.1.6 catalase
EC 1.11.1.22 hydroperoxy fatty acid reductase
*EC 1.12.1.3 hydrogen dehydrogenase (NADP+)
EC 1.12.1.5 hydrogen dehydrogenase [NAD(P)+]
EC 1.12.98.4 sulfhydrogenase
*EC 1.13.11.37 hydroxyquinol 1,2-dioxygenase
EC 1.13.12.20 noranthrone monooxygenase
*EC 1.14.13.70 sterol 14α-demethylase
*EC 1.14.15.6 cholesterol monooxygenase (side-chain-cleaving)
EC 1.14.15.12 pimeloyl-[acyl-carrier protein] synthase
*EC 1.14.99.9 steroid 17α-monooxygenase
*EC 1.14.99.10 steroid 21-monooxygenase
EC 1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductase
EC 1.23.1 With NADH or NADPH as donor (only sub-subclass identified to date)
EC 1.23.1.1 (+)-pinoresinol reductase
EC 1.23.1.2 (+)-lariciresinol reductase
EC 1.23.1.3 (–)-pinoresinol reductase
EC 1.23.1.4 (–)-lariciresinol reductase
EC 1.97.1.3 transferred
*EC 2.1.1.132 precorrin-6B C5,15-methyltransferase (decarboxylating)
EC 2.1.1.149 deleted
EC 2.1.1.266 23S rRNA (adenine2030-N6)-methyltransferase
EC 2.1.1.267 flavonoid 3′,5′-methyltransferase
EC 2.1.1.268 tRNAThr (cytosine32-N3)-methyltransferase
*EC 2.3.1.25 plasmalogen synthase
*EC 2.3.1.47 8-amino-7-oxononanoate synthase
EC 2.3.1.104 deleted
*EC 2.3.1.140 rosmarinate synthase
*EC 2.3.1.151 2,3′,4,6-tetrahydroxybenzophenone synthase
*EC 2.3.1.153 anthocyanin 5-(6′′′-hydroxycinnamoyltransferase)
EC 2.3.1.211 bisdemethoxycurcumin synthase
EC 2.3.1.212 benzalacetone synthase
EC 2.3.1.213 cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase
EC 2.3.1.214 pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4′′′-malonyltransferase
EC 2.3.1.215 anthocyanidin 3-O-glucoside 6′′-O-acyltransferase
EC 2.3.1.216 5,7-dihydroxy-2-methylchromone synthase
EC 2.3.1.217 curcumin synthase
EC 2.3.1.218 phenylpropanoylacetyl-CoA synthase
EC 2.3.1.219 demethoxycurcumin synthase
EC 2.3.1.220 2,4,6-trihydroxybenzophenone synthase
EC 2.3.1.221 noranthrone synthase
EC 2.3.1.222 phosphate propanoyltransferase
*EC 2.3.2.1 D-glutamyltransferase
*EC 2.4.1.62 ganglioside galactosyltransferase
*EC 2.4.1.116 cyanidin 3-O-rutinoside 5-O-glucosyltransferase
*EC 2.4.1.238 delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase
*EC 2.4.1.275 neolactotriaosylceramide β-1,4-galactosyltransferase
EC 2.4.1.294 cyanidin 3-O-galactosyltransferase
EC 2.4.1.295 anthocyanin 3-O-sambubioside 5-O-glucosyltransferase
EC 2.4.1.296 anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase
EC 2.4.1.297 anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase
EC 2.4.1.298 anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
EC 2.4.1.299 cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)
EC 2.4.1.300 cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)
EC 2.4.2.49 neamine phosphoribosyltransferase
EC 2.4.2.50 cyanidin 3-O-galactoside 2′′-O-xylosyltransferase
EC 2.4.2.51 anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase
EC 2.6.1.100 L-glutamine:2-deoxy-scyllo-inosose aminotransferase
EC 2.6.1.101 L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
EC 2.7.7.84 2′-5′ oligoadenylate synthase
EC 2.7.8.38 archaetidylserine synthase
EC 3.1.4.55 phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
EC 3.1.7.4 deleted
EC 3.5.4.33 tRNA(adenine34) deaminase
EC 3.5.4.34 tRNAAla(adenine37) deaminase
EC 3.5.4.35 tRNA(cytosine8) deaminase
EC 3.5.4.36 mRNA(cytosine6666) deaminase
EC 3.6.1.64 inosine diphosphate phosphatase
EC 4.1.3.42 (4S)-4-hydroxy-2-oxoglutarate aldolase
EC 4.2.3.141 sclareol synthase
EC 4.2.3.142 7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
EC 4.3.99.4 choline trimethylamine-lyase
EC 4.7 carbon-phosphorus lyases
EC 4.7.1 carbon-phosphorus lyases (only sub-subclass identified to date)
EC 4.7.1.1 α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase
EC 5.3.2.7 ascopyrone tautomerase
EC 5.3.2.8 4-oxalomesaconate tautomerase
EC 5.3.3.15 transferred
EC 5.3.3.16 transferred
EC 5.4.3.10 phenylalanine aminomutase (L-β-phenylalanine forming)
EC 5.4.3.11 phenylalanine aminomutase (D-β-phenylalanine forming)
*EC 6.3.1.14 diphthine—ammonia ligase


*EC 1.1.1.44
Accepted name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)
Reaction: 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH + H+
For diagram of the pentose phosphate pathway (early stages), click here
Other name(s): phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase
Systematic name: 6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating)
Comments: The enzyme participates in the oxidative branch of the pentose phosphate pathway, whose main purpose is to produce NADPH and pentose for biosynthetic reactions. Highly specific for NADP+. cf. EC 1.1.1.343, phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9073-95-4
References:
1.  Dickens, F. and Glock, G.E. Direct oxidation of glucose-6-phosphate, 6-phosphogluconate and pentose-5-phosphate by enzymes of animal origin. Biochem. J. 50 (1951) 81–95. [PMID: 14904376]
2.  Pontremoli, S., de Flora, A., Grazi, E., Mangiarotti, G., Bonsignore, A. and Horecker, B.L. Purification and properties of β-L-hydroxy acid dehydrogenase. II. Isolation of β-keto-L-gluconic acid, an intermediate in L-xylulose biosynthesis. J. Biol. Chem. 236 (1961) 2975–2980. [PMID: 14487824]
3.  Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 1. The isolation and properties of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Biochem. J. 55 (1953) 23–33. [PMID: 13093611]
4.  Scott, D.B.M. and Cohen, S.S. The oxidative pathway of carbohydrate metabolism in Escherichia coli. 5. Isolation and identification of ribulose phosphate produced from 6-phosphogluconate by the dehydrogenase of E. coli. Biochem. J. 65 (1957) 686–689. [PMID: 13426085]
5.  Bridges, R.B., Palumbo, M.P. and Wittenberger, C.L. Purification and properties of an NADP-specific 6-phosphogluconate dehydrogenase from Streptococcus faecalis. J. Biol. Chem. 250 (1975) 6093–6100. [PMID: 238996]
6.  Yoon, H., Anderson, C.D. and Anderson, B.M. Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Biochim. Biophys. Acta 994 (1989) 75–80. [PMID: 2783298]
7.  Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528–4534. [PMID: 15231785]
[EC 1.1.1.44 created 1961, modified 2013]
 
 
EC 1.1.1.158
Transferred entry: UDP-N-acetylmuramate dehydrogenase. Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase
[EC 1.1.1.158 created 1976, modified 1983, modified 2002, deleted 2013]
 
 
*EC 1.1.1.272
Accepted name: D-2-hydroxyacid dehydrogenase (NADP+)
Reaction: an (R)-2-hydroxycarboxylate + NADP+ = a 2-oxocarboxylate + NADPH + H+
For diagram of coenzyme M biosynthesis, click here
Other name(s): ddh (gene name)
Systematic name: (R)-2-hydroxycarboxylate:NADP+ oxidoreductase
Comments: This enzyme, characterized from the halophilic archaeon Haloferax mediterranei and the mold Aspergillus oryzae, catalyses a stereospecific reduction of 2-oxocarboxylic acids into the corresponding D-2-hydroxycarboxylic acids. The enzyme prefers substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain, and can use NADH with much lower efficiency. cf. EC 1.1.1.345, (D)-2-hydroxyacid dehydrogenase (NAD+).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 81210-65-3
References:
1.  Domenech, J. and Ferrer, J. A new D-2-hydroxyacid dehydrogenase with dual coenzyme-specificity from Haloferax mediterranei, sequence analysis and heterologous overexpression. Biochim. Biophys. Acta 1760 (2006) 1667–1674. [PMID: 17049749]
2.  Shimizu, M., Yamamoto, T., Okabe, N., Sakai, K., Koide, E., Miyachi, Y., Kurimoto, M., Mochizuki, M., Yoshino-Yasuda, S., Mitsui, S., Ito, A., Murano, H., Takaya, N. and Kato, M. Novel 4-methyl-2-oxopentanoate reductase involved in synthesis of the Japanese sake flavor, ethyl leucate. Appl. Microbiol. Biotechnol. (2015) . [PMID: 26615399]
[EC 1.1.1.272 created 2002, modified 2013]
 
 
*EC 1.1.1.274
Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming)
Reaction: 2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Other name(s): 2,5-diketo-D-gluconate reductase (ambiguous)
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-D-gluconate-forming)
Comments: The enzyme is involved in the catabolism of 2,5-didehydrogluconate. cf. EC 1.1.1.346, 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 95725-95-4
References:
1.  Sonoyama, T., Kageyama, B., Yagi, S. and Mitsushima, K. Biochemical aspects of 2-keto-L-gulonate accumulation from 2,5-diketo-D-gluconate by Corynebacterium sp. and its mutants. Agric. Biol. Chem. 51 (1987) 3039–3047.
[EC 1.1.1.274 created 2002, modified 2013]
 
 
EC 1.1.1.343
Accepted name: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating)
Reaction: 6-phospho-D-gluconate + NAD+ = D-ribulose 5-phosphate + CO2 + NADH + H+
For diagram of the pentose phosphate pathway (early stages), click here
Other name(s): 6-PGDH (ambiguous); gntZ (gene name); GNDl
Systematic name: 6-phospho-D-gluconate:NAD+ 2-oxidoreductase (decarboxylating)
Comments: Highly specific for NAD+. The enzyme catalyses both the oxidation and decarboxylation of 6-phospho-D-gluconate. In the bacterium Methylobacillus flagellatus the enzyme participates in a formaldehyde oxidation pathway [4]. cf. EC 1.1.1.44, phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9073-95-4
References:
1.  Kiriuchin, M. Y., Kletsova, L. V., Chistoserdov, A. Y. and Tsygankov, Y. D. Properties of glucose 6-phosphate and 6-phosphogluconate dehydrogenases of the obligate methylotroph Methylobacillus flagellatum KT. FEMS Microbiol. Lett. 52 (1988) 199–204.
2.  Ohara, H., Russell, R.A., Uchida, K. and Kondo, H. Purification and characterization of NAD-specific 6-phosphogluconate dehydrogenase from Leuconostoc lactis SHO-54. J. Biosci. Bioeng. 98 (2004) 126–128. [PMID: 16233677]
3.  Zamboni, N., Fischer, E., Laudert, D., Aymerich, S., Hohmann, H.P. and Sauer, U. The Bacillus subtilis yqjI gene encodes the NADP+-dependent 6-P-gluconate dehydrogenase in the pentose phosphate pathway. J. Bacteriol. 186 (2004) 4528–4534. [PMID: 15231785]
4.  Chistoserdova, L., Gomelsky, L., Vorholt, J.A., Gomelsky, M., Tsygankov, Y.D. and Lidstrom, M.E. Analysis of two formaldehyde oxidation pathways in Methylobacillus flagellatus KT, a ribulose monophosphate cycle methylotroph. Microbiology 146 (2000) 233–238. [PMID: 10658669]
[EC 1.1.1.343 created 2013]
 
 
EC 1.1.1.344
Accepted name: dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+]
Reaction: dTDP-6-deoxy-β-L-talose + NAD(P)+ = dTDP-4-dehydro-β-L-rhamnose + NAD(P)H + H+
Glossary: dTDP-4-dehydro-β-L-rhamnose = dTDP-4-dehydro-6-deoxy-β-L-mannose
dTDP-6-deoxy-β-L-talose = dTDP-β-L-pneumose
Other name(s): tal (gene name)
Systematic name: dTDP-6-deoxy-β-L-talose:NAD(P)+ 4-oxidoreductase
Comments: The enzyme works equally well with NAD+ and NADP+.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Karki, S., Yoo, H.G., Kwon, S.Y., Suh, J.W. and Kwon, H.J. Cloning and in vitro characterization of dTDP-6-deoxy-L-talose biosynthetic genes from Kitasatospora kifunensis featuring the dTDP-6-deoxy-L-lyxo-4-hexulose reductase that synthesizes dTDP-6-deoxy-L-talose. Carbohydr. Res. 345 (2010) 1958–1962. [PMID: 20667525]
[EC 1.1.1.344 created 2013]
 
 
EC 1.1.1.345
Accepted name: D-2-hydroxyacid dehydrogenase (NAD+)
Reaction: an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous)
Systematic name: (R)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640–660. [PMID: 9126843]
2.  Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143–1150. [PMID: 11120357]
3.  Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [PMID: 16957230]
4.  Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [PMID: 18391442]
5.  Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873–881. [PMID: 19047348]
6.  Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [PMID: 23954635]
[EC 1.1.1.345 created 2013]
 
