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 To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.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 1.1.1.153 sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
EC 1.1.1.318 eugenol synthase
EC 1.1.1.319 isoeugenol synthase
EC 1.1.1.320 benzil reductase [(S)-benzoin forming]
EC 1.1.1.321 benzil reductase [(R)-benzoin forming]
EC 1.1.1.322 (–)-endo-fenchol dehydrogenase
EC 1.1.1.323 (+)-thujan-3-ol dehydrogenase
EC 1.1.1.324 8-hydroxygeraniol dehydrogenase
EC 1.1.1.325 sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
EC 1.1.1.326 zerumbone synthase
EC 1.3.8.3 (R)-benzylsuccinyl-CoA dehydrogenase
EC 1.3.8.4 isovaleryl-CoA dehydrogenase
EC 1.3.99.10 transferred
EC 1.3.99.21 transferred
EC 1.3.99.32 glutaryl-CoA dehydrogenase (acceptor)
EC 1.14.13.150 α-humulene 10-hydroxylase
EC 1.14.13.151 linalool 8-monooxygenase
EC 1.14.13.152 geraniol 8-hydroxylase
EC 1.14.13.153 (+)-sabinene 3-hydroxylase
EC 1.14.13.154 erythromycin 12-hydroxylase
EC 1.14.99.28 transferred
EC 1.14.99.46 pyrimidine oxygenase
EC 1.17.2.2 lupanine 17-hydroxylase (cytochrome c)
*EC 2.1.1.90 methanol—corrinoid protein Co-methyltransferase
EC 2.1.1.243 2-ketoarginine methyltransferase
EC 2.1.1.244 protein N-terminal methyltransferase
EC 2.1.1.245 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
EC 2.1.1.246 [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
EC 2.1.1.247 [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
EC 2.1.1.248 methylamine—corrinoid protein Co-methyltransferase
EC 2.1.1.249 dimethylamine—corrinoid protein Co-methyltransferase
EC 2.1.1.250 trimethylamine—corrinoid protein Co-methyltransferase
EC 2.1.1.251 methylated-thiol—coenzyme M methyltransferase
EC 2.1.1.252 tetramethylammonium—corrinoid protein Co-methyltransferase
EC 2.1.1.253 [methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase
EC 2.1.1.254 erythromycin 3′′-O-methyltransferase
EC 2.1.1.255 geranyl diphosphate 2-C-methyltransferase
EC 2.4.1.279 nigerose phosphorylase
EC 2.4.1.280 N,N′-diacetylchitobiose phosphorylase
EC 2.4.1.281 4-O-β-D-mannosyl-D-glucose phosphorylase
EC 2.4.99.16 starch synthase (maltosyl-transferring)
EC 2.7.1.173 nicotinate riboside kinase
EC 2.7.1.174 diacylglycerol kinase (CTP)
EC 2.7.1.175 maltokinase
EC 2.7.1.176 UDP-N-acetylglucosamine kinase
EC 3.1.3.87 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
EC 3.1.7.11 geranyl diphosphate diphosphatase
*EC 3.2.1.28 α,α-trehalase
EC 3.5.1.110 peroxyureidoacrylate/ureidoacrylate amidohydrolase
EC 4.1.1.94 ethylmalonyl-CoA decarboxylase
EC 4.1.2.50 6-carboxytetrahydropterin synthase
EC 4.2.1.132 2-hydroxyhexa-2,4-dienoate hydratase
EC 4.2.3.14 deleted
EC 4.2.3.105 tricyclene synthase
EC 4.2.3.106 (E)-β-ocimene synthase
EC 4.2.3.107 (+)-car-3-ene synthase
EC 4.2.3.108 1,8-cineole synthase
EC 4.2.3.109 (-)-sabinene synthase
EC 4.2.3.110 (+)-sabinene synthase
EC 4.2.3.111 (-)-α-terpineol synthase
EC 4.2.3.112 (+)-α-terpineol synthase
EC 4.2.3.113 terpinolene synthase
EC 4.2.3.114 γ-terpinene synthase
EC 4.2.3.115 α-terpinene synthase
EC 4.2.3.116 (+)-camphene synthase
EC 4.2.3.117 (-)-camphene synthase
EC 4.2.3.118 2-methylisoborneol synthase
EC 4.2.3.119 (-)-α-pinene synthase
EC 4.2.3.120 (-)-β-pinene synthase
EC 4.2.3.121 (+)-α-pinene synthase
EC 4.2.3.122 (+)-β-pinene synthase
EC 4.2.3.123 β-sesquiphellandrene synthase
EC 5.3.2.5 2,3-diketo-5-methylthiopentyl-1-phosphate enolase
EC 5.3.99.10 thiazole tautomerase
*EC 5.5.1.8 (+)-bornyl diphosphate synthase
EC 5.5.1.22 (–)-bornyl diphosphate synthase
EC 6.3.4.20 7-cyano-7-deazaguanine synthase


*EC 1.1.1.153
Accepted name: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)
Reaction: (1) L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
(2) L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
For diagram of biopterin biosynthesis, click here
Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one
Other name(s): SR
Systematic name: L-erythro-7,8-dihydrobiopterin:NADP+ oxidoreductase
Comments: This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9059-48-7
References:
1.  Katoh, S. Sepiapterin reductase from horse liver: purification and properties of the enzyme. Arch. Biochem. Biophys. 146 (1971) 202–214. [PMID: 4401291]
2.  Matsubara, M., Katoh, S., Akino, M. and Kaufman, S. Sepiapterin reductase. Biochim. Biophys. Acta 122 (1966) 202–212. [PMID: 5969298]
3.  Werner, E.R., Schmid, M., Werner-Felmayer, G., Mayer, B. and Wachter, H. Synthesis and characterization of 3H-labelled tetrahydrobiopterin. Biochem. J. 304 (1994) 189–193. [PMID: 7528005]
4.  Kim, Y.A., Chung, H.J., Kim, Y.J., Choi, Y.K., Hwang, Y.K., Lee, S.W. and Park, Y.S. Characterization of recombinant Dictyostelium discoideum sepiapterin reductase expressed in E. coli. Mol. Cells 10 (2000) 405–410. [PMID: 10987137]
[EC 1.1.1.153 created 1972, modified 2012]
 
 
EC 1.1.1.318
Accepted name: eugenol synthase
Reaction: eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
Other name(s): LtCES1; EGS1; EGS2
Systematic name: eugenol:NADP+ oxidoreductase (coniferyl ester reducing)
Comments: The enzyme acts in the opposite direction. The enzymes from the plants Ocimum basilicum (sweet basil) [1,3], Clarkia breweri and Petunia hybrida [4] only accept coniferyl acetate and form eugenol. The enzyme from Pimpinella anisum (anise) forms anol (from 4-coumaryl acetate) in vivo, although the recombinant enzyme can form eugenol from coniferyl acetate [5]. The enzyme from Larrea tridentata (creosote bush) also forms chavicol from a coumaryl ester and can use NADH [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128–10133. [PMID: 16782809]
2.  Vassão, D.G., Kim, S.J., Milhollan, J.K., Eichinger, D., Davin, L.B. and Lewis, N.G. A pinoresinol-lariciresinol reductase homologue from the creosote bush (Larrea tridentata) catalyzes the efficient in vitro conversion of p-coumaryl/coniferyl alcohol esters into the allylphenols chavicol/eugenol, but not the propenylphenols p-anol/isoeugenol. Arch. Biochem. Biophys. 465 (2007) 209–218. [PMID: 17624297]
3.  Louie, G.V., Baiga, T.J., Bowman, M.E., Koeduka, T., Taylor, J.H., Spassova, S.M., Pichersky, E. and Noel, J.P. Structure and reaction mechanism of basil eugenol synthase. PLoS One 2 (2007) e993. [PMID: 17912370]
4.  Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362–374. [PMID: 18208524]
5.  Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384–394. [PMID: 18987218]
[EC 1.1.1.318 created 2012]
 
 
EC 1.1.1.319
Accepted name: isoeugenol synthase
Reaction: isoeugenol + acetate + NADP+ = coniferyl acetate + NADPH + H+
Other name(s): IGS1; t-anol/isoeugenol synthase 1
Systematic name: eugenol:NADP+ oxidoreductase (coniferyl acetate reducing)
Comments: The enzyme acts in the opposite direction. In Ocimum basilicum (sweet basil), Clarkia breweri and Petunia hybrida only isoeugenol is formed [1,2]. However in Pimpinella anisum (anise) only anol is formed in vivo, although the cloned enzyme does produce isoeugenol [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Koeduka, T., Fridman, E., Gang, D.R., Vassão, D.G., Jackson, B.L., Kish, C.M., Orlova, I., Spassova, S.M., Lewis, N.G., Noel, J.P., Baiga, T.J., Dudareva, N. and Pichersky, E. Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester. Proc. Natl. Acad. Sci. USA 103 (2006) 10128–10133. [PMID: 16782809]
2.  Koeduka, T., Louie, G.V., Orlova, I., Kish, C.M., Ibdah, M., Wilkerson, C.G., Bowman, M.E., Baiga, T.J., Noel, J.P., Dudareva, N. and Pichersky, E. The multiple phenylpropene synthases in both Clarkia breweri and Petunia hybrida represent two distinct protein lineages. Plant J. 54 (2008) 362–374. [PMID: 18208524]
3.  Koeduka, T., Baiga, T.J., Noel, J.P. and Pichersky, E. Biosynthesis of t-anethole in anise: characterization of t-anol/isoeugenol synthase and an O-methyltransferase specific for a C7-C8 propenyl side chain. Plant Physiol. 149 (2009) 384–394. [PMID: 18987218]
[EC 1.1.1.319 created 2012]
 
 
EC 1.1.1.320
Accepted name: benzil reductase [(S)-benzoin forming]
Reaction: (S)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (S)-benzoin = (2S)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione
Other name(s): YueD
Systematic name: (S)-benzoin:NADP+ oxidoreductase
Comments: The enzyme also reduces 1-phenylpropane-1,2-dione. The enzyme from Bacillus cereus in addition reduces 1,4-naphthoquinone and 1-(4-methylphenyl)-2-phenylethane-1,2-dione with high efficiency [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. Isolation and expression of a Bacillus cereus gene encoding benzil reductase. Biotechnol. Bioeng. 75 (2001) 630–633. [PMID: 11745140]
2.  Maruyama, R., Nishizawa, M., Itoi, Y., Ito, S. and Inoue, M. The enzymes with benzil reductase activity conserved from bacteria to mammals. J. Biotechnol. 94 (2002) 157–169. [PMID: 11796169]
[EC 1.1.1.320 created 2012]
 
 
EC 1.1.1.321
Accepted name: benzil reductase [(R)-benzoin forming]
Reaction: (R)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (R)-benzoin = (2R)-2-hydroxy-1,2-diphenylethanone
benzil = 1,2-diphenylethane-1,2-dione
Systematic name: (R)-benzoin:NADP+ oxidoreductase
Comments: The enzyme from the bacterium Xanthomonas oryzae is able to reduce enantioselectively only one of the two carbonyl groups of benzil to give optically active (R)-benzoin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Konishi, J., Ohta, H. and Tuchihashi, G. Asymmetric reduction of benzil to benzoin catalyzed by the enzyme system of a microorganism. Chem. Lett. 14 (1985) 1111–1112.
[EC 1.1.1.321 created 2012]
 
 
EC 1.1.1.322
Accepted name: (–)-endo-fenchol dehydrogenase
Reaction: (–)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+
For diagram of pinene and related monoterpenoids, click here
Other name(s): l-endo-fenchol dehydrogenase; FDH
Systematic name: (–)-endo-fenchol:NAD(P)+ oxidoreductase
Comments: Isolated from the plant Foeniculum vulgare (fennel). NADH is slightly preferred to NADPH.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343–1347.
[EC 1.1.1.322 created 2012]
 
 
EC 1.1.1.323
Accepted name: (+)-thujan-3-ol dehydrogenase
Reaction: (+)-thujan-3-ol + NAD(P)+ = (+)-thujan-3-one + NAD(P)H + H+
Other name(s): d-3-thujanol dehydrogenase; TDH
Systematic name: (+)-thujan-3-ol:NAD(P)+ oxidoreductase
Comments: Isolated from the plant Tanacetum vulgare (tansy). NADH is preferred to NADPH.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Croteau, R. and Felton, N.M. Substrate specificity of monoterpenol dehydrogenases from Foeniculum vulgare and Tanacetum vulgare. Phytochemistry 19 (1980) 1343–1347.
[EC 1.1.1.323 created 2012]
 
