The Enzyme Database

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EC 1.14.13.216     
Accepted name: asperlicin C monooxygenase
Reaction: asperlicin C + NAD(P)H + H+ + O2 = asperlicin E + NAD(P)+ + H2O
Other name(s): AspB
Systematic name: asperlicin C,NAD(P)H:oxygen oxidoreductase
Comments: The enzyme, characterized from the fungus Aspergillus alliaceus, contains an FAD cofactor. The enzyme inserts a hydroxyl group, leading to formation of a N-C bond that creates an additional cycle between the bicyclic indole and the tetracyclic core moieties, resulting in the heptacyclic asperlicin E.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Haynes, S.W., Gao, X., Tang, Y. and Walsh, C.T. Assembly of asperlicin peptidyl alkaloids from anthranilate and tryptophan: a two-enzyme pathway generates heptacyclic scaffold complexity in asperlicin E. J. Am. Chem. Soc. 134 (2012) 17444–17447. [DOI] [PMID: 23030663]
[EC 1.14.13.216 created 2016]
 
 
EC 1.14.14.1     
Accepted name: unspecific monooxygenase
Reaction: RH + [reduced NADPH—hemoprotein reductase] + O2 = ROH + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): microsomal monooxygenase; xenobiotic monooxygenase; aryl-4-monooxygenase; aryl hydrocarbon hydroxylase; microsomal P-450; flavoprotein-linked monooxygenase; flavoprotein monooxygenase; substrate,reduced-flavoprotein:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Systematic name: substrate,NADPH—hemoprotein reductase:oxygen oxidoreductase (RH-hydroxylating or -epoxidizing)
Comments: A group of P-450 heme-thiolate proteins, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. Together with EC 1.6.2.4, NADPH—hemoprotein reductase, it forms a system in which two reducing equivalents are supplied by NADPH. Some of the reactions attributed to EC 1.14.15.3, alkane 1-monooxygenase, belong here.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9038-14-6
References:
1.  Booth, J. and Boyland, E. The biochemistry of aromatic amines. 3. Enzymic hydroxylation by rat-liver microsomes. Biochem. J. 66 (1957) 73–78. [PMID: 13426111]
2.  Fujita, T. and Mannering, G.J. Differences in soluble P-450 hemoproteins from livers of rats treated with phenobarbital and 3-methylcholanthrene. Chem. Biol. Interact. 3 (1971) 264–265. [DOI] [PMID: 5132997]
3.  Haugen, D.A. and Coon, M.J. Properties of electrophoretically homogeneous phenobarbital-inducible and β-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J. Biol. Chem. 251 (1976) 7929–7939. [PMID: 187601]
4.  Imaoka, S., Inoue, K. and Funae, Y. Aminopyrine metabolism by multiple forms of cytochrome P-450 from rat liver microsomes: simultaneous quantitation of four aminopyrine metabolites by high-performance liquid chromatography. Arch. Biochem. Biophys. 265 (1988) 159–170. [DOI] [PMID: 3415241]
5.  Johnson, E.F., Zounes, M. and Müller-Eberhard, U. Characterization of three forms of rabbit microsomal cytochrome P-450 by peptide mapping utilizing limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. Arch. Biochem. Biophys. 192 (1979) 282–289. [DOI] [PMID: 434823]
6.  Kupfer, D., Miranda, G.K., Navarro, J., Piccolo, D.E. and Theoharides, A.D. Effect of inducers and inhibitors of monooxygenase on the hydroxylation of prostaglandins in the guinea pig. Evidence for several monooxygenases catalyzing ω- and ω-1-hydroxylation. J. Biol. Chem. 254 (1979) 10405–10414. [PMID: 489601]
7.  Lang, M.A., Gielen, J.E. and Nebert, D.W. Genetic evidence for many unique liver microsomal P-450-mediated monooxygenase activities in heterogeneic stock mice. J. Biol. Chem. 256 (1981) 12068–12075. [PMID: 7298645]
8.  Lang, M.A. and Nebert, D.W. Structural gene products of the Ah locus. Evidence for many unique P-450-mediated monooxygenase activities reconstituted from 3-methylcholanthrene-treated C57BL/6N mouse liver microsomes. J. Biol. Chem. 256 (1981) 12058–12075. [PMID: 7298644]
9.  Leo, M.A., Lasker, J.M., Rauby, J.L., Kim, C.I., Black, M. and Lieber, C.S. Metabolism of retinol and retinoic acid by human liver cytochrome P450IIC8. Arch. Biochem. Biophys. 269 (1989) 305–312. [DOI] [PMID: 2916844]
10.  Lu, A.Y.H., Kuntzman, S.W., Jacobson, M. and Conney, A.H. Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of the cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations. J. Biol. Chem. 247 (1972) 1727–1734. [PMID: 4401153]
11.  Mitoma, C., Posner, H.S., Reitz, H.C. and Udenfriend, S. Enzymic hydroxylation of aromatic compounds. Arch. Biochem. Biophys. 61 (1956) 431–441. [DOI] [PMID: 13314626]
12.  Mitoma, C. and Udenfriend, S. Aryl-4-hydroxylase. Methods Enzymol. 5 (1962) 816–819.
13.  Napoli, J.L., Okita, R.T., Masters, B.S. and Horst, R.L. Identification of 25,26-dihydroxyvitamin D3 as a rat renal 25-hydroxyvitamin D3 metabolite. Biochemistry 20 (1981) 5865–5871. [PMID: 7295706]
14.  Nebert, D.W. and Gelboin, H.V. Substrate-inducible microsomal aryl hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme. J. Biol. Chem. 243 (1968) 6242–6249. [PMID: 4387094]
15.  Suhara, K., Ohashi, K., Takahashi, K. and Katagiri, M. Aromatase and nonaromatizing 10-demethylase activity of adrenal cortex mitochondrial P-450(11)beta. Arch. Biochem. Biophys. 267 (1988) 31–37. [DOI] [PMID: 3264134]
16.  Theoharides, A.D. and Kupfer, D. Evidence for different hepatic microsomal monooxygenases catalyzing ω- and (ω-1)-hydroxylations of prostaglandins E1 and E2. Effects of inducers of monooxygenase on the kinetic constants of prostaglandin hydroxylation. J. Biol. Chem. 256 (1981) 2168–2175. [PMID: 7462235]
17.  Thomas, P.E., Lu, A.Y.H., Ryan, D., West, S.B., Kawalek, J. and Levin, W. Immunochemical evidence for six forms of rat liver cytochrome P450 obtained using antibodies against purified rat liver cytochromes P450 and P448. Mol. Pharmacol. 12 (1976) 746–758. [PMID: 825720]
[EC 1.14.14.1 created 1961 as EC 1.99.1.1, transferred 1965 to EC 1.14.1.1, transferred 1972 to EC 1.14.14.1 (EC 1.14.14.2 created 1972, incorporated 1976, EC 1.14.99.8 created 1972, incorporated 1984), modified 2015]
 