 
EC 1.1.1.346
Accepted name: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming)
Reaction: 2-dehydro-L-gulonate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Glossary: 2-dehydro-L-gulonate = 2-dehydro-L-idonate = 2-keto-L-gulonate
Other name(s): 2,5-diketo-D-gluconate-reductase (ambiguous); YqhE reductase; dkgA (gene name); dkgB (gene name)
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase (2-dehydro-L-gulonate-forming)
Comments: The enzyme is involved in ketogluconate metabolism, and catalyses the reaction in vivo in the reverse direction to that shown [1]. It is used in the commercial microbial production of ascorbate. cf. EC 1.1.1.274, 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Sonoyama, T. and Kobayashi, K. Purification and properties of two 2,5-diketo-D-gluconate reductases from a mutant strain derived from Corynebacterium sp. J Ferment Technol. 65 (1987) 311–317.
2.  Miller, J.V., Estell, D.A. and Lazarus, R.A. Purification and characterization of 2,5-diketo-D-gluconate reductase from Corynebacterium sp. J. Biol. Chem. 262 (1987) 9016–9020. [PMID: 3597405]
3.  Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341–3346. [PMID: 10427017]
4.  Maremonti, M., Greco, G. and Wichmann, R. Characterisation of 2,5-diketo-D-gluconic acid reductase from Corynebacterium sp. Biotechnology Letters 18 (1996) 845–850.
5.  Khurana, S., Powers, D.B., Anderson, S. and Blaber, M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-Å resolution. Proc. Natl. Acad. Sci. USA 95 (1998) 6768–6773. [PMID: 9618487]
[EC 1.1.1.346 created 2013]
 
 
EC 1.3.1.26
Transferred entry: dihydrodipicolinate reductase. Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase.
[EC 1.3.1.26 created 1976, modified 2011, deleted 2013]
 
 
EC 1.3.1.98
Accepted name: UDP-N-acetylmuramate dehydrogenase
Reaction: UDP-N-acetyl-α-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-α-D-glucosamine + NADPH + H+
Other name(s): MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5′-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase
Systematic name: UDP-N-acetyl-α-D-muramate:NADP+ oxidoreductase
Comments: A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 39307-28-3
References:
1.  Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971. [PMID: 4717533]
2.  Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012–5016. [PMID: 4394163]
3.  van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503–519. [PMID: 11699883]
[EC 1.3.1.98 created 1976 as EC 1.1.1.158, modified 1983, modified 2002, transferred 2013 to EC 1.3.1.98]
 
 
EC 1.3.1.99
Accepted name: iridoid synthase
Reaction: (6E)-8-oxogeranial + NAD(P)H + H+ = cis-trans-nepetalactol + NAD(P)+
For diagram of secologanin biosynthesis, click here
Glossary: cis-trans-nepetalactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
Systematic name: 8-oxogeranial:NAD(P)+ oxidoreductase (cyclizing, cis-trans-nepetalactol forming)
Comments: Isolated from the plant Catharanthus roseus. The reaction may involve cyclization via a Diels-Alder or Michael reaction. Iridoids are involved in the biosynthesis of many indole alkaloids. The cyclic hemiacetal is readily hydrolysed to the corresponding dial.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Geu-Flores, F., Sherden, N.H., Courdavault, V., Burlat, V., Glenn, W.S., Wu, C., Nims, E., Cui, Y. and O'Connor, S.E. An alternative route to cyclic terpenes by reductive cyclization in iridoid biosynthesis. Nature 492 (2012) 138–142. [PMID: 23172143]
[EC 1.3.1.99 created 2013]
 
 
EC 1.5.1.46
Accepted name: agroclavine dehydrogenase
Reaction: agroclavine + NADP+ = 6,8-dimethyl-6,7,8,9-tetradehydroergoline + NADPH + H+
For diagram of ergot alkaloid biosynthesis, click here
Glossary: agroclavine = 6,8-dimethyl-8,9-didehydroergoline
Other name(s): easG (gene name)
Systematic name: agroclavine:NADP+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of ergotamine, an ergot alkaloid produced by some fungi of the Clavicipitaceae family. The reaction is catalysed in the opposite direction to that shown. The substrate for the enzyme is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Matuschek, M., Wallwey, C., Xie, X. and Li, S.M. New insights into ergot alkaloid biosynthesis in Claviceps purpurea: an agroclavine synthase EasG catalyses, via a non-enzymatic adduct with reduced glutathione, the conversion of chanoclavine-I aldehyde to agroclavine. Org. Biomol. Chem. 9 (2011) 4328–4335. [PMID: 21494745]
[EC 1.5.1.46 created 2013]
 
 
EC 1.7.3.4
Transferred entry: hydroxylamine oxidase. Now covered by EC 1.7.2.6, hydroxylamine dehydrogenase, and EC 1.7.3.6, hydroxylamine oxidase (cytochrome)
[EC 1.7.3.4 created 1972, deleted 2013]
 
 
EC 1.7.3.6
Accepted name: hydroxylamine oxidase (cytochrome)
Reaction: hydroxylamine + O2 = nitrite + H2O + H+ (overall reaction)
(1a) hydroxylamine + 2 ferricytochrome c = nitroxyl + 2 ferrocytochrome c + 2 H+
(1b) nitroxyl + 2 ferrocytochrome c + O2 + H+ = nitrite + 2 ferricytochrome c + H2O (spontaneous)
Other name(s): HAO (ambiguous); hydroxylamine oxidoreductase (ambiguous); hydroxylamine oxidase (misleading)
Systematic name: hydroxylamine:oxygen oxidoreductase
Comments: The enzyme from the heterotrophic nitrifying bacterium Paracoccus denitrificans contains three to five non-heme, non-iron-sulfur iron atoms and interacts with cytochrome c556 and pseudoazurin [2,3]. Under anaerobic conditions in vitro only nitrous oxide is formed [3]. Presumably nitroxyl is released and combines with a second nitroxyl to give nitrous oxide and water. When oxygen is present, nitrite is formed.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9075-43-8
References:
1.  Kurokawa, M, Fukumori, Y and Yamanaka, T A hydroxylamine - cytochrome c reductase occurs in the heterotrophic nitrifier Arthrobacter globiformis. Plant Cell Physiol 26 (1985) 1439–1442.
2.  Wehrfritz, J.M., Reilly, A., Spiro, S. and Richardson, D.J. Purification of hydroxylamine oxidase from Thiosphaera pantotropha. Identification of electron acceptors that couple heterotrophic nitrification to aerobic denitrification. FEBS Lett. 335 (1993) 246–250. [PMID: 8253206]
3.  Moir, J.W., Wehrfritz, J.M., Spiro, S. and Richardson, D.J. The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17. Biochem. J. 319 (1996) 823–827. [PMID: 8920986]
4.  Wehrfritz, J., Carter, J.P., Spiro, S. and Richardson, D.J. Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species. Arch. Microbiol. 166 (1996) 421–424. [PMID: 9082922]
[EC 1.7.3.6 created 1972 as EC 1.7.3.4, part transferred 2013 to EC 1.7.3.6, modified 2015]
 
 
*EC 1.11.1.6
Accepted name: catalase
Reaction: 2 H2O2 = O2 + 2 H2O
Other name(s): equilase; caperase; optidase; catalase-peroxidase; CAT
Systematic name: hydrogen-peroxide:hydrogen-peroxide oxidoreductase
Comments: A hemoprotein. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, UM-BBD, CAS registry number: 9001-05-2
References:
1.  Herbert, D. and Pinsent, J. Crystalline bacterial catalase. Biochem. J. 43 (1948) 193–202. [PMID: 16748386]
2.  Herbert, D. and Pinsent, J. Crystalline human erythrocyte catalase. Biochem. J. 43 (1948) 203–205. [PMID: 16748387]
3.  Keilin, D. and Hartree, E.F. Coupled oxidation of alcohol. Proc. R. Soc. Lond. B Biol. Sci. 119 (1936) 141–159.
4.  Kono, Y. and Fridovich, I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J. Biol. Chem. 258 (1983) 6015–6019. [PMID: 6853475]
5.  Nicholls, P. and Schonbaum, G.R. Catalases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 147–225.
[EC 1.11.1.6 created 1961, modified 1986, modified 1999, modified 2013]
 
 
EC 1.11.1.22
Accepted name: hydroperoxy fatty acid reductase
Reaction: a hydroperoxy fatty acid + NADPH + H+ = a hydroxy fatty acid + NADP+ + H2O
Other name(s): slr1171 (gene name); slr1992 (gene name); hydroperoxy fatty acid:NADPH oxidoreductase
Systematic name: NADPH:hydroperoxy fatty acid oxidoreductase
Comments: The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gaber, A., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803. FEBS Lett. 499 (2001) 32–36. [PMID: 11418106]
2.  Gaber, A., Yoshimura, K., Tamoi, M., Takeda, T., Nakano, Y. and Shigeoka, S. Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress. Plant Physiol. 136 (2004) 2855–2861. [PMID: 15347790]
[EC 1.11.1.22 created 2013]
 
 
*EC 1.12.1.3
Accepted name: hydrogen dehydrogenase (NADP+)
Reaction: H2 + NADP+ = H+ + NADPH
Other name(s): NADP+-linked hydrogenase; NADP+-reducing hydrogenase; hydrogenase (ambiguous); hydrogenase I (ambiguous)
Systematic name: hydrogen:NADP+ oxidoreductase
Comments: The protein from the bacterium Desulfovibrio fructosovorans is an iron-sulfur protein that exclusively functions as a hydrogen dehydrogenase [1], while the enzyme from the archaeon Pyrococcus furiosus is a nickel, iron, iron-sulfur protein, that is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.5, hydrogen dehydrogenase [NAD(P)+].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9027-05-8
References:
1.  de Luca, G., de Philip, P., Rousset, M., Belaich, J.P. and Dermoun, Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: Evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem. Biophys. Res. Commun. 248 (1998) 591–596. [PMID: 9703971]
2.  Bryant, F.O. and Adams, M.W. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264 (1989) 5070–5079. [PMID: 2538471]
3.  Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341–5344. [PMID: 8389482]
4.  Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245–250.
5.  van Haaster, D.J., Silva, P.J., Hagedoorn, P.L., Jongejan, J.A. and Hagen, W.R. Reinvestigation of the steady-state kinetics and physiological function of the soluble NiFe-hydrogenase I of Pyrococcus furiosus. J. Bacteriol. 190 (2008) 1584–1587. [PMID: 18156274]
[EC 1.12.1.3 created 2002, modified 2013]
 
 
EC 1.12.1.5
Accepted name: hydrogen dehydrogenase [NAD(P)+]
Reaction: H2 + NAD(P)+ = H+ + NAD(P)H
Other name(s): hydrogenase II (ambiguous)
Systematic name: hydrogen:NAD(P)+ oxidoreductase
Comments: A nickel, iron, iron-sulfur protein. The enzyme from the archaeon Pyrococcus furiosus is part of a heterotetrameric complex where the α and δ subunits function as a hydrogenase while the β and γ subunits function as sulfur reductase (EC 1.12.98.4, sulfhydrogenase). Different from EC 1.12.1.3, hydrogen dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864–1871. [PMID: 10714990]
[EC 1.12.1.5 created 2013]
 
 
EC 1.12.98.4
Accepted name: sulfhydrogenase
Reaction: H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
Other name(s): sulfur reductase
Systematic name: H2:polysulfide oxidoreductase
Comments: An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the β and γ subunits function as sulfur reductase and the α and δ subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zöphel, A., Kennedy, M.C., Beinert, H. and Kroneck, P.M.H. Investigations on microbial sulfur respiration. 1. Activation and reduction of elemental sulfur in several strains of Eubacteria. Arch. Microbiol. 150 (1988) 72–77.
2.  Ma, K., Schicho, R.N., Kelly, R.M. and Adams, M.W. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 5341–5344. [PMID: 8389482]
3.  Ma, K., Zhou, Z.H. and Adams, M.W. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH. FEMS Microbiol. Lett. 122 (1994) 245–250.
4.  Ma, K., Weiss, R. and Adams, M.W. Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. 182 (2000) 1864–1871. [PMID: 10714990]
[EC 1.12.98.4 created 1992 as EC 1.97.1.3, transferred 2013 to EC 1.12.98.4]
 
 
*EC 1.13.11.37
Accepted name: hydroxyquinol 1,2-dioxygenase
Reaction: hydroxyquinol + O2 = maleylacetate
For diagram of 4-nitrophenol metabolism, click here
Glossary: hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate
Other name(s): hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing); benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)
Systematic name: hydroxyquinol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, UM-BBD, CAS registry number: 91847-14-2
References:
1.  Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353–359. [PMID: 6539772]
2.  Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144–21154. [PMID: 15772073]
3.  Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267–272. [PMID: 16232466]
[EC 1.13.11.37 created 1989, modified 2013]
 
 
EC 1.13.12.20
Accepted name: noranthrone monooxygenase
Reaction: norsolorinic acid anthrone + O2 = norsolorinic acid + H2O
For diagram of aflatoxin biosynthesis (part 1), click here
Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
norsolorinate = 2-hexanoyl-1,3,6,8-tetrahydroxy-9,10-anthraquinone
Other name(s): norsolorinate anthrone oxidase
Systematic name: norsolorinic acid anthrone:oxygen 9-oxidoreductase (norsolorinic acid-forming)
Comments: Involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ehrlich, K.C., Li, P., Scharfenstein, L. and Chang, P.K. HypC, the anthrone oxidase involved in aflatoxin biosynthesis. Appl. Environ. Microbiol. 76 (2010) 3374–3377. [PMID: 20348292]
[EC 1.13.12.20 created 2013]
 