 
EC 1.1.1.324
Accepted name: 8-hydroxygeraniol dehydrogenase
Reaction: (6E)-8-hydroxygeraniol + 2 NADP+ = (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction)
(1a) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-hydroxygeranial + NADPH + H+
(1b) (6E)-8-hydroxygeraniol + NADP+ = (6E)-8-oxogeraniol + NADPH + H+
(1c) (6E)-8-hydroxygeranial + NADP+ = (6E)-8-oxogeranial + NADPH + H+
(1d) (6E)-8-oxogeraniol + NADP+ = (6E)-8-oxogeranial + NADPH + H+
For diagram of acyclic monoterpenoid biosynthesis, click here
Other name(s): 8-hydroxygeraniol oxidoreductase; CYP76B10; G10H; CrG10H; SmG10H; acyclic monoterpene primary alcohol:NADP+ oxidoreductase
Systematic name: (6E)-8-hydroxygeraniol:NADP+ oxidoreductase
Comments: Contains Zn2+. The enzyme catalyses the oxidation of (6E)-8-hydroxygeraniol to (6E)-8-oxogeranial via either (6E)-8-hydroxygeranial or (6E)-8-oxogeraniol. Also acts on geraniol, nerol and citronellol. May be identical to EC 1.1.1.183 geraniol dehydrogenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the substrate rather than 10-hydroxygeraniol as used by references 1 and 2. See prenol nomenclature Pr-1.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ikeda, H., Esaki, N., Nakai, S., Hashimoto, K., Uesato, S., Soda, K. and Fujita, T. Acyclic monoterpene primary alcohol:NADP+ oxidoreductase of Rauwolfia serpentina cells: the key enzyme in biosynthesis of monoterpene alcohols. J. Biochem. 109 (1991) 341–347. [PMID: 1864846]
2.  Hallahan, D.L., West, J.M., Wallsgrove, R.M., Smiley, D.W., Dawson, G.W., Pickett, J.A. and Hamilton, J.G. Purification and characterization of an acyclic monoterpene primary alcohol:NADP+ oxidoreductase from catmint (Nepeta racemosa). Arch. Biochem. Biophys. 318 (1995) 105–112. [PMID: 7726550]
[EC 1.1.1.324 created 2012]
 
 
EC 1.1.1.325
Accepted name: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
Reaction: (1) L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
(2) L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-4(3H)-one
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one
Systematic name: L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase
Comments: This enzyme, isolated from the bacterium Chlorobium tepidum, catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. cf. EC 1.1.1.153, sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming).
Links to other databases: BRENDA, EXPASY, GTD, IUBMB, KEGG, PDB, CAS registry number: 9059-48-7
References:
1.  Cho, S.H., Na, J.U., Youn, H., Hwang, C.S., Lee, C.H. and Kang, S.O. Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum. Biochem. J. 340 (1999) 497–503. [PMID: 10333495]
2.  Supangat, S., Choi, Y.K., Park, Y.S., Son, D., Han, C.D. and Lee, K.H. Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 202–204. [PMID: 16510994]
[EC 1.1.1.325 created 2012]
 
 
EC 1.1.1.326
Accepted name: zerumbone synthase
Reaction: 10-hydroxy-α-humulene + NAD+ = zerumbone + NADH + H+
For diagram of zerumbone biosynthesis, click here
Other name(s): ZSD1
Systematic name: 10-hydroxy-α-humulene:NAD+ oxidoreductase
Comments: The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Okamoto, S., Yu, F., Harada, H., Okajima, T., Hattan, J., Misawa, N. and Utsumi, R. A short-chain dehydrogenase involved in terpene metabolism from Zingiber zerumbet. FEBS J. 278 (2011) 2892–2900. [PMID: 21668645]
[EC 1.1.1.326 created 2012]
 
 
EC 1.3.8.3
Accepted name: (R)-benzylsuccinyl-CoA dehydrogenase
Reaction: (R)-2-benzylsuccinyl-CoA + electron-transfer flavoprotein = (E)-2-benzylidenesuccinyl-CoA + reduced electron-transfer flavoprotein
For diagram of anaerobic toluene catabolism, click here
Other name(s): BbsG; (R)-benzylsuccinyl-CoA:(acceptor) oxidoreductase
Systematic name: (R)-benzylsuccinyl-CoA:electron transfer flavoprotein oxidoreductase
Comments: Requires FAD as prosthetic group. Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity; it is highly specific for (R)-benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA. Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica. Ferricenium ion is an effective artificial electron acceptor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD
References:
1.  Leutwein, C. and Heider, J. Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and β-oxidation of the first intermediate, (R)-(+)-benzylsuccinate. Microbiology 145 (1999) 3265–3271. [PMID: 10589736]
2.  Leutwein, C. and Heider, J. (R)-Benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme of the anaerobic toluene catabolic pathway. Arch. Microbiol. 178 (2002) 517–524. [PMID: 12420174]
[EC 1.3.8.3 created 2003 as EC 1.3.99.21, transferred 2012 to EC 1.3.8.3]
 
 
EC 1.3.8.4
Accepted name: isovaleryl-CoA dehydrogenase
Reaction: isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
Other name(s): isovaleryl-coenzyme A dehydrogenase; isovaleroyl-coenzyme A dehydrogenase; 3-methylbutanoyl-CoA:(acceptor) oxidoreductase
Systematic name: 3-methylbutanoyl-CoA:electron-transfer flavoprotein oxidoreductase
Comments: Contains FAD as prosthetic group. Pentanoate can act as donor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 37274-61-6
References:
1.  Bachhawat, B.K., Robinson, W.G. and Coon, M.J. Enzymatic carboxylation of β-hydroxyisovaleryl coenzyme A. J. Biol. Chem. 219 (1956) 539–550. [PMID: 13319276]
2.  Ikeda, Y. and Tanaka, K. Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J. Biol. Chem. 258 (1983) 1077–1085. [PMID: 6401713]
3.  Tanaka, K., Budd, M.A., Efron, M.L. and Isselbacher, K.J. Isovaleric acidemia: a new genetic defect of leucine metabolism. Proc. Natl. Acad. Sci. USA 56 (1966) 236–242. [PMID: 5229850]
[EC 1.3.8.4 created 1978 as EC 1.3.99.10, modified 1986, transferred 2012 to EC 1.3.8.4]
 
 
EC 1.3.99.10
Transferred entry: isovaleryl-CoA dehydrogenase. Now EC 1.3.8.4, isovaleryl-CoA dehydrogenase
[EC 1.3.99.10 created 1978, modified 1986, deleted 2012]
 
 
EC 1.3.99.21
Transferred entry: (R)-benzylsuccinyl-CoA dehydrogenase. Now EC 1.3.8.3, (R)-benzylsuccinyl-CoA dehydrogenase
[EC 1.3.99.21 created 2003 as EC 1.3.99.21, deleted 2012]
 
 
EC 1.3.99.32
Accepted name: glutaryl-CoA dehydrogenase (acceptor)
Reaction: glutaryl-CoA + acceptor = (E)-glutaconyl-CoA + reduced acceptor
Glossary: (E)-glutaconyl-CoA = (2E)-4-carboxybut-2-enoyl-CoA
Other name(s): GDHDes; nondecarboxylating glutaryl-coenzyme A dehydrogenase; nondecarboxylating glutaconyl-coenzyme A-forming GDH; glutaryl-CoA dehydrogenase (non-decarboxylating)
Systematic name: glutaryl-CoA:acceptor 2,3-oxidoreductase (non-decarboxylating)
Comments: The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wischgoll, S., Taubert, M., Peters, F., Jehmlich, N., von Bergen, M. and Boll, M. Decarboxylating and nondecarboxylating glutaryl-coenzyme A dehydrogenases in the aromatic metabolism of obligately anaerobic bacteria. J. Bacteriol. 191 (2009) 4401–4409. [PMID: 19395484]
2.  Wischgoll, S., Demmer, U., Warkentin, E., Gunther, R., Boll, M. and Ermler, U. Structural basis for promoting and preventing decarboxylation in glutaryl-coenzyme A dehydrogenases. Biochemistry 49 (2010) 5350–5357. [PMID: 20486657]
[EC 1.3.99.32 created 2012, modified 2013]
 
 
EC 1.14.13.150
Accepted name: α-humulene 10-hydroxylase
Reaction: α-humulene + O2 + NADPH + H+ = 10-hydroxy-α-humulene + NADP+ + H2O
For diagram of zerumbone biosynthesis, click here
Other name(s): CYP71BA1
Systematic name: α-humulene,NADPH:oxygen 10-oxidoreductase
Comments: Requires cytochrome P-450. The recommended numbering of humulene gives 10-hydroxy-α-humulene as the product rather than 8-hydroxy-α-humulene as used by the reference. See Section F: Natural Product Nomenclature.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yu, F., Okamoto, S., Harada, H., Yamasaki, K., Misawa, N. and Utsumi, R. Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. Cell. Mol. Life Sci. 68 (2011) 1033–1040. [PMID: 20730551]
[EC 1.14.13.150 created 2012]
 
 
EC 1.14.13.151
Accepted name: linalool 8-monooxygenase
Reaction: linalool + 2 NADH + 2 H+ + 2 O2 = (6E)-8-oxolinalool + 2 NAD+ + 3 H2O (overall reaction)
(1a) linalool + NADH + H+ + O2 = (6E)-8-hydroxylinalool + NAD+ + H2O
(1b) (6E)-8-hydroxylinalool + NADH + H+ + O2 = (6E)-8-oxolinalool + NAD+ + 2 H2O
For diagram of acyclic monoterpenoid biosynthesis, click here
Glossary: linalool = 3,7-dimethylocta-1,6-dien-3-ol
Other name(s): P-450lin; CYP111
Systematic name: linalool,NADH:oxygen oxidoreductase (8-hydroxylating)
Comments: A heme-thiolate protein (P-450). The secondary electron donor is a specific [2Fe-2S] ferredoxin from the same bacterial strain.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ullah, A.J., Murray, R.I., Bhattacharyya, P.K., Wagner, G.C. and Gunsalus, I.C. Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase. J. Biol. Chem. 265 (1990) 1345–1351. [PMID: 2295633]
2.  Ropp, J.D., Gunsalus, I.C. and Sligar, S.G. Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita. J. Bacteriol. 175 (1993) 6028–6037. [PMID: 8376348]
[EC 1.14.13.151 created 1989 as EC 1.14.99.28, transferred 2012 to EC 1.14.13.151]
 
 
EC 1.14.13.152
Accepted name: geraniol 8-hydroxylase
Reaction: geraniol + NADPH + H+ + O2 = (6E)-8-hydroxygeraniol + NADP+ + H2O
For diagram of acyclic monoterpenoid biosynthesis, click here
Other name(s): CYP76B6; G10H; CrG10H; SmG10H
Systematic name: geraniol,NADPH:oxygen oxidoreductase (8-hydroxylating)
Comments: Requires cytochrome P-450. Also hydroxylates nerol and citronellol, cf. EC 1.14.13.151 linalool 8-monooxygenase. The recommended numbering of geraniol gives 8-hydroxygeraniol as the product rather than 10-hydroxygeraniol as used by references 1-3. See prenol nomenclature Pr-1. The cloned enzyme also catalysed, but less efficiently, the 3′-hydroxylation of naringenin (cf. EC 1.14.13.21, flavonoid 3′-monooxygenase) [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Collu, G., Unver, N., Peltenburg-Looman, A.M., van der Heijden, R., Verpoorte, R. and Memelink, J. Geraniol 10-hydroxylase, a cytochrome P450 enzyme involved in terpenoid indole alkaloid biosynthesis. FEBS Lett. 508 (2001) 215–220. [PMID: 11718718]
2.  Wang, J., Liu, Y., Cai, Y., Zhang, F., Xia, G. and Xiang, F. Cloning and functional analysis of geraniol 10-hydroxylase, a cytochrome P450 from Swertia mussotii Franch. Biosci. Biotechnol. Biochem. 74 (2010) 1583–1590. [PMID: 20699579]
3.  Sung, P.H., Huang, F.C., Do, Y.Y. and Huang, P.L. Functional expression of geraniol 10-hydroxylase reveals its dual function in the biosynthesis of terpenoid and phenylpropanoid. J. Agric. Food Chem. 59 (2011) 4637–4643. [PMID: 21504162]
[EC 1.14.13.152 created 2012]
 