 
EC 1.14.14.23     
Accepted name: cholesterol 7α-monooxygenase
Reaction: cholesterol + [reduced NADPH—hemoprotein reductase] + O2 = 7α-hydroxycholesterol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of cholesterol catabolism (rings A, B and C), click here
Other name(s): cholesterol 7α-hydroxylase; CYP7A1 (gene name)
Systematic name: cholesterol,NADPH—hemoprotein reductase:oxygen oxidoreductase (7α-hydroxylating)
Comments: A P-450 heme-thiolate liver protein that catalyses the first step in the biosynthesis of bile acids. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH—hemoprotein reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-53-0
References:
1.  Mitton, J.R., Scholan, N.A. and Boyd, G.S. The oxidation of cholesterol in rat liver sub-cellular particles. The cholesterol-7α-hydroxylase enzyme system. Eur. J. Biochem. 20 (1971) 569–579. [DOI] [PMID: 4397276]
2.  Boyd, G.S., Grimwade, A.M. and Lawson, M.E. Studies on rat-liver microsomal cholesterol 7α-hydroxylase. Eur. J. Biochem. 37 (1973) 334–340. [DOI] [PMID: 4147676]
3.  Ogishima, T., Deguchi, S. and Okuda, K. Purification and characterization of cholesterol 7α-hydroxylase from rat liver microsomes. J. Biol. Chem. 262 (1987) 7646–7650. [PMID: 3584134]
4.  Nguyen, L.B., Shefer, S., Salen, G., Ness, G., Tanaka, R.D., Packin, V., Thomas, P., Shore, V. and Batta, A. Purification of cholesterol 7 α-hydroxylase from human and rat liver and production of inhibiting polyclonal antibodies. J. Biol. Chem. 265 (1990) 4541–4546. [PMID: 2106520]
5.  Nguyen, L.B., Shefer, S., Salen, G., Chiang, J.Y. and Patel, M. Cholesterol 7α-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation. Hepatology 24 (1996) 1468–1474. [DOI] [PMID: 8938182]
[EC 1.14.14.23 created 1976 as EC 1.14.13.17, transferred 2016 to EC 1.14.14.23]
 
 
EC 1.14.14.46     
Accepted name: pimeloyl-[acyl-carrier protein] synthase
Reaction: a long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O2 = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H2O (overall reaction)
(1a) a long-chain acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1b) a (7S)-7-hydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + oxidized flavodoxin + H2O
(1c) a (7R,8R)-7,8-dihydroxy-long-chain-acyl-[acyl-carrier protein] + reduced flavodoxin + O2 = a 7-oxoheptanoyl-[acyl-carrier protein] + an n-alkanal + oxidized flavodoxin + 2 H2O
(1d) a 7-oxoheptanoyl-[acyl-carrier protein] + oxidized flavodoxin + H2O = a pimeloyl-[acyl-carrier protein] + reduced flavodoxin + H+
Glossary: a long-chain acyl-[acyl-carrier protein] = an acyl-[acyl-carrier protein] thioester where the acyl chain contains 13 to 22 carbon atoms.
palmitoyl-[acyl-carrier protein] = hexadecanoyl-[acyl-carrier protein]
pimeloyl-[acyl-carrier protein] = 6-carboxyhexanoyl-[acyl-carrier protein]
Other name(s): bioI (gene name); P450BioI; CYP107H1
Systematic name: acyl-[acyl-carrier protein],reduced-flavodoxin:oxygen oxidoreductase (pimeloyl-[acyl-carrier protein]-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme catalyses an oxidative C-C bond cleavage of long-chain acyl-[acyl-carrier protein]s of various lengths to generate pimeloyl-[acyl-carrier protein], an intermediate in the biosynthesis of biotin. The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal. The mechanism is similar to EC 1.14.15.6, cholesterol monooxygenase (side-chain-cleaving), followed by a hydroxylation step, which may occur spontaneously [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Stok, J.E. and De Voss, J. Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384 (2000) 351–360. [DOI] [PMID: 11368323]
2.  Cryle, M.J. and De Voss, J.J. Carbon-carbon bond cleavage by cytochrome p450(BioI)(CYP107H1). Chem. Commun. (Camb.) (2004) 86–87. [DOI] [PMID: 14737344]
3.  Cryle, M.J. and Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc. Natl. Acad. Sci. USA 105 (2008) 15696–15701. [DOI] [PMID: 18838690]
4.  Cryle, M.J. Selectivity in a barren landscape: the P450(BioI)-ACP complex. Biochem. Soc. Trans. 38 (2010) 934–939. [DOI] [PMID: 20658980]
[EC 1.14.14.46 created 2013 as EC 1.14.15.12, transferred 2017 to EC 1.14.14.46]
 