 
*EC 1.14.13.70
Accepted name: sterol 14α-demethylase
Reaction: a 14α-methylsteroid + 3 O2 + 3 NADPH + 3 H+ = a Δ14-steroid + formate + 3 NADP+ + 4 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
Systematic name: sterol,NADPH:oxygen oxidoreductase (14-methyl cleaving)
Comments: This heme-thiolate (P-450) enzyme acts on a range of steroids with a 14α-methyl group, such as obtusifoliol and lanosterol. The enzyme catalyses two successive hydroxylations of the 14α-methyl group, followed by elimination as formate, leaving a 14(15) double bond.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 60063-87-8
References:
1.  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. [PMID: 9076987]
2.  Aoyama, Y. and Yoshida, Y. Different substrate specificities of lanosterol 14α-demethylase (P450-14DM) of Saccharomyces cerevisiae and rat liver of 24-methylene-24,25-dihydrolanosterol and 24,25-dihydrolanosterol. Biochem. Biophys. Res. Commun. 178 (1991) 1064–1071. [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. [PMID: 1567403]
4.  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.
[EC 1.14.13.70 created 2001, modified 2013]
 
 
*EC 1.14.15.6
Accepted name: cholesterol monooxygenase (side-chain-cleaving)
Reaction: cholesterol + 6 reduced adrenodoxin + 3 O2 + 6 H+ = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O (overall reaction)
(1a) cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
(1b) (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
(1c) (20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 + 2 H+ = pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
Other name(s): cholesterol desmolase; cytochrome P-450scc; C27-side chain cleavage enzyme; cholesterol 20-22-desmolase; cholesterol C20-22 desmolase; cholesterol side-chain cleavage enzyme; cholesterol side-chain-cleaving enzyme; steroid 20-22 desmolase; steroid 20-22-lyase; CYP11A1 (gene name)
Systematic name: cholesterol,reduced-adrenodoxin:oxygen oxidoreductase (side-chain-cleaving)
Comments: A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37292-81-2, 440354-98-3
References:
1.  Burstein, S., Middleditch, B.S. and Gut, M. Mass spectrometric study of the enzymatic conversion of cholesterol to (22R)-22-hydroxycholesterol, (20R,22R)-20,22-dihydroxycholesterol, and pregnenolone, and of (22R)-22-hydroxycholesterol to the lgycol and pregnenolone in bovine adrenocortical preparations. Mode of oxygen incorporation. J. Biol. Chem. 250 (1975) 9028–9037. [PMID: 1238395]
2.  Hanukoglu, I., Spitsberg, V., Bumpus, J.A., Dus, K.M. and Jefcoate, C.R. Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover. J. Biol. Chem. 256 (1981) 4321–4328. [PMID: 7217084]
3.  Hanukoglu, I. and Hanukoglu, Z. Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase in adrenal cortex and corpus luteum. Implications for membrane organization and gene regulation. Eur. J. Biochem. 157 (1986) 27–31. [PMID: 3011431]
4.  Strushkevich, N., MacKenzie, F., Cherkesova, T., Grabovec, I., Usanov, S. and Park, H.W. Structural basis for pregnenolone biosynthesis by the mitochondrial monooxygenase system. Proc. Natl. Acad. Sci. USA 108 (2011) 10139–10143. [PMID: 21636783]
5.  Mast, N., Annalora, A.J., Lodowski, D.T., Palczewski, K., Stout, C.D. and Pikuleva, I.A. Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1. J. Biol. Chem. 286 (2011) 5607–5613. [PMID: 21159775]
[EC 1.14.15.6 created 1983, modified 2013, modified 2014]
 
 
EC 1.14.15.12
Accepted name: pimeloyl-[acyl-carrier protein] synthase
Reaction: a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction)
(1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O
(1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
Glossary: a long-chain acyl-[acyl-carrier protein] = an acyl-[acyl-carrier protein] thioester where the acyl chain contains 13 to 22 carbon atoms.
palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 7-hydroxy-7-oxoheptanoyl-[acyl-carrier protein]
Other name(s): bioI (gene name); P450BioI; CYP107H1
Systematic name: acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein] forming)
Comments: A heme-thiolate protein (P-450). The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351–360. [PMID: 11368323]
2.  Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86–87. [PMID: 14737344]
3.  Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696–15701. [PMID: 18838690]
[EC 1.14.15.12 created 2013]
 
 
*EC 1.14.99.9
Transferred entry: steroid 17α-monooxygenase, now classified as EC 1.14.14.19, steroid 17α-monooxygenase
[EC 1.14.99.9 created 1961 as EC 1.99.1.9, transferred 1965 to EC 1.14.1.7, transferred 1972 to EC 1.14.99.9, modified 2013, deleted 2015]
 
 
*EC 1.14.99.10
Transferred entry: steroid 21-monooxygenase. Now EC 1.14.14.16, steroid 21-monooxygenase
[EC 1.14.99.10 created 1961 as EC 1.99.1.11, transferred 1965 to EC 1.14.1.8, transferred 1972 to EC 1.14.99.10, modified 2013, deleted 2015]
 
 
EC 1.17.1.8
Accepted name: 4-hydroxy-tetrahydrodipicolinate reductase
Reaction: (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+
For diagram of lysine biosynthesis (early stages), click here
Glossary: (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate = (2S)-2,3,4,5-tetrahydrodipicolinate
Other name(s): dihydrodipicolinate reductase (incorrect); dihydrodipicolinic acid reductase (incorrect); 2,3,4,5-tetrahydrodipicolinate:NAD(P)+ oxidoreductase (incorrect); dapB (gene name)
Systematic name: (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate:NAD(P)+ 4-oxidoreductase
Comments: Studies [2] of the enzyme from the bacterium Escherichia coli have shown that the enzyme accepts (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate and not (S)-2,3-dihydrodipicolinate as originally thought [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Farkas, W. and Gilvarg, C. The reduction step in diaminopimelic acid biosynthesis. J. Biol. Chem. 240 (1965) 4717–4722. [PMID: 4378965]
2.  Devenish, S.R., Blunt, J.W. and Gerrard, J.A. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J. Med. Chem. 53 (2010) 4808–4812. [PMID: 20503968]
[EC 1.17.1.8 created 1976 as EC 1.3.1.26, transferred 2013 to EC 1.17.1.8]
 
 
EC 1.23.1 With NADH or NADPH as donor (only sub-subclass identified to date)
 
EC 1.23.1.1
Accepted name: (+)-pinoresinol reductase
Reaction: (+)-lariciresinol + NADP+ = (+)-pinoresinol + NADPH + H+
For diagram of matairesinol biosynthesis, click here
Glossary: (+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-pinoresinol = (1S,3aR,4S,6aR)-4,4-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR
Systematic name: (+)-lariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that further reduces the product to the lignan (–)-secoisolariciresinol [EC 1.23.1.2, (+)-lariciresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6]. The 4-pro-R hydrogen of NADH is transferred to the 7-pro-R position of lariciresinol [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939]
2.  Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [PMID: 8910615]
3.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995]
4.  Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [PMID: 13129921]
5.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599]
6.  Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [PMID: 18489708]
[EC 1.23.1.1 created 2013]
 
 
EC 1.23.1.2
Accepted name: (+)-lariciresinol reductase
Reaction: (–)-secoisolariciresinol + NADP+ = (+)-lariciresinol + NADPH + H+
For diagram of matairesinol biosynthesis, click here
Glossary: (+)-lariciresinol = 4-[(2S,3R,4R)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-secoisolariciresinol = (2R,3R)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (+)-pinoresinol/(+)-lariciresinol; (+)-pinoresinol-(+)-lariciresinol reductase; PLR
Systematic name: (–)-secoisolariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (+)-pinoresinol [EC 1.23.1.1, (+)-pinoresinol reductase]. Isolated from the plants Forsythia intermedia [1,2], Thuja plicata (western red cedar) [3], Linum perenne (perennial flax) [5] and Linum corymbulosum [6].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L. and Lewis, N.G. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. J. Biol. Chem. 268 (1993) 27026–27033. [PMID: 8262939]
2.  Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A. and Lewis, N.G. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. J. Biol. Chem. 271 (1996) 29473–29482. [PMID: 8910615]
3.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995]
4.  Min, T., Kasahara, H., Bedgar, D.L., Youn, B., Lawrence, P.K., Gang, D.R., Halls, S.C., Park, H., Hilsenbeck, J.L., Davin, L.B., Lewis, N.G. and Kang, C. Crystal structures of pinoresinol-lariciresinol and phenylcoumaran benzylic ether reductases and their relationship to isoflavone reductases. J. Biol. Chem. 278 (2003) 50714–50723. [PMID: 13129921]
5.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599]
6.  Bayindir, Ü., Alfermann, A.W. and Fuss, E. Hinokinin biosynthesis in Linum corymbulosum Reichenb. Plant J. 55 (2008) 810–820. [PMID: 18489708]
[EC 1.23.1.2 created 2013]
 
 
EC 1.23.1.3
Accepted name: (–)-pinoresinol reductase
Reaction: (–)-lariciresinol + NADP+ = (–)-pinoresinol + NADPH + H+
For diagram of (–)-lariciresinol biosynthesis, click here
Glossary: (–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(–)-pinoresinol = (1R,3aS,4R,6aS)-4,4′-(tetrahydro-1H,3H-furo[3,4-c]furan-1,4-diyl)bis(2-methoxyphenol)
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR
Systematic name: (–)-lariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that usually further reduces the product to (+)-secoisolariciresinol [EC 1.23.1.4, (–)-lariciresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1], Linum perenne (perennial flax) [2] and Arabidopsis thaliana (thale cress) [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995]
2.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599]
3.  Nakatsubo, T., Mizutani, M., Suzuki, S., Hattori, T. and Umezawa, T. Characterization of Arabidopsis thaliana pinoresinol reductase, a new type of enzyme involved in lignan biosynthesis. J. Biol. Chem. 283 (2008) 15550–15557. [PMID: 18347017]
[EC 1.23.1.3 created 2013]
 
 
EC 1.23.1.4
Accepted name: (–)-lariciresinol reductase
Reaction: (+)-secoisolariciresinol + NADP+ = (–)-lariciresinol + NADPH + H+
For diagram of (#150)-lariciresinol biosynthesis, click here
Glossary: (–)-lariciresinol = 4-[(2R,3S,4S)-4-[(4-hydroxy-3-methoxyphenyl)methyl]-3-(hydroxymethyl)oxolan-2-yl]-2-methoxyphenol
(+)-secoisolariciresinol = (2S,3S)-2,3-bis[(4-hydroxy-3-methoxyphenyl)methyl]butane-1,4-diol
Other name(s): pinoresinol/lariciresinol reductase; pinoresinol-lariciresinol reductases; (–)-pinoresinol-(–)-lariciresinol reductase; PLR
Systematic name: (+)-secoisolariciresinol:NADP+ oxidoreductase
Comments: The reaction is catalysed in vivo in the opposite direction to that shown. A multifunctional enzyme that also reduces (–)-pinoresinol [EC 1.23.1.3, (–)-pinoresinol reductase]. Isolated from the plants Thuja plicata (western red cedar) [1] and Linum corymbulosum [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Fujita, M., Gang, D.R., Davin, L.B. and Lewis, N.G. Recombinant pinoresinol-lariciresinol reductases from western red cedar (Thuja plicata) catalyze opposite enantiospecific conversions. J. Biol. Chem. 274 (1999) 618–627. [PMID: 9872995]
2.  Hemmati, S., Schmidt, T.J. and Fuss, E. (+)-Pinoresinol/(-)-lariciresinol reductase from Linum perenne Himmelszelt involved in the biosynthesis of justicidin B. FEBS Lett. 581 (2007) 603–610. [PMID: 17257599]
[EC 1.23.1.4 created 2013]
 
 
EC 1.97.1.3
Transferred entry: sulfur reductase. Now EC 1.12.98.4, sulfhydrogenase, since hydrogen is known to be the electron donor.
[EC 1.97.1.3 created 1992, deleted 2013]
 
 
*EC 2.1.1.132
Accepted name: precorrin-6B C5,15-methyltransferase (decarboxylating)
Reaction: 2 S-adenosyl-L-methionine + precorrin-6B = 2 S-adenosyl-L-homocysteine + precorrin-8X + CO2 (overall reaction)
(1a) S-adenosyl-L-methionine + precorrin-6B = S-adenosyl-L-homocysteine + precorrin-7 + CO2
(1b) S-adenosyl-L-methionine + precorrin-7 = S-adenosyl-L-homocysteine + precorrin-8X
For diagram of corrin biosynthesis (part 4), click here
Glossary: precorrin-6B = precorrin-6Y
Other name(s): precorrin-6 methyltransferase; precorrin-6Y methylase; precorrin-6Y C5,15-methyltransferase (decarboxylating); cobL (gene name)
Systematic name: S-adenosyl-L-methionine:1-precorrin-6B C5,15-methyltransferase (C-12-decarboxylating)
Comments: The enzyme, which participates in the aerobic adenosylcobalamin biosynthesis pathway, has S-adenosyl-L-methionine-dependent methyltransferase and decarboxylase activities. The enzyme is a fusion protein with two active sites; one catalyses the methylation at C15 and the decarboxylation, while the other catalyses the methylation at C5.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 162995-22-4
References:
1.  Blanche, F., Famechon, A., Thibaut, D., Debussche, L., Cameron, B., Crouzet, J. Biosynthesis of vitamin B12 in Pseudomonas denitrificans: the biosynthetic sequence from precorrin-6Y to precorrin-8X is catalyzed by the cobL gene product. J. Bacteriol. 174 (1992) 1050–1052. [PMID: 1732195]
2.  Deery, E., Schroeder, S., Lawrence, A.D., Taylor, S.L., Seyedarabi, A., Waterman, J., Wilson, K.S., Brown, D., Geeves, M.A., Howard, M.J., Pickersgill, R.W. and Warren, M.J. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. Nat. Chem. Biol. 8 (2012) 933–940. [PMID: 23042036]
[EC 2.1.1.132 created 1999, modified 2013]
 