 
EC 1.14.13.153
Accepted name: (+)-sabinene 3-hydroxylase
Reaction: (+)-sabinene + NADPH + H+ + O2 = (+)-cis-sabinol + NADP+ + H2O
For diagram of thujane monoterpenoid biosynthesis, click here
Systematic name: (+)-sabinene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires cytochrome P-450. The enzyme has been characterized from Salvia officinalis (sage).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Karp, F., Harris, J.L. and Croteau, R. Metabolism of monoterpenes: demonstration of the hydroxylation of (+)-sabinene to (+)-cis-sabinol by an enzyme preparation from sage (Salvia officinalis) leaves. Arch. Biochem. Biophys. 256 (1987) 179–193. [PMID: 3111374]
[EC 1.14.13.153 created 2012]
 
 
EC 1.14.13.154
Accepted name: erythromycin 12-hydroxylase
Reaction: erythromycin D + NADPH + H+ + O2 = erythromycin C + NADP+ + H2O
For diagram of erythromycin biosynthesis, click here
Other name(s): EryK
Systematic name: erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis. It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Lambalot, R.H., Cane, D.E., Aparicio, J.J. and Katz, L. Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. Biochemistry 34 (1995) 1858–1866. [PMID: 7849045]
2.  Savino, C., Montemiglio, L.C., Sciara, G., Miele, A.E., Kendrew, S.G., Jemth, P., Gianni, S. and Vallone, B. Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate. J. Biol. Chem. 284 (2009) 29170–29179. [PMID: 19625248]
3.  Montemiglio, L.C., Gianni, S., Vallone, B. and Savino, C. Azole drugs trap cytochrome P450 EryK in alternative conformational states. Biochemistry 49 (2010) 9199–9206. [PMID: 20845962]
[EC 1.14.13.154 created 2012]
 
 
EC 1.14.99.28
Transferred entry: linalool 8-monooxygenase. Now EC 1.14.13.151, linalool 8-monooxygenase
[EC 1.14.99.28 created 1989, deleted 2012]
 
 
EC 1.14.99.46
Accepted name: pyrimidine oxygenase
Reaction: (1) uracil + FMNH2 + O2 = (Z)-3-ureidoacrylate peracid + FMN
(2) thymine + FMNH2 + O2 = (Z)-2-methylureidoacrylate peracid + FMN
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
Other name(s): RutA
Systematic name: uracil,FMNH2:oxygen oxidoreductase (uracil hydroxylating, ring-opening)
Comments: In vitro the product (Z)-3-ureidoacrylate peracid is spontaneously reduced to ureidoacrylate [1,2]. Part of the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Mukherjee, T., Zhang, Y., Abdelwahed, S., Ealick, S.E. and Begley, T.P. Catalysis of a flavoenzyme-mediated amide hydrolysis. J. Am. Chem. Soc. 132 (2010) 5550–5551. [PMID: 20369853]
2.  Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089–4102. [PMID: 20400551]
[EC 1.14.99.46 created 2012]
 
 
EC 1.17.2.2
Accepted name: lupanine 17-hydroxylase (cytochrome c)
Reaction: lupanine + 2 ferricytochrome c + H2O = 17-hydroxylupanine + 2 ferrocytochrome c + 2 H+
Other name(s): lupanine dehydrogenase (cytochrome c)
Systematic name: lupanine:cytochrome c-oxidoreductase (17-hydroxylating)
Comments: The enzyme isolated from Pseudomonas putida contains heme c and requires pyrroloquinoline quinone (PQQ) for activity
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Hopper, D.J., Rogozinski, J. and Toczko, M. Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp. Biochem. J. 279 (1991) 105–109. [PMID: 1656935]
2.  Hopper, D.J. and Kaderbhai, M.A. The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida. Biochim. Biophys. Acta 1647 (2003) 110–115. [PMID: 12686118]
[EC 1.17.2.2 created 2012]
 
 
*EC 2.1.1.90
Accepted name: methanol—corrinoid protein Co-methyltransferase
Reaction: methanol + a [Co(I) methanol-specific corrinoid protein] = a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
Other name(s): methanol cobalamin methyltransferase; methanol:5-hydroxybenzimidazolylcobamide methyltransferase; MT 1 (ambiguous); methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase; mtaB (gene name)
Systematic name: methanol:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of methyl groups from methanol to a methanol-specific corrinoid protein (MtaC), is involved in methanogenesis from methanol. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. Free cob(I)alamin can substitute for the corrinoid protein in vitro [2]. Inactivated by oxygen and other oxidizing agents, and reactivated by catalytic amounts of ATP and hydrogen.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 86611-98-5
References:
1.  van der Meijden, P., te Brömmelstroet, B.W., Poirot, C.M., van der Drift, C. and Vogels, G.D. Purification and properties of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri. J. Bacteriol. 160 (1984) 629–635. [PMID: 6438059]
2.  Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674–681. [PMID: 10215883]
[EC 2.1.1.90 created 1989, modified 2012]
 
 
EC 2.1.1.243
Accepted name: 2-ketoarginine methyltransferase
Reaction: S-adenosyl-L-methionine + 5-guanidino-2-oxopentanoate = S-adenosyl-L-homocysteine + 5-guanidino-3-methyl-2-oxopentanoate
Glossary: 5-guanidino-2-oxopentanoate = 2-ketoarginine
5-guanidino-3-methyl-2-oxopentanoate = 5-carbamimidamido-3-methyl-2-oxopentanoate
Other name(s): mrsA (gene name)
Systematic name: S-adenosyl-L-methionine:5-carbamimidamido-2-oxopentanoate S-methyltransferase
Comments: The enzyme is involved in production of the rare amino acid 3-methylarginine, which is used by the epiphytic bacterium Pseudomonas syringae pv. syringae as an antibiotic against the related pathogenic species Pseudomonas syringae pv. glycinea.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Braun, S.D., Hofmann, J., Wensing, A., Ullrich, M.S., Weingart, H., Völksch, B. and Spiteller, D. Identification of the biosynthetic gene cluster for 3-methylarginine, a toxin produced by Pseudomonas syringae pv. syringae 22d/93. Appl. Environ. Microbiol. 76 (2010) 2500–2508. [PMID: 20190091]
[EC 2.1.1.243 created 2012]
 
 
EC 2.1.1.244
Accepted name: protein N-terminal methyltransferase
Reaction: (1) 3 S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = 3 S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein] (overall reaction)
(1a) S-adenosyl-L-methionine + N-terminal-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-(A,S)PK-[protein]
(1b) S-adenosyl-L-methionine + N-terminal-N-methyl-N-(A,S)PK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-(A,S)PK-[protein]
(1c) S-adenosyl-L-methionine + N-terminal-N,N-dimethyl-N-(A,S)PK-serine-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N,N-trimethyl-N-(A,S)PK-[protein]
(2) 2 S-adenosyl-L-methionine + N-terminal-PPK-[protein] = 2 S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein] (overall reaction)
(2a) S-adenosyl-L-methionine + N-terminal-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N-methyl-N-PPK-[protein]
(2b) S-adenosyl-L-methionine + N-terminal-N-methyl-N-PPK-[protein] = S-adenosyl-L-homocysteine + N-terminal-N,N-dimethyl-N-PPK-[protein]
Other name(s): NMT1 (gene name); METTL11A (gene name)
Systematic name: S-adenosyl-L-methionine:N-terminal-(A,P,S)PK-[protein] methyltransferase
Comments: This enzyme methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys after the initiator L-methionine is cleaved. When the terminal amino acid is L-proline, the enzyme catalyses two successive methylations of its α-amino group. When the first amino acid is either L-alanine or L-serine, the enzyme catalyses three successive methylations. The Pro-Lys in positions 2-3 cannot be exchanged for other amino acids [1,2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Webb, K.J., Lipson, R.S., Al-Hadid, Q., Whitelegge, J.P. and Clarke, S.G. Identification of protein N-terminal methyltransferases in yeast and humans. Biochemistry 49 (2010) 5225–5235. [PMID: 20481588]
2.  Tooley, C.E., Petkowski, J.J., Muratore-Schroeder, T.L., Balsbaugh, J.L., Shabanowitz, J., Sabat, M., Minor, W., Hunt, D.F. and Macara, I.G. NRMT is an α-N-methyltransferase that methylates RCC1 and retinoblastoma protein. Nature 466 (2010) 1125–1128. [PMID: 20668449]
[EC 2.1.1.244 created 2012]
 
 
EC 2.1.1.245
Accepted name: 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase
Reaction: a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin
Other name(s): cdhD (gene name); cdhE (gene name)
Systematic name: 5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein methyltransferase
Comments: Catalyses the transfer of a methyl group from the cobamide cofactor of a corrinoid/Fe-S protein to the N5 group of tetrahydrosarcinapterin. Forms, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, the acetyl-CoA decarbonylase/synthase complex that catalyses the demethylation of acetyl-CoA in a reaction that also forms CO2. This reaction is a key step in methanogenesis from acetate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Maupin-Furlow, J. and Ferry, J.G. Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila. J. Bacteriol. 178 (1996) 340–346. [PMID: 8550451]
2.  Grahame, D.A. and DeMoll, E. Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri. J. Biol. Chem. 271 (1996) 8352–8358. [PMID: 8626532]
[EC 2.1.1.245 created 2012]
 
 
EC 2.1.1.246
Accepted name: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
Reaction: a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
Glossary: coenzyme M (CoM) = 2-mercaptoethanesulfonate
Other name(s): methyltransferase 2 (ambiguous); mtaA (gene name)
Systematic name: methylated methanol-specific corrinoid protein:coenzyme M methyltransferase
Comments: The enzyme, which is involved in methanogenesis from methanol, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. Free methylcob(I)alamin can substitute for the corrinoid protein in vitro [5].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725–18731. [PMID: 8702528]
2.  Harms, U. and Thauer, R.K. Methylcobalamin: coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri. Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli. Eur. J. Biochem. 235 (1996) 653–659. [PMID: 8654414]
3.  Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Zinc dependence and thermodynamics of the methanol:cob(I)alamin methyltransferase reaction. Eur. J. Biochem. 249 (1997) 280–285. [PMID: 9363780]
4.  Sauer, K., Harms, U. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri. Purification, properties and encoding genes of the corrinoid protein MT1. Eur. J. Biochem. 243 (1997) 670–677. [PMID: 9057830]
5.  Sauer, K. and Thauer, R.K. Methanol:coenzyme M methyltransferase from Methanosarcina barkeri – substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin. Eur. J. Biochem. 261 (1999) 674–681. [PMID: 10215883]
[EC 2.1.1.246 created 2012]
 
 
EC 2.1.1.247
Accepted name: [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
Reaction: a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
Glossary: coenzyme M (CoM) = 2-mercaptoethanesulfonate
Other name(s): methyltransferase 2 (ambiguous); MT2 (ambiguous); MT2-A; mtbA (gene name)
Systematic name: methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase
Comments: Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine—corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine—corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine—corrinoid protein Co-methyltransferase) to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Burke, S.A. and Krzycki, J.A. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177 (1995) 4410–4416. [PMID: 7635826]
2.  LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725–18731. [PMID: 8702528]
3.  Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [PMID: 9006042]
4.  Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198]
5.  Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [PMID: 10852929]
[EC 2.1.1.247 created 2012]
 
 
EC 2.1.1.248
Accepted name: methylamine—corrinoid protein Co-methyltransferase
Reaction: methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + NH3
Other name(s): mtmB (gene name); monomethylamine methyltransferase
Systematic name: monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from methylamine to a methylamine-specific corrinoid protein (MtmC), is involved in methanogenesis from methylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Burke, S.A. and Krzycki, J.A. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 272 (1997) 16570–16577. [PMID: 9195968]
2.  Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198]
3.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [PMID: 15450490]
[EC 2.1.1.248 created 2012]
 