 
EC 1.14.14.78     
Accepted name: phylloquinone ω-hydroxylase
Reaction: phylloquinone + [reduced NADPH—hemoprotein reductase] + O2 = ω-hydroxyphylloquinone + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of vitamin K biosynthesis, click here
Other name(s): vitamin K1 ω-hydroxylase; CYP4F2; CYP4F11
Systematic name: phylloquinone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxyphylloquinone-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein. Isolated from human tissue. The enzyme will also act on menaquinone-4. Prolonged action of CYP4F2, but not CYP4F11, on the ω hydroxyl group oxidizes it to the corresponding carboxylic acid. CYP4F2 also oxidizes leukotriene B4; see EC 1.14.13.30, leukotriene-B4 20-monooxygenase [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jin, R., Koop, D.R., Raucy, J.L. and Lasker, J.M. Role of human CYP4F2 in hepatic catabolism of the proinflammatory agent leukotriene B4. Arch. Biochem. Biophys. 359 (1998) 89–98. [DOI] [PMID: 9799565]
2.  Tang, Z., Salamanca-Pinzon, S.G., Wu, Z.L., Xiao, Y. and Guengerich, F.P. Human cytochrome P450 4F11: heterologous expression in bacteria, purification, and characterization of catalytic function. Arch. Biochem. Biophys. 494 (2010) 86–93. [DOI] [PMID: 19932081]
3.  Edson, K.Z., Prasad, B., Unadkat, J.D., Suhara, Y., Okano, T., Guengerich, F.P. and Rettie, A.E. Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. Biochemistry 52 (2013) 8276–8285. [DOI] [PMID: 24138531]
[EC 1.14.14.78 created 2014 as EC 1.14.13.194, transferred 2018 to EC 1.14.14.78]
 
 
EC 1.14.14.94     
Accepted name: leukotriene-B4 20-monooxygenase
Reaction: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + [reduced NADPH—hemoprotein reductase] + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): leukotriene-B4 20-hydroxylase; leucotriene-B4 ω-hydroxylase; LTB4 20-hydroxylase; LTB4 ω-hydroxylase; CYP4F2 (gene name); CYP4F3 (gene name)
Systematic name: (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (20-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 90119-11-2
References:
1.  Romano, M.C., Eckardt, R.D., Bender, P.E., Leonard, T.B., Straub, K.M. and Newton, J.F. Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases. J. Biol. Chem. 262 (1987) 1590–1595. [PMID: 3027095]
2.  Shak, S. and Goldstein, I.M. Leukotriene B4 ω-hydroxylase in human polymorphonuclear leukocytes. Partial purification and identification as a cytochrome P-450. J. Clin. Invest. 76 (1985) 1218–1228. [DOI] [PMID: 4044832]
3.  Soberman, R.J., Harper, T.W., Murphy, R.C. and Austen, K.F. Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes. Proc. Natl. Acad. Sci. USA 82 (1985) 2292–2295. [DOI] [PMID: 2986111]
[EC 1.14.14.94 created 1989 as EC 1.14.13.30, transferred 2018 to EC 1.14.14.94]
 
 
EC 1.14.14.124     
Accepted name: dihydromonacolin L hydroxylase
Reaction: dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin L acid + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) dihydromonacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = 3α-hydroxy-3,5-dihydromonacolin L acid + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) 3α-hydroxy-3,5-dihydromonacolin L acid = monacolin L acid + H2O (spontaneous)
For diagram of lovastatin biosynthesis, click here
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen1yl]-3,5-dihydroxyheptanoate
monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
3α-hydroxy-3,5-dihydromonacolin L = (3R,5R)-7-[(1R,2R,3S,6R,8aR)-3-hydroxy-2,6-dimethyl-1,2,3,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LovA (ambiguous)
Systematic name: dihydromonacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The dehydration of 3α-hydroxy-3,5-dihydromonacolin L acid is believed to be spontaneous [1,2]. The enzyme from fungi also catalyses the reaction of EC 1.14.14.125, monacolin L hydroxylase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Treiber, L.R., Reamer, R.A., Rooney, C.S. and Ramjit, H.G. Origin of monacolin L from Aspergillus terreus cultures. J. Antibiot. (Tokyo) 42 (1989) 30–36. [PMID: 2921224]
2.  Nakamura, T., Komagata, D., Murakawa, S., Sakai, K. and Endo, A. Isolation and biosynthesis of 3α-hydroxy-3,5-dihydromonacolin L. J. Antibiot. (Tokyo) 43 (1990) 1597–1600. [PMID: 2276977]
3.  Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078–8081. [DOI] [PMID: 21495633]
[EC 1.14.14.124 created 2014 as EC 1.14.13.197, transferred 2018 to EC 1.14.14.124]
 
 
EC 1.14.14.125     
Accepted name: monacolin L hydroxylase
Reaction: monacolin L acid + O2 + [reduced NADPH—hemoprotein reductase] = monacolin J acid + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of lovastatin biosynthesis, click here
Glossary: monacolin L acid = (3R,5R)-7-[(1S,2S,6R,8aR)-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
monacolin J acid = (3R,5R)-7-[(1S,2S,6R,8S,8aR)-8-hydroxy-2,6-dimethyl-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]-3,5-dihydroxyheptanoic acid
Other name(s): LovA (ambiguous)
Systematic name: monacolin L acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (8-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein. The enzyme from fungi also catalyses the reaction of EC 1.14.14.124, dihydromonacolin L hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Barriuso, J., Nguyen, D.T., Li, J.W., Roberts, J.N., MacNevin, G., Chaytor, J.L., Marcus, S.L., Vederas, J.C. and Ro, D.K. Double oxidation of the cyclic nonaketide dihydromonacolin L to monacolin J by a single cytochrome P450 monooxygenase, LovA. J. Am. Chem. Soc. 133 (2011) 8078–8081. [DOI] [PMID: 21495633]
[EC 1.14.14.125 created 2014 as EC 1.14.13.198, transferred 2018 to EC 1.14.14.125]
 