 
EC 2.1.1.149
Deleted entry: myricetin O-methyltransferase. Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase.
[EC 2.1.1.149 created 2003, modified 2011, deleted 2013]
 
 
EC 2.1.1.266
Accepted name: 23S rRNA (adenine2030-N6)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenine2030 in 23S rRNA = S-adenosyl-L-homocysteine + N6-methyladenine2030 in 23S rRNA
Other name(s): YhiR protein; rlmJ (gene name); m6A2030 methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenine2030-N6)-methyltransferase
Comments: The recombinant RlmJ protein is most active in methylating deproteinized 23S ribosomal subunit, and does not methylate the completely assembled 50S subunits [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Golovina, A.Y., Dzama, M.M., Osterman, I.A., Sergiev, P.V., Serebryakova, M.V., Bogdanov, A.A. and Dontsova, O.A. The last rRNA methyltransferase of E. coli revealed: the yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA. RNA 18 (2012) 1725–1734. [PMID: 22847818]
[EC 2.1.1.266 created 2013]
 
 
EC 2.1.1.267
Accepted name: flavonoid 3′,5′-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + a 3′-hydroxyflavonoid = S-adenosyl-L-homocysteine + a 3′-methoxyflavonoid
(2) S-adenosyl-L-methionine + a 5′-hydroxy-3′-methoxyflavonoid = S-adenosyl-L-homocysteine + a 3′,5′-dimethoxyflavonoid
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
myricetin = 3,3′,4′,5,5′,7-hexahydroxyflavone
quercetin = 3,3′,4′,5,7-pentahydroxyflavone
Other name(s): AOMT; CrOMT2
Systematic name: S-adenosyl-L-methionine:flavonoid 3′-O-methyltransferase
Comments: Isolated from Vitis vinifera (grape) [2]. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. The enzyme from Catharanthus roseus was most active with myricetin [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Cacace, S., Schröder, G., Wehinger, E., Strack, D., Schmidt, J. and Schröder, J. A flavonol O-methyltransferase from Catharanthus roseus performing two sequential methylations. Phytochemistry 62 (2003) 127–137. [PMID: 12482447]
2.  Hugueney, P., Provenzano, S., Verries, C., Ferrandino, A., Meudec, E., Batelli, G., Merdinoglu, D., Cheynier, V., Schubert, A. and Ageorges, A. A novel cation-dependent O-methyltransferase involved in anthocyanin methylation in grapevine. Plant Physiol. 150 (2009) 2057–2070. [PMID: 19525322]
[EC 2.1.1.267 created 2013, modified 2014]
 
 
EC 2.1.1.268
Accepted name: tRNAThr (cytosine32-N3)-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
(2) S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
Other name(s): ABP140; Trm140p
Systematic name: S-adenosyl-L-methionine:tRNAThr (cytosine32-N3)-methyltransferase
Comments: The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Noma, A., Yi, S., Katoh, T., Takai, Y., Suzuki, T. and Suzuki, T. Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae. RNA 17 (2011) 1111–1119. [PMID: 21518805]
2.  D'Silva, S., Haider, S.J. and Phizicky, E.M. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA 17 (2011) 1100–1110. [PMID: 21518804]
[EC 2.1.1.268 created 2013]
 
 
*EC 2.3.1.25
Accepted name: plasmalogen synthase
Reaction: acyl-CoA + 1-O-(alk-1-enyl)glycero-3-phosphocholine = CoA + plasmenylcholine
Glossary: 1-O-(alk-1-enyl)glycero-3-phosphocholine = 1-alkenylglycerophosphocholine,
plasmenylcholine = 1-alkenyl-2-acylglycerophosphocholine
Other name(s): lysoplasmenylcholine acyltransferase; O-1-alkenylglycero-3-phosphorylcholine acyltransferase; 1-alkenyl-glycero-3-phosphorylcholine:acyl-CoA acyltransferase; 1-alkenylglycerophosphocholine O-acyltransferase
Systematic name: acyl-CoA:1-O-(alk-1-enyl)-glycero-3-phosphocholine 2-O-acyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37257-10-6
References:
1.  Waku, K. and Lands, W.E.M. Acyl coenzyme A:1-alkenyl-glycero-3-phosphorylcholine acyltransferase action in plasmalogen biosynthesis. J. Biol. Chem. 243 (1968) 2654–2659. [PMID: 5689955]
2.  Arthur, G. and Choy, P.C. Acylation of 1-alkenyl-glycerophosphocholine and 1-acyl-glycerophosphocholine in guinea pig heart. Biochem. J. 236 (1986) 481–487. [PMID: 3753462]
[EC 2.3.1.25 created 1972, modified 2013]
 
 
*EC 2.3.1.47
Accepted name: 8-amino-7-oxononanoate synthase
Reaction: pimeloyl-[acyl-carrier protein] + L-alanine = 8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
Glossary: pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]
Other name(s): 7-keto-8-aminopelargonic acid synthetase; 7-keto-8-aminopelargonic synthetase; 8-amino-7-oxopelargonate synthase; bioF (gene name)
Systematic name: 6-carboxyhexanoyl-[acyl-carrier protein]:L-alanine C-carboxyhexanoyltransferase (decarboxylating)
Comments: A pyridoxal-phosphate protein. The enzyme catalyses the decarboxylative condensation of L-alanine and pimeloyl-[acyl-carrier protein], a key step in the pathway for biotin biosynthesis. Pimeloyl-CoA can be used with lower efficiency [5].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9075-61-0
References:
1.  Eisenberg, M.A. and Star, C. Synthesis of 7-oxo-8-aminopelargonic acid, a biotin vitamer, in cell-free extracts of Escherichia coli biotin auxotrophs. J. Bacteriol. 96 (1968) 1291–1297. [PMID: 4879561]
2.  Alexeev, D., Alexeeva, M., Baxter, R.L., Campopiano, D.J., Webster, S.P. and Sawyer, L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284 (1998) 401–419. [PMID: 9813126]
3.  Ploux, O., Breyne, O., Carillon, S. and Marquet, A. Slow-binding and competitive inhibition of 8-amino-7-oxopelargonate synthase, a pyridoxal-5′-phosphate-dependent enzyme involved in biotin biosynthesis, by substrate and intermediate analogs. Kinetic and binding studies. Eur. J. Biochem. 259 (1999) 63–70. [PMID: 9914476]
4.  Webster, S.P. , Alexeev. D., Campopiano, D.J., Watt, R.M., Alexeeva, M., Sawyer, L. and Baxter, R. Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry 39 (2000) 516–528. [PMID: 10642176]
5.  Lin, S., Hanson, R.E. and Cronan, J.E. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat. Chem. Biol. 6 (2010) 682–688. [PMID: 20693992]
[EC 2.3.1.47 created 1976, modified 2013]
 
 
EC 2.3.1.104
Deleted entry: 1-alkenylglycerophosphocholine O-acyltransferase. The activity is covered by EC 2.3.1.25, plasmalogen synthase
[EC 2.3.1.104 created 1989, deleted 2013]
 
 
*EC 2.3.1.140
Accepted name: rosmarinate synthase
Reaction: caffeoyl-CoA + (R)-3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate
For diagram of rosmarinate biosynthesis, click here
Glossary: (R)-3-(3,4-dihydroxyphenyl)lactate = (2R)-3-(3,4-dihydroxyphenyl)-2-hydroxypropanoate
rosmarinate = (2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoate
Other name(s): rosmarinic acid synthase; caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid caffeoyltransferase; 4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase; RAS (gene name)
Systematic name: caffeoyl-CoA:(R)-3-(3,4-dihydroxyphenyl)lactate 2′-O-caffeoyl-transferase
Comments: Involved, with EC 1.1.1.237 (hydroxyphenylpyruvate reductase) in the biosynthesis of rosmarinic acid. Characterized from the plant Melissa officinalis L. (lemon balm).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 117590-80-4
References:
1.  Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.  Petersen, M. S. Characterization of rosmarinic acid synthase from cell cultures of Coleus blumei. Phytochemistry 30 (1991) 2877–2881.
3.  Weitzel, C. and Petersen, M. Cloning and characterisation of rosmarinic acid synthase from Melissa officinalis L. Phytochemistry 72 (2011) 572–578. [PMID: 21354582]
[EC 2.3.1.140 created 1992, modified 2013]
 
 
*EC 2.3.1.151
Accepted name: 2,3′,4,6-tetrahydroxybenzophenone synthase
Reaction: 3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3′,4,6-tetrahydroxybenzophenone + 3 CO2
For diagram of polyketides biosynthesis, click here
Other name(s): benzophenone synthase (ambiguous); BPS (ambiguous)
Systematic name: malonyl-CoA:3-hydroxybenzoyl-CoA malonyltransferase (decarboxylating, 2,3′,4,6-tetrahydroxybenzophenone-forming)
Comments: Involved in the biosynthesis of plant xanthones. Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA (cf. EC 2.3.1.220, 2,4,6-trihydroxybenzophenone synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 175780-21-9
References:
1.  Beerhues, L. Benzophenone synthase from cultured cells of Centaurium erythraea. FEBS Lett. 383 (1996) 264–266. [PMID: 8925910]
[EC 2.3.1.151 created 1999, modified 2013]
 
 
*EC 2.3.1.153
Accepted name: anthocyanin 5-(6′′′-hydroxycinnamoyltransferase)
Reaction: 4-hydroxycinnamoyl-CoA + anthocyanidin 3,5-diglucoside = CoA + anthocyanidin 3-glucoside 5-(6-O-4-hydroxycinnamoylglucoside)
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: 4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA
Systematic name: 4-hydroxycinnamoyl-CoA:anthocyanidin 3,5-diglucoside 5-O-glucoside-6′′′-O-4-hydroxycinnamoyltransferase
Comments: Isolated from the plant Gentiana triflora. Transfers the hydroxycinnamoyl group only to the C-5 glucoside of anthocyanin. Caffeoyl-CoA, but not malonyl-CoA, can substitute as an acyl donor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 198841-53-1
References:
1.  Fujiwara, H., Tanaka, Y., Fukui, Y., Nakao, M., Ashikari, T., Kusumi, T. Anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Purification, characterization and its role in anthocyanin biosynthesis. Eur. J. Biochem. 249 (1997) 45–51. [PMID: 9363752]
2.  Fujiwara, H., Tanaka, Y., Yonekura-Sakakibara, K., Fukuchi-Mizutani, M., Nakao, M., Fukui, Y., Yamaguchi, M., Ashikari, T. and Kusumi, T. cDNA cloning, gene expression and subcellular localization of anthocyanin 5-aromatic acyltransferase from Gentiana triflora. Plant J. 16 (1998) 421–431. [PMID: 9881162]
[EC 2.3.1.153 created 1999, modified 2013]
 
 
EC 2.3.1.211
Accepted name: bisdemethoxycurcumin synthase
Reaction: 2 4-coumaroyl-CoA + malonyl-CoA + H2O = 3 CoA + bisdemethoxycurcumin + 2 CO2
For diagram of curcumin biosynthesis, click here
Glossary: bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
Other name(s): CUS; curcuminoid synthase (ambiguous)
Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)
Comments: A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoylacetyl-CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme’s cavity and is not released to the environment.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Morita, H., Wanibuchi, K., Nii, H., Kato, R., Sugio, S. and Abe, I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc. Natl. Acad. Sci. USA 107 (2010) 19778–19783. [PMID: 21041675]
[EC 2.3.1.211 created 2013]
 
 
EC 2.3.1.212
Accepted name: benzalacetone synthase
Reaction: 4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2
For diagram of benzalacetone biosynthesis, click here
Glossary: 4-hydroxybenzalacetone = 4-(4-hydroxyphenyl)but-3-en-2-one
Other name(s): BAS
Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (4-hydroxybenzalacetone-forming)
Comments: A polyketide synthase that catalyses the C6-C4 skeleton of phenylbutanoids in higher plants.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Borejsza-Wysocki, W. and Hrazdina, G. Aromatic polyketide synthases (purification, characterization, and antibody development to benzalacetone synthase from raspberry fruits). Plant Physiol. 110 (1996) 791–799. [PMID: 12226219]
2.  Abe, I., Takahashi, Y., Morita, H. and Noguchi, H. Benzalacetone synthase. A novel polyketide synthase that plays a crucial role in the biosynthesis of phenylbutanones in Rheum palmatum. Eur. J. Biochem. 268 (2001) 3354–3359. [PMID: 11389739]
3.  Zheng, D. and Hrazdina, G. Molecular and biochemical characterization of benzalacetone synthase and chalcone synthase genes and their proteins from raspberry (Rubus idaeus L.). Arch. Biochem. Biophys. 470 (2008) 139–145. [PMID: 18068110]
4.  Morita, H., Shimokawa, Y., Tanio, M., Kato, R., Noguchi, H., Sugio, S., Kohno, T. and Abe, I. A structure-based mechanism for benzalacetone synthase from Rheum palmatum. Proc. Natl. Acad. Sci. USA 107 (2010) 669–673. [PMID: 20080733]
[EC 2.3.1.212 created 2013]
 