 
EC 2.1.1.249
Accepted name: dimethylamine—corrinoid protein Co-methyltransferase
Reaction: dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
Other name(s): mtbB (gene name); dimethylamine methyltransferase
Systematic name: dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wassenaar, R.W., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and characterization of dimethylamine:5-hydroxybenzimidazolyl-cobamide methyltransferase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 253 (1998) 692–697. [PMID: 9654067]
2.  Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [PMID: 10852929]
3.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [PMID: 15450490]
[EC 2.1.1.249 created 2012]
 
 
EC 2.1.1.250
Accepted name: trimethylamine—corrinoid protein Co-methyltransferase
Reaction: trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Other name(s): mttB (gene name); trimethylamine methyltransferase
Systematic name: trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [PMID: 9006042]
2.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [PMID: 15450490]
[EC 2.1.1.250 created 2012]
 
 
EC 2.1.1.251
Accepted name: methylated-thiol—coenzyme M methyltransferase
Reaction: methanethiol + coenzyme M = methyl-CoM + hydrogen sulfide (overall reaction)
(1a) methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
(1b) a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
Glossary: coenzyme M = CoM = 2-mercaptoethanesulfonate
Other name(s): mtsA (gene name)
Systematic name: methylated-thiol:coenzyme M methyltransferase
Comments: The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-S-methylmercaptopropionate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase, and EC 2.1.1.246, methylated methanol-specific corrinoid protein:coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Paul, L. and Krzycki, J.A. Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase. J. Bacteriol. 178 (1996) 6599–6607. [PMID: 8932317]
2.  Tallant, T.C. and Krzycki, J.A. Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. J. Bacteriol. 179 (1997) 6902–6911. [PMID: 9371433]
3.  Tallant, T.C., Paul, L. and Krzycki, J.A. The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. J. Biol. Chem. 276 (2001) 4485–4493. [PMID: 11073950]
[EC 2.1.1.251 created 2012]
 
 
EC 2.1.1.252
Accepted name: tetramethylammonium—corrinoid protein Co-methyltransferase
Reaction: tetramethylammonium + a [Co(I) tetramethylammonium-specific corrinoid protein] = a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine
Other name(s): mtqB (gene name); tetramethylammonium methyltransferase
Systematic name: tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435]
[EC 2.1.1.252 created 2012]
 
 
EC 2.1.1.253
Accepted name: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase
Reaction: a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) tetramethylammonium-specific corrinoid protein]
Glossary: coenzyme M = CoM = 2-mercaptoethanesulfonate
Other name(s): methyltransferase 2 (ambiguous); mtqA (gene name)
Systematic name: methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase
Comments: The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435]
[EC 2.1.1.253 created 2012]
 
 
EC 2.1.1.254
Accepted name: erythromycin 3′′-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + erythromycin C = S-adenosyl-L-homocysteine + erythromycin A
(2) S-adenosyl-L-methionine + erythromycin D = S-adenosyl-L-homocysteine + erythromycin B
For diagram of erythromycin biosynthesis, click here
Other name(s): EryG
Systematic name: S-adenosyl-L-methionine:erythromycin C 3′′-O-methyltransferase
Comments: The enzyme methylates the 3 position of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. It can also methylate the precursor erythromycin D, forming erythromycin B, which is then converted to erythromycin A by EC 1.14.13.154, erythromycin 12 hydroxylase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Paulus, T.J., Tuan, J.S., Luebke, V.E., Maine, G.T., DeWitt, J.P. and Katz, L. Mutation and cloning of eryG, the structural gene for erythromycin O-methyltransferase from Saccharopolyspora erythraea, and expression of eryG in Escherichia coli. J. Bacteriol. 172 (1990) 2541–2546. [PMID: 2185226]
2.  Summers, R.G., Donadio, S., Staver, M.J., Wendt-Pienkowski, E., Hutchinson, C.R. and Katz, L. Sequencing and mutagenesis of genes from the erythromycin biosynthetic gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose and D-desosamine production. Microbiology 143 (1997) 3251–3262. [PMID: 9353926]
[EC 2.1.1.254 created 2012]
 
 
EC 2.1.1.255
Accepted name: geranyl diphosphate 2-C-methyltransferase
Reaction: S-adenosyl-L-methionine + geranyl diphosphate = S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
For diagram of reaction, click here
Other name(s): SCO7701; GPP methyltransferase; GPPMT; 2-methyl-GPP synthase; MGPPS; geranyl pyrophosphate methyltransferase
Systematic name: S-adenosyl-L-methionine:geranyl-diphosphate 2-C-methyltransferase
Comments: This enzyme, along with EC 4.2.3.118, 2-methylisoborneol synthase, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odour.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wang, C.M. and Cane, D.E. Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor. J. Am. Chem. Soc. 130 (2008) 8908–8909. [PMID: 18563898]
2.  Ariyawutthiphan, O., Ose, T., Tsuda, M., Gao, Y., Yao, M., Minami, A., Oikawa, H. and Tanaka, I. Crystallization and preliminary X-ray crystallographic study of a methyltransferase involved in 2-methylisoborneol biosynthesis in Streptomyces lasaliensis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 417–420. [PMID: 21393856]
3.  Komatsu, M., Tsuda, M., Omura, S., Oikawa, H. and Ikeda, H. Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc. Natl. Acad. Sci. USA 105 (2008) 7422–7427. [PMID: 18492804]
4.  Giglio, S., Chou, W.K., Ikeda, H., Cane, D.E. and Monis, P.T. Biosynthesis of 2-methylisoborneol in cyanobacteria. Environ. Sci. Technol. 45 (2011) 992–998. [PMID: 21174459]
[EC 2.1.1.255 created 2012]
 
 
EC 2.4.1.279
Accepted name: nigerose phosphorylase
Reaction: 3-O-α-D-glucopyranosyl-D-glucopyranose + phosphate = D-glucose + β-D-glucose 1-phosphate
Glossary: 3-O-α-D-glucopyranosyl-D-glucopyranose = nigerose
Other name(s): cphy1874 (gene name)
Systematic name: 3-O-α-D-glucopyranosyl-D-glucopyranose:phosphate β-D-glucosyltransferase
Comments: The enzymes from Clostridium phytofermentans is specific for nigerose, and shows only 0.5% relative activity with kojibiose (cf. EC 2.4.1.230, kojibiose phosphorylase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Nihira, T., Nakai, H., Chiku, K. and Kitaoka, M. Discovery of nigerose phosphorylase from Clostridium phytofermentans. Appl. Microbiol. Biotechnol. 93 (2012) 1513–1522. [PMID: 21808968]
[EC 2.4.1.279 created 2012]
 
 
EC 2.4.1.280
Accepted name: N,N′-diacetylchitobiose phosphorylase
Reaction: N,N′-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-α-D-glucosamine 1-phosphate
Glossary: N,N′-diacetylchitobiose = N-acetyl-D-glucosaminyl-β-(1→4)-N-acetyl-D-glucosamine
Other name(s): chbP (gene name)
Systematic name: N,N′-diacetylchitobiose:phosphate N-acetyl-D-glucosaminyltransferase
Comments: The enzyme is specific for N,N′-diacetylchitobiose and does not phosphorylate other N-acetylchitooligosaccharides, cellobiose, trehalose, lactose, maltose or sucrose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Park, J.K., Keyhani, N.O. and Roseman, S. Chitin catabolism in the marine bacterium Vibrio furnissii. Identification, molecular cloning, and characterization of a N,N′-diacetylchitobiose phosphorylase. J. Biol. Chem. 275 (2000) 33077–33083. [PMID: 10913116]
2.  Honda, Y., Kitaoka, M. and Hayashi, K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem. J. 377 (2004) 225–232. [PMID: 13678418]
3.  Hidaka, M., Honda, Y., Kitaoka, M., Nirasawa, S., Hayashi, K., Wakagi, T., Shoun, H. and Fushinobu, S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (α/α)6 barrel fold. Structure 12 (2004) 937–947. [PMID: 15274915]
[EC 2.4.1.280 created 2012]
 
 
EC 2.4.1.281
Accepted name: 4-O-β-D-mannosyl-D-glucose phosphorylase
Reaction: 4-O-β-D-mannopyranosyl-D-glucopyranose + phosphate = D-glucose + α-D-mannose 1-phosphate
Glossary: 4-O-β-D-mannopyranosyl-D-glucopyranose = β-D-mannopyranosyl-(1→4)-D-glucopyranose
Other name(s): mannosylglucose phosphorylase
Systematic name: 4-O-β-D-mannopyranosyl-D-glucopyranose:phosphate α-D-mannosyltransferase
Comments: This enzyme forms part of a mannan catabolic pathway in the anaerobic bacterium Bacteroides fragilis NCTC 9343.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Senoura, T., Ito, S., Taguchi, H., Higa, M., Hamada, S., Matsui, H., Ozawa, T., Jin, S., Watanabe, J., Wasaki, J. and Ito, S. New microbial mannan catabolic pathway that involves a novel mannosylglucose phosphorylase. Biochem. Biophys. Res. Commun. 408 (2011) 701–706. [PMID: 21539815]
[EC 2.4.1.281 created 2012]
 
 
EC 2.4.99.16
Accepted name: starch synthase (maltosyl-transferring)
Reaction: α-maltose 1-phosphate + [(1→4)-α-D-glucosyl]n = phosphate + [(1→4)-α-D-glucosyl]n+2
Other name(s): α1,4-glucan:maltose-1-P maltosyltransferase; GMPMT
Systematic name: α-maltose 1-phosphate:(1→4)-α-D-glucan 4-α-D-maltosyltransferase
Comments: The enzyme from the bacterium Mycobacterium smegmatis is specific for maltose. It has no activity with α-D-glucose.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Elbein, A.D., Pastuszak, I., Tackett, A.J., Wilson, T. and Pan, Y.T. Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen. J. Biol. Chem. 285 (2010) 9803–9812. [PMID: 20118231]
2.  Syson, K., Stevenson, C.E., Rejzek, M., Fairhurst, S.A., Nair, A., Bruton, C.J., Field, R.A., Chater, K.F., Lawson, D.M. and Bornemann, S. Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target. J. Biol. Chem. 286 (2011) 38298–38310. [PMID: 21914799]
[EC 2.4.99.16 created 2012]
 
 
EC 2.7.1.173
Accepted name: nicotinate riboside kinase
Reaction: ATP + β-D-ribosylnicotinate = ADP + nicotinate β-D-ribonucleotide
Other name(s): ribosylnicotinic acid kinase; nicotinic acid riboside kinase; NRK1 (ambiguous)
Systematic name: ATP:β-D-ribosylnicotinate 5-phosphotransferase
Comments: The enzyme from yeast and human also has the activity of EC 2.7.1.22 (ribosylnicotinamide kinase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Tempel, W., Rabeh, W.M., Bogan, K.L., Belenky, P., Wojcik, M., Seidle, H.F., Nedyalkova, L., Yang, T., Sauve, A.A., Park, H.W. and Brenner, C. Nicotinamide riboside kinase structures reveal new pathways to NAD+. PLoS Biol. 5:e263 (2007). [PMID: 17914902]
[EC 2.7.1.173 created 2012]
 
 
EC 2.7.1.174
Accepted name: diacylglycerol kinase (CTP)
Reaction: CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
Glossary: 1,2-diacyl-sn-glycerol 3-phosphate = phosphatidate
Other name(s): DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent)
Systematic name: CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Comments: Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Han, G.S., O'Hara, L., Carman, G.M. and Siniossoglou, S. An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth. J. Biol. Chem. 283 (2008) 20433–20442. [PMID: 18458075]
2.  Han, G.S., O'Hara, L., Siniossoglou, S. and Carman, G.M. Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase. J. Biol. Chem. 283 (2008) 20443–20453. [PMID: 18458076]
3.  Fakas, S., Konstantinou, C. and Carman, G.M. DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae. J. Biol. Chem. 286 (2011) 1464–1474. [PMID: 21071438]
[EC 2.7.1.174 created 2012, modified 2013]
 
 
EC 2.7.1.175
Accepted name: maltokinase
Reaction: ATP + maltose = ADP + α-maltose 1-phosphate
Systematic name: ATP:α-maltose 1-phosphotransferase
Comments: Requires Mg2+ for activity.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Mendes, V., Maranha, A., Lamosa, P., da Costa, M.S. and Empadinhas, N. Biochemical characterization of the maltokinase from Mycobacterium bovis BCG. BMC Biochem. 11:21 (2010). [PMID: 20507595]
[EC 2.7.1.175 created 2012]
 