 
EC 1.14.14.139     
Accepted name: 5β-cholestane-3α,7α-diol 12α-hydroxylase
Reaction: (1) 5β-cholestane-3α,7α-diol + [reduced NADPH—hemoprotein reductase] + O2 = 5β-cholestane-3α,7α,12α-triol + [oxidized NADPH—hemoprotein reductase] + H2O
(2) 7α-hydroxycholest-4-en-3-one + [reduced NADPH—hemoprotein reductase] + O2 = 7α,12α-dihydroxycholest-4-en-3-one + [oxidized NADPH—hemoprotein reductase] + H2O
(3) chenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = cholate + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of cholesterol catabolism (rings A, B and C), click here
Glossary: chenodeoxycholate = 3α,7α-dihydroxy-5β-cholan-24-oate
cholate = 3α,7α-12α-trihydroxy-5β-cholan-24-oate
Other name(s): 5β-cholestane-3α,7α-diol 12α-monooxygenase; sterol 12α-hydroxylase (ambiguous); CYP8B1; cytochrome P450 8B1; 7α-hydroxycholest-4-en-3-one 12α-hydroxylase; 7α-hydroxy-4-cholesten-3-one 12α-monooxygenase; chenodeoxycholate 12α monooxygenase
Systematic name: 5β-cholestane-3α,7α-diol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (12α-hydroxylating)
Comments: A cytochrome P-450 (heme-thiolate) protein found in mammals. This is the key enzyme in the biosynthesis of the bile acid cholate. The enzyme can also hydroxylate 5β-cholestane-3α,7α-diol at the 25 and 26 position, but to a lesser extent [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis and metabolism of bile acids. Catalytic properties of different forms of cytochrome P-450. J. Biol. Chem. 255 (1980) 1643–1649. [PMID: 6766451]
2.  Hansson, R. and Wikvall, K. Hydroxylations in biosynthesis of bile acids. Cytochrome P-450 LM4 and 12α-hydroxylation of 5β-cholestane-3α,7α-diol. Eur. J. Biochem. 125 (1982) 423–429. [DOI] [PMID: 6811268]
3.  Ishida, H., Noshiro, M., Okuda, K. and Coon, M.J. Purification and characterization of 7α-hydroxy-4-cholesten-3-one 12α-hydroxylase. J. Biol. Chem. 267 (1992) 21319–21323. [PMID: 1400444]
4.  Eggertsen, G., Olin, M., Andersson, U., Ishida, H., Kubota, S., Hellman, U., Okuda, K.I. and Björkhem, I. Molecular cloning and expression of rabbit sterol 12α-hydroxylase. J. Biol. Chem. 271 (1996) 32269–32275. [DOI] [PMID: 8943286]
5.  Lundell, K. and Wikvall, K. Gene structure of pig sterol 12α-hydroxylase (CYP8B1) and expression in fetal liver: comparison with expression of taurochenodeoxycholic acid 6α-hydroxylase (CYP4A21). Biochim. Biophys. Acta 1634 (2003) 86–96. [DOI] [PMID: 14643796]
6.  del Castillo-Olivares, A. and Gil, G. α1-Fetoprotein transcription factor is required for the expression of sterol 12α -hydroxylase, the specific enzyme for cholic acid synthesis. Potential role in the bile acid-mediated regulation of gene transcription. J. Biol. Chem. 275 (2000) 17793–17799. [DOI] [PMID: 10747975]
7.  Yang, Y., Zhang, M., Eggertsen, G. and Chiang, J.Y. On the mechanism of bile acid inhibition of rat sterol 12α-hydroxylase gene (CYP8B1) transcription: roles of α-fetoprotein transcription factor and hepatocyte nuclear factor 4alpha. Biochim. Biophys. Acta 1583 (2002) 63–73. [DOI] [PMID: 12069850]
8.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
9.  Fan, L., Joseph, J.F., Durairaj, P., Parr, M.K. and Bureik, M. Conversion of chenodeoxycholic acid to cholic acid by human CYP8B1. Biol. Chem. 400 (2019) 625–628. [DOI] [PMID: 30465713]
[EC 1.14.14.139 created 2005 as EC 1.14.13.96, transferred 2018 to EC 1.14.14.139 (EC 1.14.18.8 created 2005 as EC 1.14.13.95, transferred 2015 to EC 1.14.18.8, incorporated 2020) , modified 2020]
 
 
EC 1.14.14.184     
Accepted name: 5-dehydro-6-demethoxyfumagillol synthase
Reaction: (+)-exo-β-bergamotene + 2 [reduced NADPH—hemoprotein reductase] + 3 O2 = 5-dehydro-6-demethoxyfumagillol + 2 [oxidized NADPH—hemoprotein reductase] + 3 H2O (overall reaction)
(1a) (+)-exo-β-bergamotene + [reduced NADPH—hemoprotein reductase] + O2 = (5R)-hydroxy-(+)-exo-β-bergamotene + [oxidized NADPH—hemoprotein reductase] + H2O
(1b) (5R)-hydroxy-(+)-exo-β-bergamotene + O2 = (3S)-3-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-methylidenecyclohexan-1-one + H2O
(1c) (3S)-3-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-methylidenecyclohexan-1-one + [reduced NADPH—hemoprotein reductase] + O2 = 5-dehydro-6-demethoxyfumagillol + [oxidized NADPH—hemoprotein reductase] + H2O
For diagram of reaction, click here and for diagram of santalene and bergamotene biosynthesis, click here
Glossary: (+)-exo-β-bergamotene = β-trans-bergamotene = (1S,5S,6R)-6-methyl-2-methylidene-6-(4-methylpent-3-enyl)bicyclo[3.1.1]heptane
fumagillol = (3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]octan-6-ol
fumagillin = (2E,4E,6E,8E)-10-({(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl}oxy)-10-oxodeca-2,4,6,8-tetraenoate
Other name(s): fumagillin multifunctional cytochrome P450 monooxygenase; Fma-P450; fmaG (gene name)
Systematic name: (+)-exo-β-bergamotene,[reduced NADPH—hemoprotein reductase] oxidoreductase (5-dehydro-6-demethoxyfumagillol-producing)
Comments: The enzyme, characterized from the mold Aspergillus fumigatus, catalyses a complex transformation comprising hydroxylation, bicyclic ring-opening, and two epoxidations, generating the sesquiterpenoid core skeleton of fumagillin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lin, H.C., Tsunematsu, Y., Dhingra, S., Xu, W., Fukutomi, M., Chooi, Y.H., Cane, D.E., Calvo, A.M., Watanabe, K. and Tang, Y. Generation of complexity in fungal terpene biosynthesis: discovery of a multifunctional cytochrome P450 in the fumagillin pathway. J. Am. Chem. Soc. 136 (2014) 4426–4436. [DOI] [PMID: 24568283]
[EC 1.14.14.184 created 2022]
 