 
EC 2.3.1.213
Accepted name: cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase
Reaction: 1-O-(4-hydroxycinnamoyl)-β-D-glucose + cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) = β-D-glucose + cyanidin 3-O-[6-O-(6-O-4-hydroxycinnamoyl-β-D-glucosyl)-2-O-β-D-xylosyl-β-D-galactoside]
For diagram of cyanidin galactoside biosynthesis, click here
Glossary: 1-O-(4-hydroxycinnamoyl)-β-D-glucose = 1-O-(4-coumaroyl)-β-D-glucose
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(2"-O-xylosyl-6"-O-glucosylgalactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase
Systematic name: 1-O-(4-hydroxycinnamoyl)-β-D-glucose:cyanidin 3-O-(6-O-β-D-glucosyl-2-O-β-D-xylosyl-β-D-galactoside) 6′′′-O-(4-hydroxycinnamoyl)transferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot). In addition to 1-O-(4-hydroxycinnamoyl)-β-D-glucose, the enzyme can use the 1-O-sinapoyl- and 1-O-feruloyl- derivatives of β-D-glucose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gläßgen, W.E. and Seitz, H.U. Acylation of anthocyanins with hydroxycinnamic acids via 1-O-acylglucosides by protein preparations from cell cultures of Daucus carota L. Planta 186 (1992) 582–585.
[EC 2.3.1.213 created 2013]
 
 
EC 2.3.1.214
Accepted name: pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4′′′-malonyltransferase
Reaction: malonyl-CoA + 4′′′-demalonylsalvianin = CoA + salvianin
For diagram of salvianin biosynthesis, click here
Glossary: salvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(4,6-di-O-malonyl-β-D-glucoside)
4′′′-demalonylsalvianin = pelargonidin 3-O-(6-caffeoyl-β-D-glucoside) 5-O-(6-O-malonyl-β-D-glucoside)
Other name(s): malonyl-CoA:anthocyanin 5-glucoside 4′′′-O-malonyltransferase; Ss5MaT2
Systematic name: malonyl-CoA:4′′′-demalonylsalvianin 4′′′-O-malonyltransferase
Comments: Isolated from the plant Salvia splendens (scarlet sage).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Suzuki, H., Sawada, S., Watanabe, K., Nagae, S., Yamaguchi, M.A., Nakayama, T. and Nishino, T. Identification and characterization of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers: an enzyme that is phylogenetically separated from other anthocyanin acyltransferases. Plant J. 38 (2004) 994–1003. [PMID: 15165190]
[EC 2.3.1.214 created 2013]
 
 
EC 2.3.1.215
Accepted name: anthocyanidin 3-O-glucoside 6′′-O-acyltransferase
Reaction: 4-hydroxycinnamoyl-CoA + an anthocyanidin 3-O-β-D-glucoside = CoA + an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-β-D-glucoside]
For diagram of anthocyanidin acylglucoside biosynthesis, click here and for diagram of salvianin biosynthesis, click here
Glossary: 4-hydroxycinnamoyl-CoA = 4-coumaroyl-CoA
3,4-dihydroxycinnamoyl-CoA = caffeoyl-CoA
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
Systematic name: 4-hydroxycinnamoyl-CoA:anthocyanin-3-O-glucoside 6′′-O-acyltransferase
Comments: Isolated from the plants Perilla frutescens and Gentiana triflora (clustered gentian). Acts on a range of anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-rutinoside. It did not act on delphinidin 3,3′,7-tri-O-glucoside. Recombinant Perilla frutescens enzyme could utilize caffeoyl-CoA but not malonyl-CoA as alternative acyl donor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Fujiwara, H., Tanaka, Y., Fukui, Y., Ashikari, T., Yamaguchi, M. and Kusumi, T. Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens. Plant Sci. 137 (1998) 87–94.
2.  Yonekura-Sakakibara, K., Tanaka, Y., Fukuchi-Mizutani, M., Fujiwara, H., Fukui, Y., Ashikari, T., Murakami, Y., Yamaguchi, M. and Kusumi, T. Molecular and biochemical characterization of a novel hydroxycinnamoyl-CoA: anthocyanin 3-O-glucoside-6"-O-acyltransferase from Perilla frutescens. Plant Cell Physiol 41 (2000) 495–502. [PMID: 10845463]
[EC 2.3.1.215 created 2013]
 
 
EC 2.3.1.216
Accepted name: 5,7-dihydroxy-2-methylchromone synthase
Reaction: 5 malonyl-CoA = 5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O
For diagram of polyketides biosynthesis, click here
Other name(s): pentaketide chromone synthase
Systematic name: malonyl-CoA:malonyl-CoA malonyltransferase (5,7-dihydroxy-2-methyl-4H-chromen-4-one-forming)
Comments: A polyketide synthase from the plant Aloe arborescens (aloe).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Abe, I., Utsumi, Y., Oguro, S., Morita, H., Sano, Y. and Noguchi, H. A plant type III polyketide synthase that produces pentaketide chromone. J. Am. Chem. Soc. 127 (2005) 1362–1363. [PMID: 15686354]
[EC 2.3.1.216 created 2013]
 
 
EC 2.3.1.217
Accepted name: curcumin synthase
Reaction: feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2
For diagram of curcumin biosynthesis, click here
Glossary: curcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
Other name(s): CURS; CURS1 (gene name); CURS2 (gene name); CURS3 (gene name)
Systematic name: feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160–11170. [PMID: 19258320]
2.  Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [PMID: 19622354]
3.  Katsuyama, Y., Miyazono, K., Tanokura, M., Ohnishi, Y. and Horinouchi, S. Structural and biochemical elucidation of mechanism for decarboxylative condensation of β-keto acid by curcumin synthase. J. Biol. Chem. 286 (2011) 6659–6668. [PMID: 21148316]
[EC 2.3.1.217 created 2013]
 
 
EC 2.3.1.218
Accepted name: phenylpropanoylacetyl-CoA synthase
Reaction: (1) feruloyl-CoA + malonyl-CoA = feruloylacetyl-CoA + CO2 + CoA
(2) 4-coumaroyl-CoA + malonyl-CoA = (4-coumaroyl)acetyl-CoA + CO2 + CoA
For diagram of curcumin biosynthesis, click here
Glossary: feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
phenylpropanoylacetyl-CoA = phenylpropanoyl-diketide-CoA
Other name(s): phenylpropanoyl-diketide-CoA synthase; DCS
Systematic name: phenylpropanoyl-CoA:malonyl-CoA phenylpropanoyl-transferase (decarboxylating)
Comments: The enzyme has been characterized from the plant Curcuma longa (turmeric). It prefers feruloyl-CoA, and has no activity with cinnamoyl-CoA.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160–11170. [PMID: 19258320]
[EC 2.3.1.218 created 2013]
 
 
EC 2.3.1.219
Accepted name: demethoxycurcumin synthase
Reaction: (1) 4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
(2) 4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2
For diagram of curcumin biosynthesis, click here
Glossary: demethoxycurcumin = (1E,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
Other name(s): CURS3
Systematic name: 4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [PMID: 19622354]
[EC 2.3.1.219 created 2013]
 
 
EC 2.3.1.220
Accepted name: 2,4,6-trihydroxybenzophenone synthase
Reaction: 3 malonyl-CoA + benzoyl-CoA = 4 CoA + 2,4,6-trihydroxybenzophenone + 3 CO2
For diagram of polyketides biosynthesis, click here
Other name(s): benzophenone synthase (ambiguous); BPS (ambiguous)
Systematic name: malonyl-CoA:benzoyl-CoA malonyltransferase (2,4,6-trihydroxybenzophenone-forming)
Comments: Involved in the biosynthesis of plant xanthones. The enzyme from the plant Hypericum androsaemum L can use 3-hydroxybenzoyl-CoA instead of benzoyl-CoA, but with lower activity (cf. EC 2.3.1.151, 2,3′,4,6-tetrahydroxybenzophenone synthase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Schmidt, W. and Beerhues, L. Alternative pathways of xanthone biosynthesis in cell cultures of Hypericum androsaemum L. FEBS Lett. 420 (1997) 143–146. [PMID: 9459298]
2.  Nualkaew, N., Morita, H., Shimokawa, Y., Kinjo, K., Kushiro, T., De-Eknamkul, W., Ebizuka, Y. and Abe, I. Benzophenone synthase from Garcinia mangostana L. pericarps. Phytochemistry 77 (2012) 60–69. [PMID: 22390826]
[EC 2.3.1.220 created 2013]
 
 
EC 2.3.1.221
Accepted name: noranthrone synthase
Reaction: 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
For diagram of polyketides biosynthesis, click here
Glossary: norsolorinic acid anthrone = noranthrone = 2-hexanoyl-1,3,6,8-tetrahydroxyanthracen-9(10H)-one
Other name(s): polyketide synthase A (ambiguous); PksA (ambiguous); norsolorinic acid anthrone synthase
Systematic name: malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)
Comments: A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Crawford, J.M., Thomas, P.M., Scheerer, J.R., Vagstad, A.L., Kelleher, N.L. and Townsend, C.A. Deconstruction of iterative multidomain polyketide synthase function. Science 320 (2008) 243–246. [PMID: 18403714]
2.  Crawford, J.M., Korman, T.P., Labonte, J.W., Vagstad, A.L., Hill, E.A., Kamari-Bidkorpeh, O., Tsai, S.C. and Townsend, C.A. Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization. Nature 461 (2009) 1139–1143. [PMID: 19847268]
3.  Korman, T.P., Crawford, J.M., Labonte, J.W., Newman, A.G., Wong, J., Townsend, C.A. and Tsai, S.C. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proc. Natl. Acad. Sci. USA 107 (2010) 6246–6251. [PMID: 20332208]
[EC 2.3.1.221 created 2013]
 
 
EC 2.3.1.222
Accepted name: phosphate propanoyltransferase
Reaction: propanoyl-CoA + phosphate = CoA + propanoyl phosphate
Other name(s): PduL
Systematic name: propanoyl-CoA:phosphate propanoyltransferase
Comments: Part of the degradation pathway for propane-1,2-diol .
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Liu, Y., Leal, N.A., Sampson, E.M., Johnson, C.L., Havemann, G.D. and Bobik, T.A. PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar typhimurium LT2. J. Bacteriol. 189 (2007) 1589–1596. [PMID: 17158662]
[EC 2.3.1.222 created 2013]
 
 
*EC 2.3.2.1
Accepted name: D-glutamyltransferase
Reaction: (1) D-glutamine + D-glutamate = NH3 + γ-D-glutamyl-D-glutamate
(2) L(or D)-glutamine + (γ-D-glutamyl)n-[peptide] = NH3 + (γ-D-glutamyl)n+1-[peptide]
Other name(s): D-glutamyl transpeptidase; D-γ-glutamyl transpeptidase
Systematic name: glutamine:D-glutamyl-peptide 5-glutamyltransferase
Comments: The enzyme catalyses two reactions. The first is the transfer of a glutamyl residue from L- or D-glutamine to D-glutamate via a γ linkage, forming γ-glutamyl-D-glutamate, and the second is the transfer of additional glutamyl residues to the peptide, extending the polypeptide chain.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 9030-02-8
References:
1.  Williams, W.J. and Thorne, C.B. Biosynthesis of glutamyl peptides from glutamine by a transfer reaction. J. Biol. Chem. 210 (1954) 203–217. [PMID: 13201582]
2.  Williams, W.J., Litwin, J. and Thorne, C.B. Further studies on the biosynthesis of γ-glutamyl peptides by transfer reactions. J. Biol. Chem. 212 (1955) 427–438. [PMID: 13233245]
[EC 2.3.2.1 created 1961, modified 1976, modified 2013]
 
 
*EC 2.4.1.62
Accepted name: ganglioside galactosyltransferase
Reaction: UDP-α-D-galactose + an N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of ganglioside biosynthesis, click here
Glossary: N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = ganglioside GM2
a β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = gangloside GM1a
Other name(s): UDP-galactose—ceramide galactosyltransferase; uridine diphosphogalactose-ceramide galactosyltransferase; UDP galactose-LAC Tet-ceramide α-galactosyltransferase; UDP-galactose-GM2 galactosyltransferase; uridine diphosphogalactose-GM2 galactosyltransferase; uridine diphosphate D-galactose:glycolipid galactosyltransferase; UDP-galactose:N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosyl-glucosyl-ceramide galactosyltransferase; UDP-galactose-GM2 ganglioside galactosyltransferase; GM1-synthase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl-N-acylsphingosine β-1,3-D-galactosyltransferase; UDP-galactose:N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-(1→4)-β-D-glucosyl-N-acylsphingosine 3-β-D-galactosyltransferase
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-galactosaminyl-(1→4)-[α-N-acetylneuraminyl-(2→3)]-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 3-β-D-galactosyltransferase
Comments: The substrate is also known as gangloside GM2, the product as gangloside GM1a
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 37217-28-0
References:
1.  Basu, S., Kaufman, B. and Roseman, S. Conversion of Tay-Sachs ganglioside to monosialoganglioside by brain uridine diphosphate D-galactose: glycolipid galactosyltransferase. J. Biol. Chem. 240 (1965) 4115–4117. [PMID: 5842076]
2.  Yip, G.B. and Dain, J.A. The enzymic synthesis of ganglioside. II. UDP-galactose: N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosyl-glucosyl-ceramide galactosyltransferase in rat brain. Biochim. Biophys. Acta 206 (1970) 252–260. [PMID: 4987145]
3.  Yip, M.C.M. and Dain, J.A. Frog brain uridine diphosphate galactose-N-acetylgalactosaminyl-N-acetylneuraminylgalactosylglucosylceramide galactosyltransferase. Biochem. J. 118 (1970) 247–252. [PMID: 5484669]
[EC 2.4.1.62 created 1972, modified 2013]
 