 
EC 2.7.1.176
Accepted name: UDP-N-acetylglucosamine kinase
Reaction: ATP + UDP-N-acetyl-α-D-glucosamine = ADP + UDP-N-acetyl-α-D-glucosamine 3′-phosphate
Other name(s): UNAG kinase; ζ toxin; toxin PezT; ATP:UDP-N-acetyl-D-glucosamine 3′-phosphotransferase
Systematic name: ATP:UDP-N-acetyl-α-D-glucosamine 3′-phosphotransferase
Comments: Toxic component of a toxin-antitoxin (TA) module. The phosphorylation of UDP-N-acetyl-D-glucosamine results in the inhibition of EC 2.5.1.7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase, the first committed step in cell wall synthesis, which is then blocked. The activity of this enzyme is inhibited when the enzyme binds to the cognate ε antitoxin.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Khoo, S.K., Loll, B., Chan, W.T., Shoeman, R.L., Ngoo, L., Yeo, C.C. and Meinhart, A. Molecular and structural characterization of the PezAT chromosomal toxin-antitoxin system of the human pathogen Streptococcus pneumoniae. J. Biol. Chem. 282 (2007) 19606–19618. [PMID: 17488720]
2.  Mutschler, H., Gebhardt, M., Shoeman, R.L. and Meinhart, A. A novel mechanism of programmed cell death in bacteria by toxin-antitoxin systems corrupts peptidoglycan synthesis. PLoS Biol 9:e1001033 (2011). [PMID: 21445328]
[EC 2.7.1.176 created 2012]
 
 
EC 3.1.3.87
Accepted name: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase
Reaction: 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate
Other name(s): HK-MTPenyl-1-P phosphatase; MtnX; YkrX
Systematic name: 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate phosphohydrolase
Comments: The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2]. In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 5.3.2.5, 2,3-diketo-5-methylthiopentyl-1-phosphate enolase [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039]
2.  Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [PMID: 14551435]
[EC 3.1.3.87 created 2012]
 
 
EC 3.1.7.11
Accepted name: geranyl diphosphate diphosphatase
Reaction: geranyl diphosphate + H2O = geraniol + diphosphate
For diagram of acyclic monoterpenoid biosynthesis, click here
Other name(s): geraniol synthase; geranyl pyrophosphate pyrophosphatase; GES; CtGES
Systematic name: geranyl-diphosphate diphosphohydrolase
Comments: Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree). Requires Mg2+ or Mn2+. Geraniol is labelled when formed in the presence of [18O]H2O. Thus mechanism involves a geranyl cation [1]. Neryl diphosphate is hydrolysed more slowly. May be the same as EC 3.1.7.3 monoterpenyl-diphosphatase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Iijima, Y., Gang, D.R., Fridman, E., Lewinsohn, E. and Pichersky, E. Characterization of geraniol synthase from the peltate glands of sweet basil. Plant Physiol. 134 (2004) 370–379. [PMID: 14657409]
2.  Yang, T., Li, J., Wang, H.X. and Zeng, Y. A geraniol-synthase gene from Cinnamomum tenuipilum. Phytochemistry 66 (2005) 285–293. [PMID: 15680985]
[EC 3.1.7.11 created 2012]
 
 
*EC 3.2.1.28
Accepted name: α,α-trehalase
Reaction: α,α-trehalose + H2O = β-D-glucose + α-D-glucose
Other name(s): trehalase
Systematic name: α,α-trehalose glucohydrolase
Comments: The enzyme is an anomer-inverting glucosidase that catalyses the hydrolysis of the α-glucosidic O-linkage of α,α-trehalose, releasing initially equimolar amounts of α- and β-D-glucose. It is widely distributed in microorganisms, plants, invertebrates and vertebrates.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9025-52-9
References:
1.  Myrbäck, K. and Örtenblad, B. Trehalose und Hefe. II. Trehalasewirkung von Hefepräparaten. Biochem. Z. 291 (1937) 61–69.
2.  Kalf, G.F. and Rieder, S.V. The preparation and properties of trehalase. J. Biol. Chem. 230 (1958) 691–698. [PMID: 13525386]
3.  Hehre, E.J., Sawai, T., Brewer, C.F., Nakano, M. and Kanda, T. Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-D-glucosyl fluoride. Biochemistry 21 (1982) 3090–3097. [PMID: 7104311]
4.  Mori, H., Lee, J.H., Okuyama, M., Nishimoto, M., Ohguchi, M., Kim, D., Kimura, A. and Chiba, S. Catalytic reaction mechanism based on α-secondary deuterium isotope effects in hydrolysis of trehalose by European honeybee trehalase. Biosci. Biotechnol. Biochem. 73 (2009) 2466–2473. [PMID: 19897915]
[EC 3.2.1.28 created 1961, modified 2012]
 
 
EC 3.5.1.110
Accepted name: peroxyureidoacrylate/ureidoacrylate amidohydrolase
Reaction: (1) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + CO2 + NH3 (overall reaction)
(1a) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + carbamate
(1b) carbamate = CO2 + NH3 (spontaneous)
(2) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + CO2 + NH3 (overall reaction)
(2a) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + carbamate
(2b) carbamate = CO2 + NH3 (spontaneous)
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
Other name(s): RutB
Systematic name: (Z)-3-ureidoacrylate peracid amidohydrolase
Comments: The enzyme also shows activity towards ureidoacrylate. Part of the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089–4102. [PMID: 20400551]
[EC 3.5.1.110 created 2012]
 
 
EC 4.1.1.94
Accepted name: ethylmalonyl-CoA decarboxylase
Reaction: (S)-ethylmalonyl-CoA = butanoyl-CoA + CO2
Systematic name: (S)-ethylmalonyl-CoA carboxy-lyase (butanoyl-CoA-forming)
Comments: The enzyme, which exists in all vertebrates, decarboxylates ethylmalonyl-CoA, a potentially toxic compound that is formed in low amounts by the activity of EC 6.4.1.2 (acetyl-CoA carboxylase) and EC 6.4.1.3 (propanoyl-CoA carboxylase). It prefers the S isomer, and can decarboxylate (R)-methylmalonyl-CoA with lower efficiency. cf. EC 4.1.1.41 (methylmalonyl-CoA decarboxylase).
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Linster, C.L., Noel, G., Stroobant, V., Vertommen, D., Vincent, M.F., Bommer, G.T., Veiga-da-Cunha, M. and Van Schaftingen, E. Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite proofreading. J. Biol. Chem. 286 (2011) 42992–43003. [PMID: 22016388]
[EC 4.1.1.94 created 2012]
 
 
EC 4.1.2.50
Accepted name: 6-carboxytetrahydropterin synthase
Reaction: 7,8-dihydroneopterin 3′-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
For diagram of queuine biosynthesis, click here
Glossary: 7,8-dihydroneopterin 3′-triphosphate = 2-amino-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-4-oxo-2,3,7,8-tetrahydropteridine
6-carboxy-5,6,7,8-tetrahydropterin = 2-amino-4-oxo-2,3,5,6,7,8-hexahydropteridine-6-carboxylate
Other name(s): CPH4 synthase; queD (gene name); ToyB; ykvK (gene name)
Systematic name: 7,8-dihydroneopterin 3′-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming)
Comments: Binds Zn2+. Isolated from the bacteria Bacillus subtilis and Escherichia coli. The reaction is part of the biosynthesis pathway of queuosine.The enzyme from Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Cicmil, N. and Shi, L. Crystallization and preliminary X-ray characterization of queD from Bacillus subtilis, an enzyme involved in queuosine biosynthesis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 119–122. [PMID: 18259064]
2.  McCarty, R.M., Somogyi, A. and Bandarian, V. Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase. Biochemistry 48 (2009) 2301–2303. [PMID: 19231875]
[EC 4.1.2.50 created 2012]
 
 
EC 4.2.1.132
Accepted name: 2-hydroxyhexa-2,4-dienoate hydratase
Reaction: 4-hydroxy-2-oxohexanoate = (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + H2O
Other name(s): tesE (gene name); hsaE (gene name)
Systematic name: 4-hydroxy-2-oxohexanoate hydro-lyase [(2Z,4Z)-2-hydroxyhexa-2,4-dienoate-forming]
Comments: This enzyme catalyses a late step in the bacterial steroid degradation pathway. The product, 4-hydroxy-2-oxohexanoate, forms a 2-hydroxy-4-hex-2-enolactone under acidic conditions.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, UM-BBD
References:
1.  Horinouchi, M., Hayashi, T., Koshino, H., Kurita, T. and Kudo, T. Identification of 9,17-dioxo-1,2,3,4,10,19-hexanorandrostan-5-oic acid, 4-hydroxy-2-oxohexanoic acid, and 2-hydroxyhexa-2,4-dienoic acid and related enzymes involved in testosterone degradation in Comamonas testosteroni TA441. Appl. Environ. Microbiol. 71 (2005) 5275–5281. [PMID: 16151114]
[EC 4.2.1.132 created 2012]
 
 
EC 4.2.3.14
Deleted entry: pinene synthase. Now covered by EC 4.2.3.119, (-)-α-pinene synthase, and EC 4.2.3.120, (-)-β-pinene synthase
[EC 4.2.3.14 created 2000 as EC 4.1.99.8, transferred 2000 to EC 4.2.3.14, deleted 2012]
 
 
EC 4.2.3.105
Accepted name: tricyclene synthase
Reaction: geranyl diphosphate = tricyclene + diphosphate
For diagram of bornane and related monoterpenoids, click here
Other name(s): TPS3
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing; tricyclene-forming)
Comments: The enzyme from Solanum lycopersicum (tomato) gives a mixture of tricyclene, camphene, β-myrcene, limonene, and traces of several other monoterpenoids. See EC 4.2.3.117. (-)-camphene synthase, EC 4.2.3.15, myrcene synthase and EC 4.2.3.16, (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Falara, V., Akhtar, T.A., Nguyen, T.T., Spyropoulou, E.A., Bleeker, P.M., Schauvinhold, I., Matsuba, Y., Bonini, M.E., Schilmiller, A.L., Last, R.L., Schuurink, R.C. and Pichersky, E. The tomato terpene synthase gene family. Plant Physiol. 157 (2011) 770–789. [PMID: 21813655]
[EC 4.2.3.105 created 2012]
 
 
EC 4.2.3.106
Accepted name: (E)-β-ocimene synthase
Reaction: geranyl diphosphate = (E)-β-ocimene + diphosphate
Glossary: (E)-β-ocimene = (3E)-3,7-dimethylocta-1,3,6-triene
Other name(s): β-ocimene synthase; AtTPS03; ama0a23; LjEβOS; MtEBOS
Systematic name: geranyl-diphosphate diphosphate-lyase [(E)-β-ocimene-forming]
Comments: Widely distributed in plants, which release β-ocimene when attacked by herbivorous insects.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Faldt, J., Arimura, G., Gershenzon, J., Takabayashi, J. and Bohlmann, J. Functional identification of AtTPS03 as (E)-β-ocimene synthase: a monoterpene synthase catalyzing jasmonate- and wound-induced volatile formation in Arabidopsis thaliana. Planta 216 (2003) 745–751. [PMID: 12624761]
2.  Dudareva, N., Martin, D., Kish, C.M., Kolosova, N., Gorenstein, N., Faldt, J., Miller, B. and Bohlmann, J. (E)-β-ocimene and myrcene synthase genes of floral scent biosynthesis in snapdragon: function and expression of three terpene synthase genes of a new terpene synthase subfamily. Plant Cell 15 (2003) 1227–1241. [PMID: 12724546]
3.  Arimura, G., Ozawa, R., Kugimiya, S., Takabayashi, J. and Bohlmann, J. Herbivore-induced defense response in a model legume. Two-spotted spider mites induce emission of (E)-β-ocimene and transcript accumulation of (E)-β-ocimene synthase in Lotus japonicus. Plant Physiol. 135 (2004) 1976–1983. [PMID: 15310830]
4.  Navia-Gine, W.G., Yuan, J.S., Mauromoustakos, A., Murphy, J.B., Chen, F. and Korth, K.L. Medicago truncatula (E)-β-ocimene synthase is induced by insect herbivory with corresponding increases in emission of volatile ocimene. Plant Physiol. Biochem. 47 (2009) 416–425. [PMID: 19249223]
[EC 4.2.3.106 created 2012]
 
