An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
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 reaction 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, 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 1.1.1.318
Accepted name: eugenol synthase
Reaction: eugenol + a carboxylate + NADP+ = a coniferyl ester + NADPH + H+
For diagram of reaction click here.
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].
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 1.1.1.319
Accepted name: isoeugenol synthase
Reaction: isoeugenol + acetate + NADP+ = coniferyl acetate + NADPH + H+
For diagram of reaction click here.
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].
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 1.1.1.320
Accepted name: benzil reductase [(S)-benzoin forming]
Reaction: (S)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (S)-benzoin = (2S)-2-hydroxy-1,2-diphenylethanone
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].
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 1.1.1.321
Accepted name: benzil reductase [(R)-benzoin forming]
Reaction: (R)-benzoin + NADP+ = benzil + NADPH + H+
Glossary: (R)-benzoin = (2R)-2-hydroxy-1,2-diphenylethanone
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.
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 1.1.1.322
Accepted name: (–)-endo-fenchol dehydrogenase
Reaction: (–)-endo-fenchol + NAD(P)+ = (+)-fenchone + NAD(P)H + H+
For diagram of reaction 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.
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
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.
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 1.1.1.324
Accepted name: 8-hydroxygeraniol dehydrogenase
Reaction: (6E)-8-hydroxygeraniol + 2 NADP+ = (6E)-8-oxogeranial + 2 NADPH + 2 H+ (overall reaction)
For diagram of reaction 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.
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 1.1.1.325
Accepted name: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
Reaction: (1) L-threo-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH + H+
Glossary: sepiapterin = 2-amino-6-lactoyl-7,8-dihydropteridin-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).
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 1.1.1.326
Accepted name: zerumbone synthase
Reaction: 10-hydroxy-α-humulene + NAD+ = zerumbone + NADH + H+
For diagram of reaction click here.
Other name(s): ZSD1
Systematic name: 10-hydroxy-α-humulene:NAD+ oxidoreductase
Comments: The enzyme was cloned from shampoo ginger, Zingiber zerumbet.
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 1.3.8.3
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 reaction, 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.
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 1.3.8.4
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.
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 1.3.99.10 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 (non-decarboxylating)
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
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.
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 1.14.13.150
Accepted name: α-humulene 10-hydroxylase
Reaction: α-humulene + O2 + NADPH + H+ = 10-hydroxy-α-humulene + NADP+ + H2O
For diagram of reaction click here.
Other name(s): CYP71BA1
Systematic name: α-humulene,NADPH:oxygen 10-oxidoreductase
Comments: Requires cytochrome P450. The recommended numbering of humulene gives 10-hydroxy-α-humulene as the product rather than 8-hydroxy-α-humulene as used by the reference. See Section F: Natural Product Nomenclature.
References:
1. Yu, F., Okamoto, S., Harada, H., Yamasaki, K., Misawa, N. and Utsumi, R. Zingiber zerumbet CYP71BA1 catalyzes the conversion of α-humulene to 8-hydroxy-α-humulene in zerumbone biosynthesis. Cell. Mol. Life Sci. 68 (2011) 1033-1040. [PMID: 20730551]
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)
For diagram of reaction 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.
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 1.14.13.152
Accepted name: geraniol 8-hydroxylase
Reaction: geraniol + NADPH + H+ + O2 = (6E)-8-hydroxygeraniol + NADP+ + H2O
For diagram of reaction click here.
Other name(s): CYP76B6; G10H; CrG10H; SmG10H
Systematic name: geraniol,NADPH:oxygen oxidoreductase (8-hydroxylating)
Comments: Requires cytochrome P450. 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].
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 1.14.13.153
Accepted name: (+)-sabinene 3-hydroxylase
Reaction: (+)-sabinene + NADPH + H+ + O2 = (+)-cis-sabinol + NADP+ + H2O
For diagram of reaction click here.
Systematic name: (+)-sabinene,NADPH:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires cytochrome P450. The enzyme has been characterized from Salvia officinalis (sage).
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 1.14.13.154
Accepted name: erythromycin 12 hydroxylase
Reaction: erythromycin D + NADPH + H+ + O2 = erythromycin C + NADP+ + H2O
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].
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 1.14.99.28 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
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-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.
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 1.17.2.2
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
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 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,
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 2.1.1.243
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
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.
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 2.1.1.244
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)
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].
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 2.1.1.245
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.
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 2.1.1.246
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].
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 2.1.1.247
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.
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 2.1.1.248
Accepted name: methylamine—corrinoid protein Co-methyltransferase
Reaction: methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + ammonia
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.
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 2.1.1.249
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.
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 2.1.1.250
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.