 
*EC 2.4.1.116
Accepted name: cyanidin 3-O-rutinoside 5-O-glucosyltransferase
Reaction: UDP-α-D-glucose + cyanidin-3-O-rutinoside = UDP + cyanidin 3-O-rutinoside 5-O-β-D-glucoside
For diagram of anthocyanidin rutoside biosynthesis, click here
Glossary: cyanidin 3-O-rutinoside = cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): uridine diphosphoglucose-cyanidin 3-rhamnosylglucoside 5-O-glucosyltransferase; cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-D-rhamnosyl-1,6-D-glucoside 5-O-D-glucosyltransferase
Systematic name: UDP-α-D-glucose:cyanidin-3-O-α-L-rhamnosyl-(1→6)-β-D-glucoside 5-O-β-D-glucosyltransferase
Comments: Isolated from the plants Silene dioica (red campion) [1], Iris ensata (Japanese iris) [2] and Iris hollandica (Dutch iris) [3]. Also acts on the 3-O-rutinosides of pelargonidin, delphinidin and malvidin, but not the corresponding glucosides or 6-acylglucosides. The enzyme does not catalyse the glucosylation of the 5-hydroxy group of cyanidin 3-glucoside.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 70248-66-7
References:
1.  Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification, properties, and genetic control of UDP-glucose: cyanidin-3-rhamnosyl-(1→6)-glucoside-5-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1059–1071. [PMID: 751641]
2.  Yabuya, T., Yamaguchi, M., Imayama, T., Katoh, K. and Ino I. Anthocyanin 5-O-glucosyltransferase in flowers of Iris ensata. Plant Sci. 162 (2002) 779–784.
3.  Imayama, T., Yoshihara, Y., Fukuchi-Mizutani, M., Tanaka, Y., Ino, I. and Yabuya, T. Isolation and characterization of a cDNA clone of UDP-glucose:anthocyanin 5-O-glucosyltransferase in Iris hollandica. Plant Sci. 167 (2004) 1243–1248.
[EC 2.4.1.116 created 1984 (EC 2.4.1.235 created 2004, incorporated 2006), modified 2006, modified 2013]
 
 
*EC 2.4.1.238
Accepted name: delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase
Reaction: UDP-α-D-glucose + delphinidin 3,5-di-O-β-D-glucoside = UDP + delphinidin 3,3′,5-tri-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: delphinidin = 3,3′,4′,5,5′,7-hexahydroxyflavylium
Other name(s): UDP-glucose:anthocyanin 3′-O-glucosyltransferase; 3’GT
Systematic name: UDP-α-D-glucose:delphinidin-3,5-di-O-β-D-glucoside 3′-O-glucosyltransferase
Comments: Isolated from the plant Gentiana triflora (clustered gentian).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 380231-41-4
References:
1.  Fukuchi-Mizutani, M., Okuhara, H., Fukui, Y., Nakao, M., Katsumoto, Y., Yonekura-Sakakibara, K., Kusumi, T., Hase, T. and Tanaka, Y. Biochemical and molecular characterization of a novel UDP-glucose:anthocyanin 3′-O-glucosyltransferase, a key enzyme for blue anthocyanin biosynthesis, from gentian. Plant Physiol. 132 (2003) 1652–1663. [PMID: 12857844]
[EC 2.4.1.238 created 2004, modified 2013]
 
 
*EC 2.4.1.275
Accepted name: neolactotriaosylceramide β-1,4-galactosyltransferase
Reaction: UDP-α-D-galactose + N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = UDP + β-D-galactosyl-(1→4)-N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide
For diagram of neolactotetraosylceramide biosynthesis, click here
Glossary: N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide = neolactotriaosylceramide
Other name(s): β4Gal-T4; UDP-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide β-1,4-galactosyltransferase; lactotriaosylceramide β-1,4-galactosyltransferase (incorrect)
Systematic name: UDP-α-D-galactose:N-acetyl-β-D-glucosaminyl-(1→3)-β-D-galactosyl-(1→4)-β-D-glucosyl-(1↔1)-ceramide 4-β-D-galactosyltransferase
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Schwientek, T., Almeida, R., Levery, S.B., Holmes, E.H., Bennett, E. and Clausen, H. Cloning of a novel member of the UDP-galactose:β-N-acetylglucosamine β1,4-galactosyltransferase family, β4Gal-T4, involved in glycosphingolipid biosynthesis. J. Biol. Chem. 273 (1998) 29331–29340. [PMID: 9792633]
[EC 2.4.1.275 created 2011, modified 2013]
 
 
EC 2.4.1.294
Accepted name: cyanidin 3-O-galactosyltransferase
Reaction: UDP-α-D-galactose + cyanidin = UDP + cyanidin 3-O-β-D-galactoside
For diagram of cyanidin galactoside biosynthesis, click here
Glossary: cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): UDP-galactose:cyanidin galactosyltransferase
Systematic name: UDP-α-D-galactose:cyanidin 3-O-galactosyltransferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397–403. [PMID: 8717136]
[EC 2.4.1.294 created 2013]
 
 
EC 2.4.1.295
Accepted name: anthocyanin 3-O-sambubioside 5-O-glucosyltransferase
Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-sambubioside = UDP + an anthocyanidin 5-O-β-D-glucoside 3-O-β-D-sambubioside
For diagram of anthocyanidin sambubioside biosynthesis, click here
Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)
Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-β-D-sambubioside 5-O-glucosyltransferase
Comments: Isolated from the plant Matthiola incana (stock). No activity with anthocyanidin 3-O-glucosides.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Teusch, M., Forkmann, G. and Seyffert, W. Genetic control of UDP-glucose: anthocyanin 5-O-glucosyltransferase from flowers of Matthiola incana R.Br. Planta 168 (1986) 586–591.
[EC 2.4.1.295 created 2013]
 
 
EC 2.4.1.296
Accepted name: anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase
Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] = UDP + an anthocyanidin 3-O-[2-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucoside
For diagram of anthocyanidin rutoside biosynthesis, click here
Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-[3-O-(4-coumaroyl)-α-L-rhamnosyl-(1→6)-β-D-glucoside] 5-O-β-D-glucosyltransferase
Comments: Isolated from the plant Petunia hybrida. It does not act on an anthocyanidin 3-O-rutinoside
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Jonsson, L.M.V., Aarsman, M.E.G., van Diepen, J., de Vlaming, P., Smit, N. and Schram, A.W. Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida. Planta 160 (1984) 341–347.
[EC 2.4.1.296 created 2013]
 
 
EC 2.4.1.297
Accepted name: anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase
Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-sophoroside
For diagram of anthocyanidin glycoside biosynthesis, click here
Glossary: anthocyanidin 3-O-sophoroside = anthocyanidin 3-O-(β-D-glucosyl(1→2)-β-D-glucoside)
Other name(s): 3GGT
Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-glucoside 2′′-O-glucosyltransferase
Comments: Isolated from Ipomoea nil (Japanese morning glory).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Morita, Y., Hoshino, A., Kikuchi, Y., Okuhara, H., Ono, E., Tanaka, Y., Fukui, Y., Saito, N., Nitasaka, E., Noguchi, H. and Iida, S. Japanese morning glory dusky mutants displaying reddish-brown or purplish-gray flowers are deficient in a novel glycosylation enzyme for anthocyanin biosynthesis, UDP-glucose:anthocyanidin 3-O-glucoside-2′′-O-glucosyltransferase, due to 4-bp insertions in the gene. Plant J. 42 (2005) 353–363. [PMID: 15842621]
[EC 2.4.1.297 created 2013]
 
 
EC 2.4.1.298
Accepted name: anthocyanidin 3-O-glucoside 5-O-glucosyltransferase
Reaction: UDP-α-D-glucose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3,5-di-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Other name(s): UDP-glucose:anthocyanin 5-O-glucosyltransferase
Systematic name: UDP-α-D-glucose:anthocyanidin-3-O-β-D-glucoside 5-O-glucosyltransferase
Comments: Isolated from the plants Perilla frutescens var. crispa, Verbena hybrida [1], Dahlia variabilis [2] and Gentiana triflora (clustered gentian) [3]. It will also act on anthocyanidin 3-O-(6-O-malonylglucoside) [2] and is much less active with hydroxycinnamoylglucose derivatives [3]. There is no activity in the absence of the 3-O-glucoside group.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yamazaki, M., Gong, Z., Fukuchi-Mizutani, M., Fukui, Y., Tanaka, Y., Kusumi, T. and Saito, K. Molecular cloning and biochemical characterization of a novel anthocyanin 5-O-glucosyltransferase by mRNA differential display for plant forms regarding anthocyanin. J. Biol. Chem. 274 (1999) 7405–7411. [PMID: 10066805]
2.  Ogata, J., Sakamoto, T., Yamaguchi, M., Kawanobu, S., Yoshitama, K. Isolation and characterization of anthocyanin 5-O-glucosyltransferase from flowers of Dahlia variabilis. J. Plant Physiol. 158 (2001) 709–714.
3.  Nakatsuka, T., Sato, K., Takahashi, H., Yamamura, S. and Nishihara, M. Cloning and characterization of the UDP-glucose:anthocyanin 5-O-glucosyltransferase gene from blue-flowered gentian. J. Exp. Bot. 59 (2008) 1241–1252. [PMID: 18375606]
[EC 2.4.1.298 created 2013]
 
 
EC 2.4.1.299
Accepted name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)
Reaction: 1-O-sinapoyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = sinapate + cyanidin 3,5-di-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: sinapate = 4-hydroxy-3,5-dimethoxycinnamate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): AA5GT
Systematic name: 1-O-sinapoyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 5-O-β-D-glucosyltransferase
Comments: Isolated from the plant Dianthus caryophyllus (carnation). Also acts on other anthocyanidins and with other acyl-glucose donors. cf. EC 2.4.1.298, anthocyanidin 3-O-glucoside 5-O-glucosyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [PMID: 20971893]
2.  Nishizaki, Y., Matsuba, Y., Okamoto, E., Okamura, M., Ozeki, Y. and Sasaki, N. Structure of the acyl-glucose-dependent anthocyanin 5-O-glucosyltransferase gene in carnations and its disruption by transposable elements in some varieties. Mol. Genet. Genomics 286 (2011) 383–394. [PMID: 22048706]
[EC 2.4.1.299 created 2013]
 
 
EC 2.4.1.300
Accepted name: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose)
Reaction: 1-O-vanilloyl-β-D-glucose + cyanidin 3-O-β-D-glucoside = vanillate + cyanidin 3,7-di-O-β-D-glucoside
For diagram of anthocyanidin glucoside biosynthesis, click here
Glossary: vanillate = 4-hydroxy-3-methoxybenzoate
cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): AA7GT
Systematic name: 1-O-vanilloyl-β-D-glucose:cyanidin-3-O-β-D-glucoside 7-O-β-D-glucosyltransferase
Comments: Isolated from the plant Delphinium grandiflorum (delphinium). Also acts on other anthocyanidins and with other acyl-glucose derivatives.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Matsuba, Y., Sasaki, N., Tera, M., Okamura, M., Abe, Y., Okamoto, E., Nakamura, H., Funabashi, H., Takatsu, M., Saito, M., Matsuoka, H., Nagasawa, K. and Ozeki, Y. A novel glucosylation reaction on anthocyanins catalyzed by acyl-glucose-dependent glucosyltransferase in the petals of carnation and delphinium. Plant Cell 22 (2010) 3374–3389. [PMID: 20971893]
[EC 2.4.1.300 created 2013]
 
 
EC 2.4.2.49
Accepted name: neamine phosphoribosyltransferase
Reaction: neamine + 5-phospho-α-D-ribose 1-diphosphate = 5′′-phosphoribostamycin + diphosphate
For diagram of neamine and ribostamycin biosynthesis, click here
Glossary: neamine = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2,3-dihydroxycyclohexyl]oxy}oxane-3,4-diol
ribostamycin = (2R,3S,4R,5R,6R)-5-amino-2-(aminomethyl)-6-{[(1R,2R,3S,4R,6S)-4,6-diamino-2-{[(2S,3R,4S,5R)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy}-3-hydroxycyclohexyl]oxy}oxane-3,4-diol
Other name(s): btrL (gene name); neoM (gene name)
Systematic name: neamine:5-phospho-α-D-ribose 1-diphosphate phosphoribosyltransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including ribostamycin, neomycin and butirosin. The enzyme requires a divalent metal ion, optimally Mg2+, Ni2+ or Co2+.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kudo, F., Fujii, T., Kinoshita, S. and Eguchi, T. Unique O-ribosylation in the biosynthesis of butirosin. Bioorg. Med. Chem. 15 (2007) 4360–4368. [PMID: 17482823]
[EC 2.4.2.49 created 2013]
 
 
EC 2.4.2.50
Accepted name: cyanidin 3-O-galactoside 2′′-O-xylosyltransferase
Reaction: UDP-α-D-xylose + cyanidin 3-O-β-D-galactoside = UDP + cyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-galactoside)
For diagram of cyanidin galactoside biosynthesis, click here
Glossary: cyanidin = 3,3′,4′,5,7-pentahydroxyflavylium
Other name(s): CGXT
Systematic name: UDP-α-D-xylose:cyanidin-3-O-β-D-galactoside 2′′-O-xylosyltransferase
Comments: Isolated from the plant Daucus carota (Afghan cultivar carrot).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Rose, A., Glassgen, W.E., Hopp, W. and Seitz, H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397–403. [PMID: 8717136]
[EC 2.4.2.50 created 2013]
 