 
EC 1.14.15.12      
Transferred entry: pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase
[EC 1.14.15.12 created 2013, deleted 2017]
 
 
EC 1.14.15.37     
Accepted name: luteothin monooxygenase
Reaction: luteothin + 2 O2 + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ = aureothin + 3 H2O + 4 oxidized ferredoxin [iron-sulfur] cluster (overall reaction)
(1a) luteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = (7R)-7-hydroxyluteothin + H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
(1b) (7R)-7-hydroxyluteothin + O2 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ = aureothin + 2 H2O + 2 oxidized ferredoxin [iron-sulfur] cluster
For diagram of aureothin catabolism, click here
Glossary: luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
Other name(s): aurH (gene name)
Systematic name: luteothin,ferredoxin:oxygen oxidoreductase (aureothin-forming)
Comments: The enzyme, characterized from the bacterium Streptomyces thioluteus, is a bifunctional cytochrome P-450 (heme-thiolate) protein that catalyses both the hydroxylation of its substrate and formation of a furan ring, the final step in the biosynthesis of the antibiotic aureothin. In the bacteria Streptomyces orinoci and Streptomyces spectabilis an orthologous enzyme catalyses a similar reaction that forms spectinabilin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  He, J., Muller, M. and Hertweck, C. Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome P450 monooxygenase. J. Am. Chem. Soc. 126 (2004) 16742–16743. [PMID: 15612710]
2.  Traitcheva, N., Jenke-Kodama, H., He, J., Dittmann, E. and Hertweck, C. Non-colinear polyketide biosynthesis in the aureothin and neoaureothin pathways: an evolutionary perspective. ChemBioChem 8 (2007) 1841–1849. [PMID: 17763486]
[EC 1.14.15.37 created 2019]
 
 
EC 1.14.19.59     
Accepted name: tryptophan 6-halogenase
Reaction: (1) L-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-L-tryptophan + FAD + 2 H2O
(2) D-tryptophan + FADH2 + chloride + O2 + H+ = 6-chloro-D-tryptophan + FAD + 2 H2O
For diagram of chlorotryptophan biosynthesis, click here
Other name(s): sttH (gene name); thdH (gene name)
Systematic name: L-tryptophan:FADH2 oxidoreductase (6-halogenating)
Comments: The enzyme is a flavin-dependent halogenase that has been described from several bacterial species. It utilizes molecular oxygen to oxidize the FADH2 cofactor, giving C4a-hydroperoxyflavin, which then reacts with chloride to produce a hypochlorite ion. The latter reacts with an active site lysine to generate a chloramine, which chlorinates the substrate. cf. EC 1.14.19.58, tryptophan 5-halogenase, and EC 1.14.19.9, tryptophan 7-halogenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zeng, J. and Zhan, J. Characterization of a tryptophan 6-halogenase from Streptomyces toxytricini. Biotechnol. Lett. 33 (2011) 1607–1613. [DOI] [PMID: 21424165]
2.  Milbredt, D., Patallo, E.P. and van Pee, K.H. A tryptophan 6-halogenase and an amidotransferase are involved in thienodolin biosynthesis. ChemBioChem 15 (2014) 1011–1020. [DOI] [PMID: 24692213]
3.  Shepherd, S.A., Menon, B.R., Fisk, H., Struck, A.W., Levy, C., Leys, D. and Micklefield, J. A structure-guided switch in the regioselectivity of a tryptophan halogenase. ChemBioChem 17 (2016) 821–824. [DOI] [PMID: 26840773]
[EC 1.14.19.59 created 2018]
 
 
EC 1.14.20.3     
Accepted name: (5R)-carbapenem-3-carboxylate synthase
Reaction: (3S,5S)-carbapenam-3-carboxylate + 2-oxoglutarate + O2 = (5R)-carbapen-2-em-3-carboxylate + succinate + CO2 + H2O
Glossary: (3S,5S)-carbapenam-3-carboxylate = (2S,5S)-7-oxo-1-azabicyclo[3.2.0]heptane-2-carboxylate
(5R)-carbapen-2-em-3-carboxylate = (5R)-7-oxo-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylate
Other name(s): carC (gene name)
Systematic name: (3S,5S)-carbapenam-3-carboxylate,2-oxoglutarate:oxygen oxidoreductase (dehydrating)
Comments: Requires Fe2+. The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. It catalyses a stereoinversion at C-5 and introduces a double bond between C-2 and C-3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Clifton, I.J., Doan, L.X., Sleeman, M.C., Topf, M., Suzuki, H., Wilmouth, R.C. and Schofield, C.J. Crystal structure of carbapenem synthase (CarC). J. Biol. Chem. 278 (2003) 20843–20850. [DOI] [PMID: 12611886]
2.  Stapon, A., Li, R. and Townsend, C.A. Carbapenem biosynthesis: confirmation of stereochemical assignments and the role of CarC in the ring stereoinversion process from L-proline. J. Am. Chem. Soc. 125 (2003) 8486–8493. [DOI] [PMID: 12848554]
3.  Sleeman, M.C., Smith, P., Kellam, B., Chhabra, S.R., Bycroft, B.W. and Schofield, C.J. Biosynthesis of carbapenem antibiotics: new carbapenam substrates for carbapenem synthase (CarC). ChemBioChem 5 (2004) 879–882. [DOI] [PMID: 15174175]
[EC 1.14.20.3 created 2013]
 