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 2.1.1.251
Accepted name: methylated-thiol—coenzyme M methyltransferase
Reaction: methanethiol + coenzyme M = methyl-CoM + hydrogen sulfide (overall reaction)
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.
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 2.1.1.252
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.
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
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.
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 2.1.1.254
Accepted name: erythromycin 3"-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + erythromycin C = S-adenosyl-L-homocysteine + erythromycin A
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.
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 2.1.1.255
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 and mechanism 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.
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 2.4.1.279
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)
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 2.4.1.280
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.
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 2.4.1.281
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.
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 2.4.99.16
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 from the bacterium Mycobacterium smegmatis is specific for maltose. It has no activity with α-D-glucose.
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]
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).
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 (2007) e263. [PMID: 17914902]
EC 2.7.1.174
Accepted name: diacylglycerol kinase (CTP dependent)
Reaction: CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate
Other name(s): DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous)
Systematic name: CTP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Comments: Requires Ca2+ or Mg2+ for activity. The enzyme from Saccharomyces cerevisiae can use dCTP instead of CTP, but not ATP, GTP or UTP.
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]
EC 2.7.1.175
Accepted name: maltokinase
Reaction: ATP + maltose = ADP + α-maltose-1-phosphate
Systematic name: ATP:maltose 1-phosphotransferase
Comments: Requires Mg2+ for activity.
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 (2010) 21. [PMID: 20507595]
EC 2.7.1.176
Accepted name: UDP-N-acetylglucosamine kinase
Reaction: ATP + UDP-N-acetyl-D-glucosamine = ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate
Other name(s): UNAG kinase; ζ toxin; toxin PezT
Systematic name: ATP:UDP-N-acetyl-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.
References:
1. 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 (2011) e1001033. [PMID: 21445328]
2. 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]
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].
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 3.1.7.11
Accepted name: geranyl diphosphate diphosphatase
Reaction: geranyl diphosphate + H2O = geraniol + diphosphate
For diagram of reaction 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.
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 3.2.1.28
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,
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 3.5.1.110
Accepted name: peroxyureidoacrylate/ureidoacrylate amidohydrolase
Reaction: (1) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + CO2 + NH3 (overall reaction)
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-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.
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 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).
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 4.1.2.50
Accepted name: 6-carboxytetrahydropterin synthase
Reaction: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
Other name(s): CPH4 synthase; queD (gene name)
Systematic name: 7,8-dihydroneopterin 3'-triphosphate acetaldehyde-lyase (6-carboxy-5,6,7,8-tetrahydropterin and triphosphate-forming)
Comments: Binds Zn2+. The reaction is part of the biosynthesis pathway of queuosine. The enzyme from the bacterium Escherichia coli can also convert 6-pyruvoyl-5,6,7,8-tetrahydropterin and sepiapterin to 6-carboxy-5,6,7,8-tetrahydropterin [1].
References:
1. 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 4.2.1.132
Accepted name: 2-hydroxyhexa-2,4-dienoate hydratase
Reaction: (2Z,4Z)-2-hydroxyhexa-2,4-dienoate + H2O = 4-hydroxy-2-oxohexanoate
Other name(s): tesE (gene name); hsaE (gene name)
Systematic name: (2Z,4Z)-2-hydroxyhexa-2,4-dienoate hydro-lyase
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.
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 4.2.3.14 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 reaction 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.
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 4.2.3.106
Accepted name: (E)-β-ocimene synthase
Reaction: geranyl diphosphate = (E)-β-ocimene + diphosphate
For diagram of reaction click here.
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.
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 4.2.3.107
Accepted name: (+)-car-3-ene synthase
Reaction: geranyl diphosphate = (+)-car-3-ene + diphosphate
For diagram of reaction click here and mechanism 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].
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 (2009) 106. [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 4.2.3.108
Accepted name: 1,8-cineole synthase
Reaction: geranyl diphosphate + H2O = 1,8-cineole + diphosphate
For diagram of reaction click here.
Glossary: 1,8-cineole = 1,8-epoxymenthane = 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-Cineol 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].
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 4.2.3.109
Accepted name: (–)-sabinene synthase
Reaction: geranyl diphosphate = (–)-sabinene + diphosphate
For diagram of reaction 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].
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 4.2.3.110
Accepted name: (+)-sabinene synthase
Reaction: geranyl diphosphate = (+)-sabinene + diphosphate
For diagram of reaction 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.
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 4.2.3.111
Accepted name: (–)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (–)-α-terpineol + diphosphate
For diagram of reaction 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.
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 4.2.3.112
Accepted name: (+)-α-terpineol synthase
Reaction: geranyl diphosphate + H2O = (+)-α-terpineol + diphosphate
For diagram of reaction 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.
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 4.2.3.113
Accepted name: terpinolene synthase
Reaction: geranyl diphosphate = terpinolene + diphosphate
For diagram of reaction 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.