 
EC 4.2.3.107
Accepted name: (+)-car-3-ene synthase
Reaction: geranyl diphosphate = (+)-car-3-ene + diphosphate
For diagram of monoterpenoid biosynthesis, click here
Glossary: (+)-car-3-ene = (1S,6R)-3,7,7-trimethylbicyclo[4.1.0]hept-3-ene
Other name(s): 3-carene cyclase; 3-carene synthase; 3CAR; (+)-3-carene synthase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-car-3-ene-forming]
Comments: The enzyme reacts with (3S)-linalyl diphosphate twice as rapidly as geranyl diphosphate, but 25 times as rapidly as (3R)-linalyl diphosphate. It is assumed that (3S)-linalyl diphosphate is normally formed as an enzyme bound intermediate in the reaction. In the reaction the 5-pro-R hydrogen of geranyl diphosphate is eliminated during cyclopropane ring formation [1,2]. In Picea abies (Norway spruce) and Picea sitchensis (Sitka spruce) terpinolene is also formed [4,6]. See EC 4.2.3.113 terpinolene synthase. (+)-Car-3-ene is associated with resistance of Picea sitchensis (Sitka spruce) to white pine weevil [6].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Savage, T.J. and Croteau, R. Biosynthesis of monoterpenes: regio- and stereochemistry of (+)-3-carene biosynthesis. Arch. Biochem. Biophys. 305 (1993) 581–587. [PMID: 8373196]
2.  Savage, T.J., Ichii, H., Hume, S.D., Little, D.B. and Croteau, R. Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents. Arch. Biochem. Biophys. 320 (1995) 257–265. [PMID: 7625832]
3.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
4.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
5.  Hamberger, B., Hall, D., Yuen, M., Oddy, C., Hamberger, B., Keeling, C.I., Ritland, C., Ritland, K. and Bohlmann, J. Targeted isolation, sequence assembly and characterization of two white spruce (Picea glauca) BAC clones for terpenoid synthase and cytochrome P450 genes involved in conifer defence reveal insights into a conifer genome. BMC Plant Biol. 9:106 (2009). [PMID: 19656416]
6.  Hall, D.E., Robert, J.A., Keeling, C.I., Domanski, D., Quesada, A.L., Jancsik, S., Kuzyk, M.A., Hamberger, B., Borchers, C.H. and Bohlmann, J. An integrated genomic, proteomic and biochemical analysis of (+)-3-carene biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are resistant or susceptible to white pine weevil. Plant J. 65 (2011) 936–948. [PMID: 21323772]
[EC 4.2.3.107 created 2012]
 
 
EC 4.2.3.108
Accepted name: 1,8-cineole synthase
Reaction: geranyl diphosphate + H2O = 1,8-cineole + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: 1,8-cineole = 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane
Other name(s): 1,8-cineole cyclase; geranyl pyrophoshate:1,8-cineole cyclase; 1,8-cineole synthetase
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, 1,8-cineole-forming)
Comments: Requires Mn2+ or Zn2+. Mg2+ is less effective than either. 1,8-Cineole is the main product from the enzyme with just traces of other monoterpenoids. The oxygen atom is derived from water. The reaction proceeds via linalyl diphosphate and α-terpineol, the stereochemistry of both depends on the organism. However neither intermediate can substitute for geranyl diphosphate. The reaction in Salvia officinalis (sage) proceeds via (–)-(3R)-linalyl diphosphate [1-3] while that in Arabidopsis (rock cress) proceeds via (+)-(3S)-linalyl diphosphate [4].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 110637-19-9
References:
1.  Croteau, R., Alonso, W.R., Koepp, A.E. and Johnson, M.A. Biosynthesis of monoterpenes: partial purification, characterization, and mechanism of action of 1,8-cineole synthase. Arch. Biochem. Biophys. 309 (1994) 184–192. [PMID: 8117108]
2.  Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [PMID: 9614092]
3.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [PMID: 12941302]
4.  Chen, F., Ro, D.K., Petri, J., Gershenzon, J., Bohlmann, J., Pichersky, E. and Tholl, D. Characterization of a root-specific Arabidopsis terpene synthase responsible for the formation of the volatile monoterpene 1,8-cineole. Plant Physiol. 135 (2004) 1956–1966. [PMID: 15299125]
5.  Keszei, A., Brubaker, C.L., Carter, R., Kollner, T., Degenhardt, J. and Foley, W.J. Functional and evolutionary relationships between terpene synthases from Australian Myrtaceae. Phytochemistry 71 (2010) 844–852. [PMID: 20399476]
[EC 4.2.3.108 created 2012]
 
 
EC 4.2.3.109
Accepted name: (-)-sabinene synthase
Reaction: geranyl diphosphate = (-)-sabinene + diphosphate
For diagram of thujane monoterpenoid biosynthesis, click here
Glossary: (-)-sabinene = (1S,5S)-1-isopropyl-4-methylenebicyclo[3.1.0]hexane
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-sabinene-forming]
Comments: Requires Mg2+. Isolated from Pinus contorta (lodgepole pine) as cyclase I [1] and from Conocephalum conicum (liverwort) [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Savage, T.J., Hatch, M.W. and Croteau, R. Monoterpene synthases of Pinus contorta and related conifers. A new class of terpenoid cyclase. J. Biol. Chem. 269 (1994) 4012–4020. [PMID: 8307957]
2.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [PMID: 12941302]
[EC 4.2.3.109 created 2012]
 
 
EC 4.2.3.110
Accepted name: (+)-sabinene synthase
Reaction: geranyl diphosphate = (+)-sabinene + diphosphate
For diagram of thujane monoterpenoid biosynthesis, click here
Glossary: (+)-sabinene = (+)-thuj-4(10)-ene = (1R,5R)-1-isopropyl-4-methylenebicyclo[3.1.0]hexane
Other name(s): SS
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-sabinene-forming]
Comments: Isolated from Salvia officinalis (sage). The recombinant enzyme gave 63% (+)-sabinene, 21% γ-terpinene, and traces of other monoterpenoids. See EC 4.2.3.114 γ-terpinene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [PMID: 9614092]
2.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [PMID: 12941302]
[EC 4.2.3.110 created 2012]
 
 
EC 4.2.3.111
Accepted name: (-)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (-)-α-terpineol + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-α-terpineol-forming]
Comments: The enzyme has been characterized from Vitis vinifera (grape). Also forms some 1,8-cineole and traces of other monoterpenoids.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Martin, D.M. and Bohlmann, J. Identification of Vitis vinifera (-)-α-terpineol synthase by in silico screening of full-length cDNA ESTs and functional characterization of recombinant terpene synthase. Phytochemistry 65 (2004) 1223–1229. [PMID: 15184006]
2.  Lucker, J., Bowen, P. and Bohlmann, J. Vitis vinifera terpenoid cyclases: functional identification of two sesquiterpene synthase cDNAs encoding (+)-valencene synthase and (-)-germacrene D synthase and expression of mono- and sesquiterpene synthases in grapevine flowers and berries. Phytochemistry 65 (2004) 2649–2659. [PMID: 15464152]
[EC 4.2.3.111 created 2012]
 
 
EC 4.2.3.112
Accepted name: (+)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (+)-α-terpineol + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-terpineol-forming]
Comments: The enzyme has been characterized from Santalum album (sandalwood). Also forms some (-)-limonene and traces of other monoterpenoids. See EC 4.2.3.16 (4S)-limonene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Jones, C.G., Keeling, C.I., Ghisalberti, E.L., Barbour, E.L., Plummer, J.A. and Bohlmann, J. Isolation of cDNAs and functional characterisation of two multi-product terpene synthase enzymes from sandalwood, Santalum album L. Arch. Biochem. Biophys. 477 (2008) 121–130. [PMID: 18541135]
[EC 4.2.3.112 created 2012]
 
 
EC 4.2.3.113
Accepted name: terpinolene synthase
Reaction: geranyl diphosphate = terpinolene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: terpinolene = 1-methyl-4-(propan-2-ylidene)cyclohexene
Other name(s): ag9; PmeTPS2; LaLIMS_RR
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, terpinolene-forming)
Comments: Requires Mg2+. Mn2+ is less effective and product ratio changes. Forms traces of other monoterpenoids.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
2.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [PMID: 10441373]
3.  Faldt, J., Martin, D., Miller, B., Rawat, S. and Bohlmann, J. Traumatic resin defense in Norway spruce (Picea abies): methyl jasmonate-induced terpene synthase gene expression, and cDNA cloning and functional characterization of (+)-3-carene synthase. Plant Mol. Biol. 51 (2003) 119–133. [PMID: 12602896]
4.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [PMID: 15921711]
5.  Landmann, C., Fink, B., Festner, M., Dregus, M., Engel, K.H. and Schwab, W. Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia). Arch. Biochem. Biophys. 465 (2007) 417–429. [PMID: 17662687]
[EC 4.2.3.113 created 2012]
 
 
EC 4.2.3.114
Accepted name: γ-terpinene synthase
Reaction: geranyl diphosphate = γ-terpinene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: γ-terpinene = 1-isopropyl-4-methylcyclohexa-1,4-diene
Other name(s): OvTPS2; ClcTS
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, γ-terpinene-forming)
Comments: Isolated from Thymus vulgaris (thyme) [1,2], Citrus limon (lemon) [3], Citrus unshiu (satsuma) [4] and Origanum vulgare (oregano) [5]. Requires Mg2+. Mn2+ less effective. The reaction involves a 1,2-hydride shift. The 5-pro-S hydrogen of geranyl diphosphate is lost. Traces of several other monoterpenoids are formed in addition to γ-terpinene.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Alonso, W.R. and Croteau, R. Purification and characterization of the monoterpene cyclase γ-terpinene synthase from Thymus vulgaris. Arch. Biochem. Biophys. 286 (1991) 511–517. [PMID: 1897973]
2.  LaFever, R.E. and Croteau, R. Hydride shifts in the biosynthesis of the p-menthane monoterpenes α-terpinene, γ-terpinene, and β-phellandrene. Arch. Biochem. Biophys. 301 (1993) 361–366. [PMID: 8460944]
3.  Lücker, J., El Tamer, M.K., Schwab, W., Verstappen, F.W., van der Plas, L.H., Bouwmeester, H.J. and Verhoeven, H.A. Monoterpene biosynthesis in lemon (Citrus limon). cDNA isolation and functional analysis of four monoterpene synthases. Eur. J. Biochem. 269 (2000) 3160–3171. [PMID: 12084056]
4.  Suzuki, Y., Sakai, H., Shimada, T., Omura, M., Kumazawa, S. and Nakayama, T. Characterization of γ-terpinene synthase from Citrus unshiu (Satsuma mandarin). Biofactors 21 (2004) 79–82. [PMID: 15630174]
5.  Crocoll, C., Asbach, J., Novak, J., Gershenzon, J. and Degenhardt, J. Terpene synthases of oregano (Origanum vulgare L.) and their roles in the pathway and regulation of terpene biosynthesis. Plant Mol. Biol. 73 (2010) 587–603. [PMID: 20419468]
[EC 4.2.3.114 created 2012]
 
 
EC 4.2.3.115
Accepted name: α-terpinene synthase
Reaction: geranyl diphosphate = α-terpinene + diphosphate
For diagram of menthane monoterpenoid biosynthesis, click here
Glossary: α-terpinene = 1-isopropyl-4-methylcyclohexa-1,3-diene
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, α-terpinene-forming)
Comments: The enzyme has been characterized from Dysphania ambrosioides (American wormseed). Requires Mg2+. Mn2+ is less effective. The enzyme will also use (3R)-linalyl diphosphate. The reaction involves a 1,2-hydride shift. The 1-pro-S hydrogen of geranyl diphosphate is lost.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Poulose, A.J. and Croteau, R. γ-Terpinene synthetase: a key enzyme in the biosynthesis of aromatic monoterpenes. Arch. Biochem. Biophys. 191 (1978) 400–411. [PMID: 736574]
2.  LaFever, R.E. and Croteau, R. Hydride shifts in the biosynthesis of the p-menthane monoterpenes α-terpinene, γ-terpinene, and β-phellandrene. Arch. Biochem. Biophys. 301 (1993) 361–366. [PMID: 8460944]
[EC 4.2.3.115 created 2012]
 