 
EC 1.15.1.1     
Accepted name: superoxide dismutase
Reaction: 2 superoxide + 2 H+ = O2 + H2O2
Glossary: superoxide = O2.-
Other name(s): superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein; hepatocuprein
Systematic name: superoxide:superoxide oxidoreductase
Comments: A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-89-1
References:
1.  Keele, B.B., McCord, J.M. and Fridovich, I. Further characterization of bovine superoxide dismutase and its isolation from bovine heart. J. Biol. Chem. 246 (1971) 2875–2880. [PMID: 4324341]
2.  Sawada, Y., Ohyama, T. and Yamazaki, I. Preparation and physicochemical properties of green pea superoxide dismutase. Biochim. Biophys. Acta 268 (1972) 305–312. [DOI] [PMID: 4337330]
3.  Vance, P.G., Keele, B.B. and Rajagopalan, K.V. Superoxide dismutase from Streptococcus mutans. Isolation and characterization of two forms of the enzyme. J. Biol. Chem. 247 (1972) 4782–4786. [PMID: 4559499]
[EC 1.15.1.1 created 1972]
 
 
EC 1.16.3.1     
Accepted name: ferroxidase
Reaction: 4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O
Other name(s): ceruloplasmin; caeruloplasmin; ferroxidase I; iron oxidase; iron(II):oxygen oxidoreductase; ferro:O2 oxidoreductase; iron II:oxygen oxidoreductase; hephaestin; HEPH
Systematic name: Fe(II):oxygen oxidoreductase
Comments: The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-37-2, 104404-69-5
References:
1.  Osaki, S. Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase (ceruloplasmin). J. Biol. Chem. 241 (1966) 5053–5059. [PMID: 5925868]
2.  Osaki, S. and Walaas, O. Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase. II. Rate constants at various steps and formation of a possible enzyme-substrate complex. J. Biol. Chem. 242 (1967) 2653–2657. [PMID: 6027241]
3.  Lindley, P.F. Card, G. Zaitseva, I. Zaitsev, V. Reinhammar, B. SelinLindgren, E. and Yoshida, K. An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity. J. Biol. Inorg. Chem. 2 (1997) 454–463.
4.  Takai, M., Kamimura, K. and Sugio, T. A new iron oxidase from a moderately thermophilic iron oxidizing bacterium strain TI-1. Eur. J. Biochem. 268 (2001) 1653–1658. [DOI] [PMID: 11248684]
5.  Chen, H., Attieh, Z.K., Su, T., Syed, B.A., Gao, H., Alaeddine, R.M., Fox, T.C., Usta, J., Naylor, C.E., Evans, R.W., McKie, A.T., Anderson, G.J. and Vulpe, C.D. Hephaestin is a ferroxidase that maintains partial activity in sex-linked anemia mice. Blood 103 (2004) 3933–3939. [DOI] [PMID: 14751926]
[EC 1.16.3.1 created 1972, modified 2011]
 
 
EC 1.17.99.3     
Accepted name: 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase
Reaction: (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3α,7α,12α,24-tetrahydroxy-5β-cholestan-26-oyl-CoA + reduced acceptor
For diagram of cholic-acid biosynthesis (sidechain), click here
Other name(s): trihydroxycoprostanoyl-CoA oxidase; THC-CoA oxidase; THCA-CoA oxidase; 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase; 3α,7α,12α-trihydroxy-5β-cholestan-26-oate 24-hydroxylase
Systematic name: (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oyl-CoA:acceptor 24-oxidoreductase (24R-hydroxylating)
Comments: Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration [1]. However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate and not via hydration of a 24(25) double bond [5]. In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 119799-47-2
References:
1.  Gustafsson, J. Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of 3α,7α,12α-trihydroxy-5β-cholestanoic acid. J. Biol. Chem. 250 (1975) 8243–8247. [PMID: 240854]
2.  Schepers, L., Van Veldhoven, P.P., Casteels, M., Eyssen, H.J. and Mannaerts, G.P. Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. J. Biol. Chem. 265 (1990) 5242–5246. [PMID: 2156865]
3.  Dieuaide-Noubhani, M., Novikov, D., Baumgart, E., Vanhooren, J.C., Fransen, M., Goethals, M., Vandekerckhove, J., Van Veldhoven, P.P. and Mannaerts, G.P. Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins. Eur. J. Biochem. 240 (1996) 660–666. [DOI] [PMID: 8856068]
4.  Dieuaide-Noubhani, M., Novikov, D., Baumgart, E., Vanhooren, J.C., Fransen, M., Goethals, M., Vandekerckhove, J., Van Veldhoven, P.P. and Mannaerts, G.P. Erratum report. Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins. Eur. J. Biochem. 243 (1997) 537.
5.  Pedersen, J.I., Eggertsen, G., Hellman, U., Andersson, U. and Björkhem, I. Molecular cloning and expression of cDNA encoding 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase from rabbit liver. J. Biol. Chem. 272 (1997) 18481–18489. [DOI] [PMID: 9218493]
6.  Russell, D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 72 (2003) 137–174. [DOI] [PMID: 12543708]
[EC 1.17.99.3 created 2005]
 
 
EC 2.1.1.11     
Accepted name: magnesium protoporphyrin IX methyltransferase
Reaction: S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester
For diagram of the earlier stages of chlorophyll biosynthesis, click here
Systematic name: S-adenosyl-L-methionine:magnesium-protoporphyrin-IX O-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-82-7
References:
1.  Gibson, K.D., Neuberger, A. and Tait, G.H. Studies on the biosynthesis of porphyrin and bacteriochlorophyll by Rhodopseudomonas spheroides. 4. S-Adenosylmethioninemagnesium protoporphyrin methyltransferase. Biochem. J. 88 (1963) 325–334. [PMID: 14063871]
2.  Shepherd, M., Reid, J.D. and Hunter, C.N. Purification and kinetic characterisation of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803. Biochem. J. 371 (2003) 351–360. [DOI] [PMID: 12489983]
3.  Bollivar, D.W., Jiang, Z.Y., Bauer, C.E. and Beale, S.I. Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase. J. Bacteriol. 176 (1994) 5290–5296. [DOI] [PMID: 8071204]
4.  Gibson, L.C. and Hunter, C.N. The bacteriochlorophyll biosynthesis gene, bchM, of Rhodobacter sphaeroides encodes S-adenosyl-L-methionine: Mg protoporphyrin IX methyltransferase. FEBS Lett. 352 (1994) 127–130. [DOI] [PMID: 7925960]
5.  Ebbon, J.G. and Tait, G.H. Studies on S-adenosylmethionine-magnesium protoporphyrin methyltransferase in Euglena gracilis strain Z. Biochem. J. 111 (1969) 573–582. [PMID: 5774480]
[EC 2.1.1.11 created 1965, modified 2003]
 