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 4.2.3.114
Accepted name: γ-terpinene synthase
Reaction: geranyl diphosphate = γ-terpinene + diphosphate
For diagram of reaction 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.
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 4.2.3.115
Accepted name: α-terpinene synthase
Reaction: geranyl diphosphate = α-terpinene + diphosphate
For diagram of reaction 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.
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 4.2.3.116
Accepted name: (+)-camphene synthase
Reaction: geranyl diphosphate = (+)-camphene + diphosphate
For diagram of reaction click here.
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.
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 4.2.3.117
Accepted name: (–)-camphene synthase
Reaction: geranyl diphosphate = (–)-camphene + diphosphate
For diagram of reaction click here.
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.
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 4.2.3.118
Accepted name: 2-methylisoborneol synthase
Reaction: (E)-2-methylgeranyl diphosphate + H2O = 2-methylisoborneol + diphosphate
For diagram of reaction click here and mechanism 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.
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 4.2.3.119
Accepted name: (–)-α-pinene synthase
Reaction: geranyl diphosphate = (–)-α-pinene + diphosphate
For diagram of reaction 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.
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 4.2.3.120
Accepted name: (–)-β-pinene synthase
Reaction: geranyl diphosphate = (–)-β-pinene + diphosphate
For diagram of reaction 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.
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 4.2.3.121
Accepted name: (+)-α-pinene synthase
Reaction: geranyl diphosphate = (+)-α-pinene + diphosphate
For diagram of reaction 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.
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 4.2.3.122
Accepted name: (+)-β-pinene synthase
Reaction: geranyl diphosphate = (+)-β-pinene + diphosphate
For diagram of reaction 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.
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 4.2.3.123
Accepted name: β-sesquiphellandrene synthase
Reaction: (2E,6E)-farnesyl diphosphate = β-sesquiphellandrene + diphosphate
For diagram of reaction click here and mechanism click here.
Other name(s): Tps1; Os08g07100 (gene name)
Systematic name: (2E,6E)-farnesyl diphosphate diphosphate-lyase (cyclizing, β-sesquiphellandrene-forming)
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 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 keto—enol-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].
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 5.3.99.10
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 reaction click here.
Glossary: cThz*-P = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate
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.
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 5.5.1.8
Accepted name: (+)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (+)-bornyl diphosphate
For diagram of reaction click here and mechanism 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; bornyl pyrophosphate synthetase; (+)-bornylpyrophosphate cyclase; geranyl-diphosphate cyclase (ambiguous)
Systematic name: (+)-bornyl-diphosphate lyase (decyclizing)
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,
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 5.5.1.22
Accepted name: (–)-bornyl diphosphate synthase
Reaction: geranyl diphosphate = (–)-bornyl diphosphate
For diagram of reaction click here.
Glossary: (–)-bornyl diphosphate = (2R,4S)-1,7,7-trimethylbicyclo[2.2.1]hept-2-yl diphosphate
Other name(s): bornyl pyrophosphate synthase; bornyl pyrophosphate synthetase; (–)-bornyl pyrophosphate cyclase; bornyl diphosphate synthase; geranyl-diphosphate cyclase (ambiguous)
Systematic name: (–)-bornyl-diphosphate lyase (decyclizing)
Comments: Requires Mg2+. The enzyme from Tanacetum vulgare (tansey) 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.
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 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 reaction click here.
Glossary: preQ0 = 7-cyano-7-carbaguanine = 7-cyano-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.
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]
benzil = 1,2-diphenylethane-1,2-dione
benzil = 1,2-diphenylethane-1,2-dione
(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+
(2) L-threo-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
tetrahydrobiopterin = 5,6,7,8-tetrahydrobiopterin = 2-amino-6-(1,2-dihydroxypropyl)-5,6,7,8-tetrahydropteridin-4(3H)-one
(1a) linalool + NADH + H+ + O2 = (6E)-8-hydroxylinalool + NAD+ + H2O
(1b) (6E)-8-hydroxylinalool + NADH + H+ + O2 = (6E)-8-oxolinalool + NAD+ + 2 H2O
(2) thymine + FMNH2 + O2 = (Z)-2-methylureidoacrylate peracid + FMN
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
5-guanidino-3-methyl-2-oxopentanoate = 5-carbamimidamido-3-methyl-2-oxopentanoate
(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]
(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]
(2) S-adenosyl-L-methionine + erythromycin D = S-adenosyl-L-homocysteine + erythromycin B
(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)
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
cThz-P = 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = 4-methyl-5-[2-(phosphonooxy)ethyl]-1,3-thiazole-2-carboxylate
7-carboxy-7-carbaguanine = 7-carboxy-7-deazaguanine
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