 
EC 4.2.3.116
Accepted name: (+)-camphene synthase
Reaction: geranyl diphosphate = (+)-camphene + diphosphate
Glossary: (+)-camphene = (1R,4S)-2,2-dimethyl-3-methylenebicyclo[2.2.1]heptane
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-camphene-forming]
Comments: Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-camphene and (+)-α-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. Requires Mg2+ (preferred to Mn2+). See also EC 4.2.3.121 (+)-α-pinene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gambliel, H. and Croteau, R. Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. J. Biol. Chem. 259 (1984) 740–748. [PMID: 6693393]
2.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006]
3.  Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477–487. [PMID: 8109978]
4.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [PMID: 8109979]
[EC 4.2.3.116 created 2012]
 
 
EC 4.2.3.117
Accepted name: (-)-camphene synthase
Reaction: geranyl diphosphate = (-)-camphene + diphosphate
Glossary: (-)-camphene = (1S,4R)-2,2-dimethyl-3-methylenebicyclo[2.2.1]heptane
Other name(s): CS
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-camphene-forming]
Comments: (-)-Camphene is the major product in Abies grandis (grand fir) with traces of other monoterpenoids [1]. In Pseudotsuga menziesii (Douglas-fir) there are about equal parts of (-)-camphene and (-)-α-pinene with traces of four other monoterpenoids [2,3]. In Solanum lycopersicum (tomato) tricyclene, β-myrcene, limonene, and traces of several other monoterpenoids are also formed [4]. See also EC 4.2.3.15 myrcene synthase, EC 4.2.3.16 (4S)-limonene synthase, EC 4.2.3.119 (-)-α-pinene synthase and EC 4.2.3.105 tricyclene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [PMID: 10441373]
2.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [PMID: 15921711]
3.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [PMID: 15978541]
4.  Falara, V., Akhtar, T.A., Nguyen, T.T., Spyropoulou, E.A., Bleeker, P.M., Schauvinhold, I., Matsuba, Y., Bonini, M.E., Schilmiller, A.L., Last, R.L., Schuurink, R.C. and Pichersky, E. The tomato terpene synthase gene family. Plant Physiol. 157 (2011) 770–789. [PMID: 21813655]
[EC 4.2.3.117 created 2012]
 
 
EC 4.2.3.118
Accepted name: 2-methylisoborneol synthase
Reaction: (E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol + diphosphate
For diagram of bornane and related monoterpenoids, click here and for diagram of reaction, click here
Other name(s): sco7700; 2-MIB cyclase; MIB synthase; MIBS
Systematic name: (E)-2-methylgeranyl-diphosphate diphosphate-lyase (cyclizing, 2-methylisoborneol-forming)
Comments: The product, 2-methylisoborneol, is a characteristc odiferous compound with a musty smell produced by soil microorganisms.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wang, C.M. and Cane, D.E. Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor. J. Am. Chem. Soc. 130 (2008) 8908–8909. [PMID: 18563898]
2.  Komatsu, M., Tsuda, M., Omura, S., Oikawa, H. and Ikeda, H. Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc. Natl. Acad. Sci. USA 105 (2008) 7422–7427. [PMID: 18492804]
3.  Giglio, S., Chou, W.K., Ikeda, H., Cane, D.E. and Monis, P.T. Biosynthesis of 2-methylisoborneol in cyanobacteria. Environ. Sci. Technol. 45 (2011) 992–998. [PMID: 21174459]
[EC 4.2.3.118 created 2012]
 
 
EC 4.2.3.119
Accepted name: (-)-α-pinene synthase
Reaction: geranyl diphosphate = (-)-α-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (-)-α-pinene = (1S,5S)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene
Other name(s): (-)-α-pinene/(-)-camphene synthase; (-)-α-pinene cyclase
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-α-pinene-forming]
Comments: Cyclase II of Salvia officinalis (sage) gives about equal parts (-)-α-pinene, (-)-β-pinene and (-)-camphene, plus traces of other monoterpenoids. (3S)-Linalyl diphosphate can also be used by the enzyme in preference to (3R)-linalyl diphosphate. The 4-pro-S-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-6]. The enzyme from Abies grandis (grand fir) gives roughly equal parts (-)-α-pinene and (-)-β-pinene. However the clone ag11 gave 35% (-)-limonene, 24% (-)-α-pinene and 20% (-)-β-phellandrene. It requires Mn2+ and K+ (Mg2+ is ineffective) [7-10]. Synthase I from Pinus taeda (loblolly pine) produces (-)-α-pinene with traces of (-)-β-pinene and requires Mn2+ (preferred to Mg2+) [11,12]. The enzyme from Picea sitchensis (Sika spruce) forms 70% (-)-α-pinene and 30% (-)-β-pinene [13]. The recombinant PmeTPS1 enzyme from Pseudotsuga menziesii (Douglas fir) gave roughly equal proportions of (-)-α-pinene and (-)-camphene plus traces of other monoterpenoids [14]. See also EC 4.2.3.120, (-)-β-pinene synthase; EC 4.2.3.117, (-)-camphene synthase; EC 4.2.3.16, (-)-limonene synthase; and EC 4.2.3.52, (-)-β-phellandrene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gambliel, H. and Croteau, R. Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. J. Biol. Chem. 259 (1984) 740–748. [PMID: 6693393]
2.  Croteau, R.B., Wheeler, C.J., Cane, D.E., Ebert, R. and Ha, H.J. Isotopically sensitive branching in the formation of cyclic monoterpenes: proof that (-)-α-pinene and (-)-β-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate. Biochemistry 26 (1987) 5383–5389. [PMID: 3314988]
3.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006]
4.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
5.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [PMID: 8109979]
6.  Lu, S., Xu, R., Jia, J.W., Pang, J., Matsuda, S.P. and Chen, X.Y. Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression. Plant Physiol. 130 (2002) 477–486. [PMID: 12226526]
7.  Lewinsohn, E., Gijzen, M. and Croteau, R. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. Arch. Biochem. Biophys. 293 (1992) 167–173. [PMID: 1731633]
8.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [PMID: 9268308]
9.  Bohlmann, J., Phillips, M., Ramachandiran, V., Katoh, S. and Croteau, R. cDNA cloning, characterization, and functional expression of four new monoterpene synthase members of the Tpsd gene family from grand fir (Abies grandis). Arch. Biochem. Biophys. 368 (1999) 232–243. [PMID: 10441373]
10.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [PMID: 15978541]
11.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [PMID: 10562434]
12.  Phillips, M.A., Wildung, M.R., Williams, D.C., Hyatt, D.C. and Croteau, R. cDNA isolation, functional expression, and characterization of (+)-α-pinene synthase and (-)-α-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis. Arch. Biochem. Biophys. 411 (2003) 267–276. [PMID: 12623076]
13.  McKay, S.A., Hunter, W.L., Godard, K.A., Wang, S.X., Martin, D.M., Bohlmann, J. and Plant, A.L. Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce. Plant Physiol. 133 (2003) 368–378. [PMID: 12970502]
14.  Huber, D.P.W., Philippe, R.N., Godard, K.-A., Sturrock, R.N. and Bohlmann, J. Characterization of four terpene synthase cDNAs from methyl jasmonate-induced Douglas-fir, Pseudotsuga menziesii. Phytochemistry 66 (2005) 1427–1439. [PMID: 15921711]
[EC 4.2.3.119 created 2012]
 
 
EC 4.2.3.120
Accepted name: (-)-β-pinene synthase
Reaction: geranyl diphosphate = (-)-β-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (-)-β-pinene = (1S,5S)-6,6-dimethyl-2-methylenebicyclo[3.1.1]hept-2-ene
Other name(s): β-geraniolene synthase; (-)-(1S,5S)-pinene synthase; geranyldiphosphate diphosphate lyase (pinene forming)
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (-)-β-pinene-forming]
Comments: Cyclase II of Salvia officinalis (sage) produces about equal parts (-)-α-pinene, (-)-β-pinene and (-)-camphene, plus traces of other monoterpenoids. The enzyme, which requires Mg2+ (preferred to Mn2+), can also use (3S)-Linalyl diphosphate (preferred to (3R)-linalyl diphosphate) [1-4]. The enzyme from Abies grandis (grand fir) produces roughly equal parts of (-)-α-pinene and (-)-β-pinene [6-9]. Cyclase IV from Pinus contorta (lodgepole pine) produces 63% (-)-β-pinene, 26% 3-carene, and traces of α-pinene [10]. Synthase III from Pinus taeda (loblolly pine) forms (-)-β-pinene with traces of α-pinene and requires Mn2+ and K+ (Mg2+ is ineffective) [11]. A cloned enzyme from Artemisia annua (sweet wormwood) gave (-)-β-pinene with traces of (-)-α-pinene [5]. The enzyme from Picea sitchensis (Sika spruce) forms 30% (-)-β-pinene and 70% (-)-α-pinene [12]. See also EC 4.2.3.119, (-)-α-pinene synthase, EC 4.2.3.117, (-)-camphene synthase, and EC 4.2.3.107 (+)-3-carene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Croteau, R.B., Wheeler, C.J., Cane, D.E., Ebert, R. and Ha, H.J. Isotopically sensitive branching in the formation of cyclic monoterpenes: proof that (-)-α-pinene and (-)-β-pinene are synthesized by the same monoterpene cyclase via deprotonation of a common intermediate. Biochemistry 26 (1987) 5383–5389. [PMID: 3314988]
2.  Croteau, R. and Satterwhite, D.M. Biosynthesis of monoterpenes. Stereochemical implications of acyclic and monocyclic olefin formation by (+)- and (-)-pinene cyclases from sage. J. Biol. Chem. 264 (1989) 15309–15315. [PMID: 2768265]
3.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006]
4.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [PMID: 8109979]
5.  Lu, S., Xu, R., Jia, J.W., Pang, J., Matsuda, S.P. and Chen, X.Y. Cloning and functional characterization of a β-pinene synthase from Artemisia annua that shows a circadian pattern of expression. Plant Physiol. 130 (2002) 477–486. [PMID: 12226526]
6.  Gijzen, M., Lewinsohn, E. and Croteau, R. Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis). Arch. Biochem. Biophys. 289 (1991) 267–273. [PMID: 1898071]
7.  Lewinsohn, E., Gijzen, M. and Croteau, R. Wound-inducible pinene cyclase from grand fir: purification, characterization, and renaturation after SDS-PAGE. Arch. Biochem. Biophys. 293 (1992) 167–173. [PMID: 1731633]
8.  Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (-)-(4S)-limonene synthase, and (-)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784–21792. [PMID: 9268308]
9.  Hyatt, D.C. and Croteau, R. Mutational analysis of a monoterpene synthase reaction: altered catalysis through directed mutagenesis of (-)-pinene synthase from Abies grandis. Arch. Biochem. Biophys. 439 (2005) 222–233. [PMID: 15978541]
10.  Savage, T.J., Ichii, H., Hume, S.D., Little, D.B. and Croteau, R. Monoterpene synthases from gymnosperms and angiosperms: stereospecificity and inactivation by cysteinyl- and arginyl-directed modifying reagents. Arch. Biochem. Biophys. 320 (1995) 257–265. [PMID: 7625832]
11.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [PMID: 10562434]
12.  McKay, S.A., Hunter, W.L., Godard, K.A., Wang, S.X., Martin, D.M., Bohlmann, J. and Plant, A.L. Insect attack and wounding induce traumatic resin duct development and gene expression of (-)-pinene synthase in Sitka spruce. Plant Physiol. 133 (2003) 368–378. [PMID: 12970502]
[EC 4.2.3.120 created 2012]
 