 
EC 2.1.1.37     
Accepted name: DNA (cytosine-5-)-methyltransferase
Reaction: S-adenosyl-L-methionine + DNA containing cytosine = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Other name(s): EcoRI methylase; DNA 5-cytosine methylase; DNA cytosine C5 methylase; DNA cytosine methylase; DNA methylase (ambiguous); DNA methyltransferase (ambiguous); DNA transmethylase (ambiguous); DNA-cytosine 5-methylase; DNA-cytosine methyltransferase; HpaII methylase; HpaII′ methylase; M.BsuRIa; M.BsuRIb; Type II DNA methylase; cytosine 5-methyltransferase; cytosine DNA methylase; cytosine DNA methyltransferase; cytosine-specific DNA methyltransferase; deoxyribonucleate methylase (ambiguous); deoxyribonucleate methyltransferase (ambiguous); deoxyribonucleic (cytosine-5-)-methyltransferase; deoxyribonucleic acid (cytosine-5-)-methyltransferase; deoxyribonucleic acid methylase (ambiguous); deoxyribonucleic acid methyltransferase (ambiguous); deoxyribonucleic acid modification methylase (ambiguous); deoxyribonucleic methylase (ambiguous); methylphosphotriester-DNA methyltransferase (ambiguous); modification methylase (ambiguous); restriction-modification system (ambiguous); site-specific DNA-methyltransferase (cytosine-specific); DNA-(cytosine C5)-methylase
Systematic name: S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9037-42-7
References:
1.  Gold, M. and Hurwitz, J. The enzymatic methylation of ribonucleic acid and deoxyribonucleic acid. V. Purification and properties of the deoxyribonucleic acid-methylating activity of Escherichia coli. J. Biol. Chem. 239 (1964) 3858. [PMID: 14257620]
2.  Kalousek, F. and Morris, N.R. The purification and properties of deoxyribonucleic acid methylase from rat spleen. J. Biol. Chem. 244 (1969) 1157–1163. [PMID: 4975067]
3.  Roy, P.H. and Weissbach, A. DNA methylase from HeLa cell nuclei. Nucleic Acids Res. 2 (1975) 1669–1684. [DOI] [PMID: 1187340]
4.  Simon, D., Grunert, F., Acken, U.Y., Döring, H.P. and Kröger, H. DNA-methylase from regenerating rat liver: purification and characterisation. Nucleic Acids Res. 5 (1978) 2153–2167. [DOI] [PMID: 673848]
5.  Sneider, T.W., Teague, W.M. and Rogachewsky, L.M. S-Adenosylmethionine: DNA-cytosine 5-methyltransferase from a Novikoff rat hepatoma cell line. Nucleic Acids Res. 2 (1975) 1685–1700. [DOI] [PMID: 171625]
6.  Turnbull, J.F. and Adams, R.L.P. DNA methylase: purification from ascites cells and the effect of various DNA substrates on its activity. Nucleic Acids Res. 3 (1976) 677–695. [DOI] [PMID: 131936]
7.  Kessler, C. and Manta, V. Specificity of restriction endonucleases and DNA modification methyltransferases: a review. Gene 92 (1990) 1–248. [DOI] [PMID: 2172084]
8.  Roberts, R.J. Restriction enzymes and their isoschizomers. Nucleic Acids Res. 18 (1990) 2331–2365. [PMID: 2159140]
9.  Yuan, R. Structure and mechanism of multifunctional restriction endonucleases. Annu. Rev. Biochem. 50 (1981) 285–319. [DOI] [PMID: 6267988]
[EC 2.1.1.37 created 1972, (EC 2.1.1.73 incorporated 2003), modified 2003]
 
 
EC 2.1.1.55     
Accepted name: tRNA (adenine-N6-)-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N6-methyladenine
Other name(s): S-adenosyl-L-methionine:tRNA (adenine-6-N-)-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (adenine-N6-)-methyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9014-53-3
References:
1.  Mandel, R., Hacker, B. and Maag, T.A. Altered transfer RNA methylase patterns in Marek's disease tumors. Cancer Res. 31 (1971) 613–616. [PMID: 4996578]
2.  Mittelman, A., Hall, R.H., Yohn, D.S. and Grace, J.T. The in vitro soluble RNA methylase activity of SV40-induced hamster tumors. Cancer Res. 27 (1967) 1409–1414. [PMID: 4292682]
3.  Sharma, O.K. Differences in the transfer RNA methyltransferases from normal rat liver and Novikoff hepatoma. Biochim. Biophys. Acta 299 (1973) 415–427. [DOI] [PMID: 4349332]
[EC 2.1.1.55 created 1981]
 