 
EC 2.4.2.51
Accepted name: anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase
Reaction: UDP-α-D-xylose + an anthocyanidin 3-O-β-D-glucoside = UDP + an anthocyanidin 3-O-β-D-sambubioside
For diagram of anthocyanidin sambubioside biosynthesis, click here
Glossary: anthocyanidin 3-O-β-D-sambubioside = anthocyanidin 3-O-(β-D-xylosyl-(1→2)-β-D-glucoside)
Other name(s): uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase; UGT79B1
Systematic name: UDP-α-D-xylose:anthocyanidin-3-O-β-D-glucoside 2′′′-O-xylosyltransferase
Comments: Isolated from the plants Matthiola incana (stock) [1] and Arabidopsis thaliana (mouse-eared cress) [2]. The enzyme has similar activity with the 3-glucosides of pelargonidin, cyanidin, delphinidin, quercetin and kaempferol as well as with cyanidin 3-O-rhamnosyl-(1→6)-glucoside and cyanidin 3-O-(6-acylglucoside). There is no activity with other UDP-sugars or with cyanidin 3,5-diglucoside.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Teusch, M. Uridine 5′-diphosphate-xylose:anthocyanidin 3-O-glucose-xylosyltransferase from petals of Matthiola incana R.Br. Planta 169 (1986) 559–563.
2.  Yonekura-Sakakibara, K., Fukushima, A., Nakabayashi, R., Hanada, K., Matsuda, F., Sugawara, S., Inoue, E., Kuromori, T., Ito, T., Shinozaki, K., Wangwattana, B., Yamazaki, M. and Saito, K. Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J. 69 (2012) 154–167. [PMID: 21899608]
[EC 2.4.2.51 created 2013]
 
 
EC 2.6.1.100
Accepted name: L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Reaction: L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine
For diagram of paromamine biosynthesis, click here
Glossary: 2-deoxy-scyllo-inosose = (2S,3R,4S,5R)-2,3,4,5-tetrahydroxycyclohexan-1-one
Other name(s): btrR (gene name); neoB (gene name); kanB (gene name)
Systematic name: L-glutamine:2-deoxy-scyllo-inosose aminotransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.101, L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Tamegai, H., Eguchi, T. and Kakinuma, K. First identification of Streptomyces genes involved in the biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics--genetic and evolutionary analysis of L-glutamine:2-deoxy-scyllo-inosose aminotransferase genes. J. Antibiot. (Tokyo) 55 (2002) 1016–1018. [PMID: 12546424]
2.  Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [PMID: 15827636]
3.  Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [PMID: 16506694]
4.  Jnawali, H.N., Subba, B., Liou, K. and Sohng, J.K. Functional characterization of kanB by complementing in engineered Streptomyces fradiae Δneo6::tsr. Biotechnol. Lett. 31 (2009) 869–875. [PMID: 19219581]
[EC 2.6.1.100 created 2013]
 
 
EC 2.6.1.101
Accepted name: L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase
Reaction: L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine
For diagram of paromamine biosynthesis, click here
Glossary: 3-amino-2,3-dideoxy-scyllo-inosose = (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexan-1-one
Systematic name: L-glutamine:5-amino-2,3,4-trihydroxycyclohexanone aminotransferase
Comments: Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. Also catalyses EC 2.6.1.100, L-glutamine:2-deoxy-scyllo-inosose aminotransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Huang, F., Haydock, S.F., Mironenko, T., Spiteller, D., Li, Y. and Spencer, J.B. The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine. Org. Biomol. Chem. 3 (2005) 1410–1418. [PMID: 15827636]
2.  Kudo, F., Yamamoto, Y., Yokoyama, K., Eguchi, T. and Kakinuma, K. Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773. J. Antibiot. (Tokyo) 58 (2005) 766–774. [PMID: 16506694]
[EC 2.6.1.101 created 2013]
 
 
EC 2.7.7.84
Accepted name: 2′-5′ oligoadenylate synthase
Reaction: 3 ATP = pppA2′p5’A2′p5’A + 2 diphosphate
Glossary: pppA2′p5’A2′p5’A = 5′-triphosphoadenylyl-(2′→5′)-adenylyl-(2′→5′)-adenosine
Other name(s): OAS
Systematic name: ATP:ATP adenylyltransferase (2′-5′ linkages-forming)
Comments: The enzyme is activated by binding to double-stranded RNA. The resulting product binds to and activates RNase L, which subsequently degrades the RNA. Oligoadenylates of chain lengths 2, 4 and 5 are also produced. The dimer does not have any known biological activity [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kerr, I.M. and Brown, R.E. pppA2′p5’A2′p5’A: an inhibitor of protein synthesis synthesized with an enzyme fraction from interferon-treated cells. Proc. Natl. Acad. Sci. USA 75 (1978) 256–260. [PMID: 272640]
2.  Martin, E.M., Birdsall, N.J., Brown, R.E. and Kerr, I.M. Enzymic synthesis, characterisation and nuclear-magnetic-resonance spectra of pppA2′p5’A2′p5’A and related oligonucleotides: comparison with chemically synthesised material. Eur. J. Biochem. 95 (1979) 295–307. [PMID: 456356]
3.  Hartmann, R., Justesen, J., Sarkar, S.N., Sen, G.C. and Yee, V.C. Crystal structure of the 2′-specific and double-stranded RNA-activated interferon-induced antiviral protein 2′-5′-oligoadenylate synthetase. Mol. Cell 12 (2003) 1173–1185. [PMID: 14636576]
4.  Hovanessian, A.G. and Justesen, J. The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie 89 (2007) 779–788. [PMID: 17408844]
[EC 2.7.7.84 created 2013]
 
 
EC 2.7.8.38
Accepted name: archaetidylserine synthase
Reaction: (1) CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine
(2) CDP-2,3-bis-(O-phytanyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine
For diagram of archaetidylserine biosynthesis, click here
Glossary: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol = CDP-unsaturated archaeol
2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine = unsaturated archaetidylserine
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP archaeol
2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine = archaetidylserine
Systematic name: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol:L-serine 2,3-bis-(O-geranylgeranyl)-sn-glycerol phosphotransferase
Comments: Requires Mn2+. Isolated from the archaeon Methanothermobacter thermautotrophicus.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181–1189. [PMID: 12562787]
[EC 2.7.8.38 created 2013, modified 2013]
 
 
EC 3.1.4.55
Accepted name: phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
Reaction: 5-phospho-α-D-ribose 1,2-cyclic phosphate + H2O = α-D-ribose 1,5-bisphosphate
For diagram of phosphonate metabolism, click here
Other name(s): phnP (gene name)
Systematic name: 5-phospho-α-D-ribose 1,2-cyclic phosphate 2-phosphohydrolase (α-D-ribose 1,5-bisphosphate-forming)
Comments: Binds Mn2+ and Zn2+. Isolated from the bacterium Escherichia coli, where it participates in the degradation of methylphosphonate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Podzelinska, K., He, S.M., Wathier, M., Yakunin, A., Proudfoot, M., Hove-Jensen, B., Zechel, D.L. and Jia, Z. Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation. J. Biol. Chem. 284 (2009) 17216–17226. [PMID: 19366688]
2.  Hove-Jensen, B., McSorley, F.R. and Zechel, D.L. Physiological role of phnP-specified phosphoribosyl cyclic phosphodiesterase in catabolism of organophosphonic acids by the carbon-phosphorus lyase pathway. J. Am. Chem. Soc. 133 (2011) 3617–3624. [PMID: 21341651]
3.  He, S.M., Wathier, M., Podzelinska, K., Wong, M., McSorley, F.R., Asfaw, A., Hove-Jensen, B., Jia, Z. and Zechel, D.L. Structure and mechanism of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway. Biochemistry 50 (2011) 8603–8615. [PMID: 21830807]
[EC 3.1.4.55 created 2013]
 
 
EC 3.1.7.4
Deleted entry: Now recognized as two enzymes EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141 sclareol synthase
[EC 3.1.7.4 created 2008, deleted 2013]
 
 
EC 3.5.4.33
Accepted name: tRNA(adenine34) deaminase
Reaction: adenine34 in tRNA + H2O = hypoxanthine34 in tRNA + NH3
Other name(s): tRNA:A34 deaminase; tadA protein; ADAT2-ADAT3 complex; TADA; tRNA adenosine deaminase arginine; AtTadA; tadA/ecADAT2; tRNA A:34 deaminase
Systematic name: tRNA(adenine34) aminohydrolase
Comments: The enzyme is involved in editing of tRNA. The active site contains Zn2+ [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Spears, J.L., Rubio, M.A., Gaston, K.W., Wywial, E., Strikoudis, A., Bujnicki, J.M., Papavasiliou, F.N. and Alfonzo, J.D. A single zinc ion is sufficient for an active Trypanosoma brucei tRNA editing deaminase. J. Biol. Chem. 286 (2011) 20366–20374. [PMID: 21507956]
2.  Delannoy, E., Le Ret, M., Faivre-Nitschke, E., Estavillo, G.M., Bergdoll, M., Taylor, N.L., Pogson, B.J., Small, I., Imbault, P. and Gualberto, J.M. Arabidopsis tRNA adenosine deaminase arginine edits the wobble nucleotide of chloroplast tRNAArg(ACG) and is essential for efficient chloroplast translation. Plant Cell 21 (2009) 2058–2071. [PMID: 19602623]
3.  Kuratani, M., Ishii, R., Bessho, Y., Fukunaga, R., Sengoku, T., Shirouzu, M., Sekine, S. and Yokoyama, S. Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex aeolicus. J. Biol. Chem. 280 (2005) 16002–16008. [PMID: 15677468]
4.  Wolf, J., Gerber, A.P. and Keller, W. tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli. EMBO J. 21 (2002) 3841–3851. [PMID: 12110595]
5.  Lee, W.H., Kim, Y.K., Nam, K.H., Priyadarshi, A., Lee, E.H., Kim, E.E., Jeon, Y.H., Cheong, C. and Hwang, K.Y. Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes. Proteins 68 (2007) 1016–1019. [PMID: 17554781]
6.  Ragone, F.L., Spears, J.L., Wohlgamuth-Benedum, J.M., Kreel, N., Papavasiliou, F.N. and Alfonzo, J.D. The C-terminal end of the Trypanosoma brucei editing deaminase plays a critical role in tRNA binding. RNA 17 (2011) 1296–1306. [PMID: 21602302]
[EC 3.5.4.33 created 2013]
 
 
EC 3.5.4.34
Accepted name: tRNAAla(adenine37) deaminase
Reaction: adenine37 in tRNAAla + H2O = hypoxanthine37 in tRNAAla + NH3
Other name(s): ADAT1; Tad1p
Systematic name: tRNAAla(adenine37) aminohydrolase
Comments: The enzyme deaminates adenosine37 to inosine in eukaryotic tRNAAla [1]. tRNA editing is strictly dependent on Mg2+ [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Maas, S., Gerber, A.P. and Rich, A. Identification and characterization of a human tRNA-specific adenosine deaminase related to the ADAR family of pre-mRNA editing enzymes. Proc. Natl. Acad. Sci. USA 96 (1999) 8895–8900. [PMID: 10430867]
2.  Gerber, A., Grosjean, H., Melcher, T. and Keller, W. Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the mammalian pre-mRNA editing enzymes ADAR1 and ADAR2. EMBO J. 17 (1998) 4780–4789. [PMID: 9707437]
3.  Keegan, L.P., Gerber, A.P., Brindle, J., Leemans, R., Gallo, A., Keller, W. and O'Connell, M.A. The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification. Mol. Cell Biol. 20 (2000) 825–833. [PMID: 10629039]
[EC 3.5.4.34 created 2013]
 
 
EC 3.5.4.35
Accepted name: tRNA(cytosine8) deaminase
Reaction: cytosine8 in tRNA + H2O = uracil8 in tRNA + NH3
Other name(s): CDAT8
Systematic name: tRNA(cytosine8) aminohydrolase
Comments: The enzyme from Methanopyrus kandleri specifically catalyses the deamimation of cytosine at poition 8 of tRNA in 30 different tRNAs. This cytosine-to-uracil editing guarantees the proper folding and functionality of the tRNAs.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Randau, L., Stanley, B.J., Kohlway, A., Mechta, S., Xiong, Y. and Söll, D. A cytidine deaminase edits C to U in transfer RNAs in Archaea. Science 324 (2009) 657–659. [PMID: 19407206]
[EC 3.5.4.35 created 2013]
 
 
EC 3.5.4.36
Accepted name: mRNA(cytosine6666) deaminase
Reaction: cytosine6666 in apolipoprotein B mRNA + H2O = uracil6666 in apolipoprotein B mRNA + NH3
Other name(s): APOBEC-1 (catalytic component of an RNA-editing complex); APOBEC1 (catalytic subunit); apolipoprotein B mRNA-editing enzyme 1 (catalytic component of an RNA-editing complex); apoB mRNA-editing enzyme catalytic polypeptide 1 (catalytic component of an RNA-editing complex); apoB mRNA editing complex; apolipoprotein B mRNA editing enzyme; REPR
Systematic name: mRNA(cytosine6666) aminohydrolase
Comments: The apolipoprotein B mRNA editing enzyme complex catalyses the editing of apolipoprotein B mRNA at cytidine6666 to uridine, thereby transforming the codon for glutamine-2153 to a termination codon. Editing results in translation of a truncated apolipoprotein B isoform (apoB-48) with distinct functions in lipid transport. The catalytic component (APOBEC-1) contains zinc at the active site [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Chester, A., Weinreb, V., Carter, C.W., Jr. and Navaratnam, N. Optimization of apolipoprotein B mRNA editing by APOBEC1 apoenzyme and the role of its auxiliary factor, ACF. RNA 10 (2004) 1399–1411. [PMID: 15273326]
2.  Fujino, T., Navaratnam, N., Jarmuz, A., von Haeseler, A. and Scott, J. C-→U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica. Nucleic Acids Res. 27 (1999) 2662–2671. [PMID: 10373583]
3.  Barnes, C. and Smith, H.C. Apolipoprotein B mRNA editing in vitro is a zinc-dependent process. Biochem. Biophys. Res. Commun. 197 (1993) 1410–1414. [PMID: 8280158]
4.  Chester, A., Somasekaram, A., Tzimina, M., Jarmuz, A., Gisbourne, J., O'Keefe, R., Scott, J. and Navaratnam, N. The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay. EMBO J. 22 (2003) 3971–3982. [PMID: 12881431]
[EC 3.5.4.36 created 2013]
 