 
EC 4.2.3.121
Accepted name: (+)-α-pinene synthase
Reaction: geranyl diphosphate = (+)-α-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (+)-α-pinene = (1R,5R)-2,6,6-trimethylbicyclo[3.1.1]hept-2-ene
Other name(s): (+)-α-pinene cyclase; cyclase I
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (+)-α-pinene-forming]
Comments: Cyclase I of Salvia officinalis (sage) gives about equal parts (+)-α-pinene and (+)-camphene, whereas cyclase III gives about equal parts of (+)-α-pinene and (+)-β-pinene. (3R)-Linalyl diphosphate can also be used by the enzyme in preference to (3S)-linalyl diphosphate. The 4-pro-R-hydrogen of geranyl diphosphate is lost. Requires Mg2+ (preferred to Mn2+) [1-4]. With synthase II of Pinus taeda (loblolly pine) (+)-α-pinene was the only product [5,6]. Requires Mn2+ (preferred to Mg2+). See also EC 4.2.3.122, (+)-β-pinene synthase, and EC 4.2.3.116, (+)-camphene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Gambliel, H. and Croteau, R. Pinene cyclases I and II. Two enzymes from sage (Salvia officinalis) which catalyze stereospecific cyclizations of geranyl pyrophosphate to monoterpene olefins of opposite configuration. J. Biol. Chem. 259 (1984) 740–748. [PMID: 6693393]
2.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-pinene and (+)- and (-)-camphene. J. Biol. Chem. 263 (1988) 10063–10071. [PMID: 3392006]
3.  Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477–487. [PMID: 8109978]
4.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [PMID: 8109979]
5.  Phillips, M.A., Savage, T.J. and Croteau, R. Monoterpene synthases of loblolly pine (Pinus taeda) produce pinene isomers and enantiomers. Arch. Biochem. Biophys. 372 (1999) 197–204. [PMID: 10562434]
6.  Phillips, M.A., Wildung, M.R., Williams, D.C., Hyatt, D.C. and Croteau, R. cDNA isolation, functional expression, and characterization of (+)-α-pinene synthase and (-)-α-pinene synthase from loblolly pine (Pinus taeda): stereocontrol in pinene biosynthesis. Arch. Biochem. Biophys. 411 (2003) 267–276. [PMID: 12623076]
[EC 4.2.3.121 created 2012]
 
 
EC 4.2.3.122
Accepted name: (+)-β-pinene synthase
Reaction: geranyl diphosphate = (+)-β-pinene + diphosphate
For diagram of pinene and related monoterpenoids, click here
Glossary: (+)-β-pinene = (1R,5R)-6,6-dimethyl-2-methylenebicyclo[3.1.1]hept-2-ene
Other name(s): (+)-pinene cyclase; cyclase III
Systematic name: geranyl-diphosphate diphosphate-lyase [(+)-β-pinene-forming]
Comments: Cyclase III from Salvia officinalis (sage) gives roughly equal parts of (+)-β-pinene and (+)-α-pinene. See EC 4.2.3.121, (+)-α-pinene synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477–487. [PMID: 8109978]
2.  Pyun, H.J., Wagschal, K.C., Jung, D.I., Coates, R.M. and Croteau, R. Stereochemistry of the proton elimination in the formation of (+)- and (-)-α-pinene by monoterpene cyclases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 488–496. [PMID: 8109979]
[EC 4.2.3.122 created 2012]
 
 
EC 4.2.3.123
Accepted name: β-sesquiphellandrene synthase
Reaction: (2E,6E)-farnesyl diphosphate = β-sesquiphellandrene + diphosphate
For diagram of bisabolene biosynthesis, click here and for diagram of β-sesquiphellandrene and zingiberene biosynthesis, click here
Other name(s): Tps1; Os08g07100 (gene name)
Systematic name: (2E,6E)-farnesyl-diphosphate diphosphate-lyase (cyclizing, β-sesquiphellandrene-forming)
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zhuang, X., Kollner, T.G., Zhao, N., Li, G., Jiang, Y., Zhu, L., Ma, J., Degenhardt, J. and Chen, F. Dynamic evolution of herbivore-induced sesquiterpene biosynthesis in sorghum and related grass crops. Plant J. 69 (2012) 70–80. [PMID: 21880075]
[EC 4.2.3.123 created 2012]
 
 
EC 5.3.2.5
Accepted name: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase
Reaction: 5-(methylthio)-2,3-dioxopentyl phosphate = 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
Other name(s): DK-MTP-1-P enolase; MtnW; YkrW; RuBisCO-like protein; RLP
Systematic name: 2,3-diketo-5-methylthiopentyl-1-phosphate ketoenol-isomerase
Comments: The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2]. In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase [1].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Myers, R.W., Wray, J.W., Fish, S. and Abeles, R.H. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem. 268 (1993) 24785–24791. [PMID: 8227039]
2.  Ashida, H., Saito, Y., Kojima, C., Kobayashi, K., Ogasawara, N. and Yokota, A. A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302 (2003) 286–290. [PMID: 14551435]
[EC 5.3.2.5 created 2012]
 
 
*EC 5.3.99.10 – private review period expired (13 February 2017) [Last modified: 2012-05-02 19:40:51]
Accepted name: thiazole tautomerase
Reaction: 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate = 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate
For diagram of thiamine diphosphate biosynthesis, click here
Glossary: cThz*-P = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate
cThz-P = 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = 4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazole-2-carboxylate
Other name(s): tenI (gene name)
Systematic name: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate isomerase
Comments: The enzyme catalyses the irreversible aromatization of the thiazole moiety of 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, MetaCyc
References:
1.  Hazra, A.B., Han, Y., Chatterjee, A., Zhang, Y., Lai, R.Y., Ealick, S.E. and Begley, T.P. A missing enzyme in thiamin thiazole biosynthesis: identification of TenI as a thiazole tautomerase. J. Am. Chem. Soc. 133 (2011) 9311–9319. [PMID: 21534620]
[EC 5.3.99.10 created 2012]
 
 
*EC 5.5.1.8
Accepted name: (+)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (+)-bornyl diphosphate
For diagram of bornane and related monoterpenoids, click here
Glossary: (+)-bornyl diphosphate = (1R,2S,4R)-1,7,7-trimethylbicyclo[2.2.1]heptan-2-yl diphosphate
Other name(s): bornyl pyrophosphate synthase (ambiguous); bornyl pyrophosphate synthetase (ambiguous); (+)-bornylpyrophosphate cyclase; geranyl-diphosphate cyclase (ambiguous); (+)-bornyl-diphosphate lyase (decyclizing)
Systematic name: (+)-bornyl-diphosphate lyase (ring-opening)
Comments: Requires Mg2+. The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro [3]. The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (+)-bornyl diphosphate [3]. cf. EC 5.5.1.22 [(–)-bornyl diphosphate synthase].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 72668-91-8
References:
1.  Croteau, R. and Karp, F. Biosynthesis of monoterpenes: preliminary characterization of bornyl pyrophosphate synthetase from sage (Salvia officinalis) and demonstration that geranyl pyrophosphate is the preferred substrate for cyclization. Arch. Biochem. Biophys. 198 (1979) 512–522. [PMID: 42356]
2.  Croteau, R., Gershenzon, J., Wheeler, C.J. and Satterwhite, D.M. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. Arch. Biochem. Biophys. 277 (1990) 374–381. [PMID: 2178556]
3.  Croteau, R., Satterwhite, D.M., Cane, D.E. and Chang, C.C. Biosynthesis of monoterpenes. Enantioselectivity in the enzymatic cyclization of (+)- and (-)-linalyl pyrophosphate to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 261 (1986) 13438–13445. [PMID: 3759972]
4.  Croteau, R., Felton, N.M. and Wheeler, C.J. Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 260 (1985) 5956–5962. [PMID: 3997807]
5.  Croteau, R.B., Shaskus, J.J., Renstrom, B., Felton, N.M., Cane, D.E., Saito, A. and Chang, C. Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates. Biochemistry 24 (1985) 7077–7085. [PMID: 4084562]
6.  McGeady, P. and Croteau, R. Isolation and characterization of an active-site peptide from a monoterpene cyclase labeled with a mechanism-based inhibitor. Arch. Biochem. Biophys. 317 (1995) 149–155. [PMID: 7872777]
7.  Wise, M.L., Savage, T.J., Katahira, E. and Croteau, R. Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase. J. Biol. Chem. 273 (1998) 14891–14899. [PMID: 9614092]
8.  Whittington, D.A., Wise, M.L., Urbansky, M., Coates, R.M., Croteau, R.B. and Christianson, D.W. Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase. Proc. Natl. Acad. Sci. USA 99 (2002) 15375–15380. [PMID: 12432096]
9.  Peters, R.J. and Croteau, R.B. Alternative termination chemistries utilized by monoterpene cyclases: chimeric analysis of bornyl diphosphate, 1,8-cineole, and sabinene synthases. Arch. Biochem. Biophys. 417 (2003) 203–211. [PMID: 12941302]
[EC 5.5.1.8 created 1984, modified 2012]
 
 
EC 5.5.1.22
Accepted name: (–)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (–)-bornyl diphosphate
For diagram of bornane and related monoterpenoids, click here
Glossary: (–)-bornyl diphosphate = (2R,4S)-1,7,7-trimethylbicyclo[2.2.1]hept-2-yl diphosphate
Other name(s): bornyl pyrophosphate synthase (ambiguous); bornyl pyrophosphate synthetase (ambiguous); (–)-bornyl pyrophosphate cyclase; bornyl diphosphate synthase; geranyl-diphosphate cyclase (ambiguous); (–)-bornyl-diphosphate lyase (decyclizing)
Systematic name: (–)-bornyl-diphosphate lyase (ring-opening)
Comments: Requires Mg2+. The enzyme from Tanacetum vulgare (tansy) can also use (3S)-linalyl diphosphate or more slowly neryl diphosphate in vitro. The reaction proceeds via isomeration of geranyl diphosphate to (3S)-linalyl diphosphate [3]. The oxygen and phosphorus originally linked to C-1 of geranyl diphosphate end up linked to C-2 of (–)-bornyl diphosphate [4]. cf. EC 5.5.1.8 (+)-bornyl diphosphate synthase.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, CAS registry number: 110639-17-3
References:
1.  Croteau, R., Gershenzon, J., Wheeler, C.J. and Satterwhite, D.M. Biosynthesis of monoterpenes: stereochemistry of the coupled isomerization and cyclization of geranyl pyrophosphate to camphane and isocamphane monoterpenes. Arch. Biochem. Biophys. 277 (1990) 374–381. [PMID: 2178556]
2.  Croteau, R. and Shaskus, J. Biosynthesis of monoterpenes: demonstration of a geranyl pyrophosphate:(-)-bornyl pyrophosphate cyclase in soluble enzyme preparations from tansy (Tanacetum vulgare). Arch. Biochem. Biophys. 236 (1985) 535–543. [PMID: 3970524]
3.  Croteau, R., Felton, N.M. and Wheeler, C.J. Stereochemistry at C-1 of geranyl pyrophosphate and neryl pyrophosphate in the cyclization to (+)- and (-)-bornyl pyrophosphate. J. Biol. Chem. 260 (1985) 5956–5962. [PMID: 3997807]
4.  Croteau, R.B., Shaskus, J.J., Renstrom, B., Felton, N.M., Cane, D.E., Saito, A. and Chang, C. Mechanism of the pyrophosphate migration in the enzymatic cyclization of geranyl and linalyl pyrophosphates to (+)- and (-)-bornyl pyrophosphates. Biochemistry 24 (1985) 7077–7085. [PMID: 4084562]
5.  Adam, K.P. and Croteau, R. Monoterpene biosynthesis in the liverwort Conocephalum conicum: demonstration of sabinene synthase and bornyl diphosphate synthase. Phytochemistry 49 (1998) 475–480. [PMID: 9747540]
[EC 5.5.1.22 created 2012]
 
 
EC 6.3.4.20
Accepted name: 7-cyano-7-deazaguanine synthase
Reaction: 7-carboxy-7-carbaguanine + NH3 + ATP = 7-cyano-7-carbaguanine + ADP + phosphate + H2O
For diagram of queuine biosynthesis, click here
Glossary: preQ0 = 7-cyano-7-carbaguanine = 7-cyano-7-deazaguanine
7-carboxy-7-carbaguanine = 7-carboxy-7-deazaguanine
Other name(s): preQ0 synthase; 7-cyano-7-carbaguanine synthase; queC (gene name)
Systematic name: 7-carboxy-7-carbaguanine:ammonia ligase (ADP-forming)
Comments: Binds Zn2+. The reaction is part of the biosynthesis pathway of queuosine.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  McCarty, R.M., Somogyi, A., Lin, G., Jacobsen, N.E. and Bandarian, V. The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of preQ0 from guanosine 5′-triphosphate in four steps. Biochemistry 48 (2009) 3847–3852. [PMID: 19354300]
2.  Cicmil, N. and Huang, R.H. Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis. Proteins 72 (2008) 1084–1088. [PMID: 18491386]
[EC 6.3.4.20 created 2012]
 
 


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