 
EC 3.6.1.64
Accepted name: inosine diphosphate phosphatase
Reaction: (1) IDP + H2O = IMP + phosphate
(2) dIDP + H2O = dIMP + phosphate
Other name(s): (deoxy)inosine diphosphatase; NUDT16
Systematic name: inosine diphosphate phosphatase
Comments: The human enzyme also hydrolyses GDP and dGDP, and to a lesser extent ITP, dITP and XTP.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Iyama, T., Abolhassani, N., Tsuchimoto, D., Nonaka, M. and Nakabeppu, Y. NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest. Nucleic Acids Res. 38 (2010) 4834–4843. [PMID: 20385596]
[EC 3.6.1.64 created 2013]
 
 
EC 4.1.3.42
Accepted name: (4S)-4-hydroxy-2-oxoglutarate aldolase
Reaction: (4S)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Glossary: (4S)-4-hydroxy-2-oxoglutatrate = (S)-2-hydroxy-4-oxopentanedioate = L-4-hydroxy-2-oxoglutarate
Other name(s): 2-oxo-4-hydroxyglutarate aldolase (ambiguous); hydroxyketoglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutaric aldolase (ambiguous); 2-keto-4-hydroxyglutaric aldolase (ambiguous); 4-hydroxy-2-ketoglutarate aldolase (ambiguous); 2-keto-4-hydroxyglutarate aldolase (ambiguous); 2-oxo-4-hydroxyglutaric aldolase (ambiguous); hydroxyketoglutarate aldolase (ambiguous); 2-keto-4-hydroxybutyrate aldolase (ambiguous); 4-hydroxy-2-oxoglutarate glyoxylate-lyase (ambiguous); eda (gene name)
Systematic name: (4S)-4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)
Comments: The enzyme from the bacterium Escherichia coli is specific for the (S) enantiomer. That enzyme is trifunctional, and also catalyses the reactions of EC 4.1.1.3, oxaloacetate decarboxylase and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase. cf. EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase.
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9030-81-3
References:
1.  Nishihara, H. and Dekker, E.E. Purification, substrate specificity and binding, β-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. J. Biol. Chem. 247 (1972) 5079–5087. [PMID: 4560498]
2.  Patil, R.V. and Dekker, E.E. Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene. J. Bacteriol. 174 (1992) 102–107. [PMID: 1339418]
[EC 4.1.3.42 created 2013]
 
 
EC 4.2.3.141
Accepted name: sclareol synthase
Reaction: (13E)-8α-hydroxylabd-13-en-15-yl diphosphate + H2O = sclareol + diphosphate
For diagram of labdane, pimarane and phyllocadane diterpenoids biosynthesis, click here
Glossary: sclareol = (13R)-labd-14-ene-8α,13-diol
(13E)-8α-hydroxylabd-13-en-15-yl diphosphate = copal-8-ol diphosphate
Other name(s): SS
Systematic name: (13E)-8α-hydroxylabd-13-en-15-yl-diphosphate-lyase (sclareol forming)
Comments: Isolated from the plant Salvia sclarea (clary sage). Originally thought to be synthesized in one step from geranylgeranyl diphosphate it is now known to require two enzymes, EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141, sclareol synthase. Sclareol is used in perfumery.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Caniard, A., Zerbe, P., Legrand, S., Cohade, A., Valot, N., Magnard, J.L., Bohlmann, J. and Legendre, L. Discovery and functional characterization of two diterpene synthases for sclareol biosynthesis in Salvia sclarea (L.) and their relevance for perfume manufacture. BMC Plant Biol. 12:119 (2012). [PMID: 22834731]
[EC 4.2.3.141 created 2013]
 
 
EC 4.2.3.142
Accepted name: 7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]
Reaction: (2Z,6Z)-farnesyl diphosphate = 7-epizingiberene + diphosphate
Glossary: 7-epizingiberene = (5R)-2-methyl-5-[(2R)-6-methylhept-5-en-2-yl]cyclohexa-1,3-diene
Other name(s): ShZIS (gene name)
Systematic name: (2Z,6Z)-farnesyl-diphosphate lyase (cyclizing; 7-epizingiberene-forming)
Comments: Isolated from the plant Solanum habrochaites. 7-Epizingiberene is a whitefly repellant.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Bleeker, P.M., Mirabella, R., Diergaarde, P.J., Vandoorn, A., Tissier, A., Kant, M.R., Prins, M., de Vos, M., Haring, M.A. and Schuurink, R.C. Improved herbivore resistance in cultivated tomato with the sesquiterpene biosynthetic pathway from a wild relative. Proc. Natl. Acad. Sci. USA 109 (2012) 20124–20129. [PMID: 23169639]
[EC 4.2.3.142 created 2013]
 
 
EC 4.3.99.4
Accepted name: choline trimethylamine-lyase
Reaction: choline = trimethylamine + acetaldehyde
Other name(s): cutC (gene name)
Systematic name: choline trimethylamine-lyase (acetaldehyde-forming)
Comments: The enzyme utilizes a glycine radical to break the C-N bond in choline. Found in choline-degrading anaerobic bacteria.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Craciun, S. and Balskus, E.P. Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme. Proc. Natl. Acad. Sci. USA 109 (2012) 21307–21312. [PMID: 23151509]
[EC 4.3.99.4 created 2013]
 
 
EC 4.7 carbon-phosphorus lyases
 
EC 4.7.1 carbon-phosphorus lyases (only sub-subclass identified to date)
 
EC 4.7.1.1
Accepted name: α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase
Reaction: α-D-ribose 1-methylphosphonate 5-phosphate + S-adenosyl-L-methionine + reduced electron acceptor = α-D-ribose 1,2-cyclic phosphate 5-phosphate + methane + L-methionine + 5′-deoxyadenosine + oxidized electron acceptor
For diagram of phosphonate metabolism, click here
Other name(s): phnJ (gene name)
Systematic name: α-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)
Comments: This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional α-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. α-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and α-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kamat, S.S., Williams, H.J. and Raushel, F.M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480 (2011) 570–573. [PMID: 22089136]
2.  Jochimsen, B., Lolle, S., McSorley, F.R., Nabi, M., Stougaard, J., Zechel, D.L. and Hove-Jensen, B. Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway. Proc. Natl. Acad. Sci. USA 108 (2011) 11393–11398. [PMID: 21705661]
3.  Zhang, Q. and van der Donk, W.A. Answers to the carbon-phosphorus lyase conundrum. Chembiochem 13 (2012) 627–629. [PMID: 22334536]
[EC 4.7.1.1 created 2013, modified 2016]
 
 
EC 5.3.2.7
Accepted name: ascopyrone tautomerase
Reaction: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose
For diagram of the anhydrofructose pathway, click here
Glossary: ascopyrone M = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = (6S)-4-hydroxy-6-(hydroxymethyl)-2H-pyran-3(6H)-one
ascopyrone P = 1,5-anhydro-4-deoxy-D-glycero-hex-1-en-3-ulose = (2S)-5-hydroxy-2-(hydroxymethyl)-2H-pyran-4(3H)-one
Other name(s): ascopyrone isomerase; ascopyrone intramolecular oxidoreductase; 1,5-anhydro-D-glycero-hex-3-en-2-ulose tautomerase; APM tautomerase; ascopyrone P tautomerase; APTM
Systematic name: 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose Δ31-isomerase
Comments: This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase) and EC 4.2.2.13 [exo-(1→4)-α-D-glucan lyase]. Ascopyrone P is an anti-oxidant [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yu, S., Refdahl, C. and Lundt, I. Enzymatic description of the anhydrofructose pathway of glycogen degradation; I. Identification and purification of anhydrofructose dehydratase, ascopyrone tautomerase and α-1,4-glucan lyase in the fungus Anthracobia melaloma. Biochim. Biophys. Acta 1672 (2004) 120–129. [PMID: 15110094]
2.  Yu, S. and Fiskesund, R. The anhydrofructose pathway and its possible role in stress response and signaling. Biochim. Biophys. Acta 1760 (2006) 1314–1322. [PMID: 16822618]
[EC 5.3.2.7 created 2006 as EC 5.3.3.15, transferred 2012 to EC 5.3.2.7]
 
 
EC 5.3.2.8
Accepted name: 4-oxalomesaconate tautomerase
Reaction: (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Glossary: (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate = keto tautomer of 4-oxalomesaconate
(1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate = one of the enol tautomers of 4-oxalomesaconate
Other name(s): GalD
Systematic name: 4-oxalomesaconate ketoenol-isomerase
Comments: This enzyme has been characterized from the bacterium Pseudomonas putida KT2440 and is involved in the degradation pathway of syringate and 3,4,5-trihydroxybenzoate. It catalyses the interconversion of two of the tautomers of 4-oxalomesaconate, a reaction that can also occur spontaneously.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [PMID: 21219457]
[EC 5.3.2.8 created 2011 as 5.3.3.16, modified 2011, transferred 2012 to EC 5.3.2.8]
 
 
EC 5.3.3.15
Transferred entry: ascopyrone tautomerase. Now EC 5.3.2.7, ascopyrone tautomerase
[EC 5.3.3.15 created 2006, deleted 2013]
 
 
EC 5.3.3.16
Transferred entry: 4-oxalomesaconate tautomerase. Now EC 5.3.2.8, 4-oxalomesaconate tautomerase
[EC 5.3.3.16 created 2011, modified 2011, deleted 2013]
 
 
EC 5.4.3.10
Accepted name: phenylalanine aminomutase (L-β-phenylalanine forming)
Reaction: L-phenylalanine = L-β-phenylalanine
Glossary: L-β-phenylalanine = (R)-3-amino-3-phenylpropanoate
Systematic name: L-phenylalanine 2,3-aminomutase [(R)-3-amino-3-phenylpropanoate forming]
Comments: The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO). This unique cofactor is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.11, phenylalanine aminomutase (D-β-phenylalanine forming).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Feng, L., Wanninayake, U., Strom, S., Geiger, J. and Walker, K.D. Mechanistic, mutational, and structural evaluation of a Taxus phenylalanine aminomutase. Biochemistry 50 (2011) 2919–2930. [PMID: 21361343]
[EC 5.4.3.10 created 2013]
 
 
EC 5.4.3.11
Accepted name: phenylalanine aminomutase (D-β-phenylalanine forming)
Reaction: L-phenylalanine = D-β-phenylalanine
Glossary: D-β-phenylalanine = (S)-3-amino-3-phenylpropanoate
Other name(s): admH (gene name); L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate]
Systematic name: L-phenylalanine 2,3-aminomutase [(S)-3-amino-3-phenylpropanoate-forming]
Comments: The enzyme from the bacterium Pantoea agglomerans produces D-β-phenylalanine, an intermediate in the biosynthesis of the polyketide non-ribosomal antibiotic andrimid. The enzyme contains the cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO), which is formed autocatalytically by cyclization and dehydration of the three amino-acid residues alanine, serine and glycine. cf. EC 5.4.3.10, phenylalanine aminomutase (L-β-phenylalanine forming).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ratnayake, N.D., Wanninayake, U., Geiger, J.H. and Walker, K.D. Stereochemistry and mechanism of a microbial phenylalanine aminomutase. J. Am. Chem. Soc. 133 (2011) 8531–8533. [PMID: 21561099]
[EC 5.4.3.11 created 2013]
 
 
*EC 6.3.1.14
Accepted name: diphthine—ammonia ligase
Reaction: ATP + diphthine-[translation elongation factor 2] + NH3 = AMP + diphosphate + diphthamide-[translation elongation factor 2]
For diagram of diphthamide biosynthesis, click here
Glossary: translation elongation factor 2 = EF2 = eEF2
diphthine = 2-[(3S)-3-carboxy-3-(trimethylammonio)propyl]-L-histidine
diphthamide =2-[(3S)-3-carbamoyl-3-(trimethylammonio)propyl]-L-histidine
Other name(s): diphthamide synthase; diphthamide synthetase; DPH6 (gene name); ATPBD4 (gene name); diphthine:ammonia ligase (AMP-forming)
Systematic name: diphthine-[translation elongation factor 2]:ammonia ligase (AMP-forming)
Comments: This amidase catalyses the last step in the conversion of an L-histidine residue in the translation elongation factor EF2 to diphthamide. This factor is found in all archaebacteria and eukaryotes, but not in eubacteria, and is the target of bacterial toxins such as the diphtheria toxin and the Pseudomonas exotoxin A (see EC 2.4.2.36, NAD+—diphthamide ADP-ribosyltransferase). The substrate of the enzyme, diphthine, is produced by EC 2.1.1.98, diphthine synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 114514-33-9
References:
1.  Moehring, T.J. and Moehring, J.M. Mutant cultured cells used to study the synthesis of diphthamide. UCLA Symp. Mol. Cell. Biol. New Ser. 45 (1987) 53–63.
2.  Moehring, J.M. and Moehring, T.J. The post-translational trimethylation of diphthamide studied in vitro. J. Biol. Chem. 263 (1988) 3840–3844. [PMID: 3346227]
3.  Su, X., Lin, Z., Chen, W., Jiang, H., Zhang, S. and Lin, H. Chemogenomic approach identified yeast YLR143W as diphthamide synthetase. Proc. Natl. Acad. Sci. USA 109 (2012) 19983–19987. [PMID: 23169644]
[EC 6.3.1.14 created 1990 as EC 6.3.2.22, transferred 2010 to EC 6.3.1.14, modified 2013]
 
 


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