 
EC 2.1.1.64     
Accepted name: 3-demethylubiquinol 3-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-demethylubiquinol-n = S-adenosyl-L-homocysteine + ubiquinol-n
For diagram of ubiquinol biosynthesis, click here
Glossary: 3-demethylubiquinol-n = 3-hydroxy-2-methoxy-5-methyl-6-(all-trans-polyprenyl)-1,4-benzoquinol
Other name(s): 5-demethylubiquinone-9 methyltransferase; OMHMB-methyltransferase; 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; 3-demethylubiquinone-9 3-methyltransferase; ubiG (gene name, ambiguous)
Systematic name: S-adenosyl-L-methionine:3-hydroxy-2-methoxy-5-methyl-6-(all-trans-polyprenyl)-1,4-benzoquinol 3-O-methyltransferase
Comments: This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate [3] (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 63774-48-1
References:
1.  Houser, R.M. and Olson, R.E. 5-Demethylubiquinone-9-methyltransferase from rat liver mitochondria. Characterization, localization, and solubilization. J. Biol. Chem. 252 (1977) 4017–4021. [PMID: 863914]
2.  Leppik, R.A., Stroobant, P., Shineberg, B., Young, I.G. and Gibson, F. Membrane-associated reactions in ubiquinone biosynthesis. 2-Octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase. Biochim. Biophys. Acta 428 (1976) 146–156. [DOI] [PMID: 769831]
3.  Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 274 (1999) 21665–21672. [DOI] [PMID: 10419476]
4.  Jonassen, T. and Clarke, C.F. Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. J. Biol. Chem. 275 (2000) 12381–12387. [DOI] [PMID: 10777520]
[EC 2.1.1.64 created 1982, modified 2011]
 
 
EC 2.1.1.114     
Accepted name: polyprenyldihydroxybenzoate methyltransferase
Reaction: S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
For diagram of ubiquinol biosynthesis, click here
Other name(s): 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase; dihydroxyhexaprenylbenzoate methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; DHHB O-methyltransferase
Systematic name: S-adenosyl-L-methionine:3,4-dihydroxy-5-all-trans-polyprenylbenzoate 3-O-methyltransferase
Comments: This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast and rat also catalyse the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively [2] (this activity is classified as EC 2.1.1.64, 3-demethylubiquinol 3-O-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 139569-31-6
References:
1.  Clarke, C.F., Williams, W., Teruya, J.H. Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene. J. Biol. Chem. 266 (1991) 16636–16641. [PMID: 1885593]
2.  Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 274 (1999) 21665–21672. [DOI] [PMID: 10419476]
3.  Jonassen, T. and Clarke, C.F. Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. J. Biol. Chem. 275 (2000) 12381–12387. [DOI] [PMID: 10777520]
4.  Xing, L., Zhu, Y., Fang, P., Wang, J., Zeng, F., Li, X., Teng, M. and Li, X. Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 727–729. [DOI] [PMID: 21636923]
[EC 2.1.1.114 created 1999]
 
 
EC 2.1.1.137     
Accepted name: arsenite methyltransferase
Reaction: (1) S-adenosyl-L-methionine + arsenic triglutathione + thioredoxin + 2 H2O = S-adenosyl-L-homocysteine + methylarsonous acid + 3 glutathione + thioredoxin disulfide
(2) 2 S-adenosyl-L-methionine + arsenic triglutathione + 2 thioredoxin + H2O = S-adenosyl-L-homocysteine + dimethylarsinous acid + 3 glutathione + 2 thioredoxin disulfide
(3) 3 S-adenosyl-L-methionine + arsenic triglutathione + 3 thioredoxin = S-adenosyl-L-homocysteine + trimethylarsane + 3 glutathione + 3 thioredoxin disulfide
For diagram of arsenate catabolism, click here
Other name(s): AS3MT (gene name); arsM (gene name); S-adenosyl-L-methionine:arsenic(III) methyltransferase; S-adenosyl-L-methionine:methylarsonite As-methyltransferase; methylarsonite methyltransferase
Systematic name: S-adenosyl-L-methionine:arsenous acid As-methyltransferase
Comments: An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes [11] or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) [6], from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues [10] via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid [9]. However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 167140-41-2
References:
1.  Zakharyan, R.A., Wu, Y., Bogdan, G.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. Chem. Res. Toxicol. 8 (1995) 1029–1038. [PMID: 8605285]
2.  Zakharyan, R.A., Wildfang, E. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140 (1996) 77–84. [DOI] [PMID: 8806872]
3.  Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 12 (1999) 1278–1283. [DOI] [PMID: 10604879]
4.  Zakharyan, R.A., Ayala-Fierro, F., Cullen, W.R., Carter, D.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. Toxicol. Appl. Pharmacol. 158 (1999) 9–15. [DOI] [PMID: 10387927]
5.  Lin, S., Shi, Q., Nix, F.B., Styblo, M., Beck, M.A., Herbin-Davis, K.M., Hall, L.L., Simeonsson, J.B. and Thomas, D.J. A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol. J. Biol. Chem. 277 (2002) 10795–10803. [DOI] [PMID: 11790780]
6.  Hayakawa, T., Kobayashi, Y., Cui, X. and Hirano, S. A new metabolic pathway of arsenite: arsenic-glutathione complexes are substrates for human arsenic methyltransferase Cyt19. Arch Toxicol 79 (2005) 183–191. [DOI] [PMID: 15526190]
7.  Dheeman, D.S., Packianathan, C., Pillai, J.K. and Rosen, B.P. Pathway of human AS3MT arsenic methylation. Chem. Res. Toxicol. 27 (2014) 1979–1989. [DOI] [PMID: 25325836]
8.  Marapakala, K., Packianathan, C., Ajees, A.A., Dheeman, D.S., Sankaran, B., Kandavelu, P. and Rosen, B.P. A disulfide-bond cascade mechanism for arsenic(III) S-adenosylmethionine methyltransferase. Acta Crystallogr. D Biol. Crystallogr. 71 (2015) 505–515. [DOI] [PMID: 25760600]
9.  Yang, H.C. and Rosen, B.P. New mechanisms of bacterial arsenic resistance. Biomed J 39 (2016) 5–13. [DOI] [PMID: 27105594]
10.  Packianathan, C., Kandavelu, P. and Rosen, B.P. The structure of an As(III) S-adenosylmethionine methyltransferase with 3-coordinately bound As(III) depicts the first step in catalysis. Biochemistry 57 (2018) 4083–4092. [DOI] [PMID: 29894638]
11.  Chen, J., Yoshinaga, M. and Rosen, B.P. The antibiotic action of methylarsenite is an emergent property of microbial communities. Mol. Microbiol. 111 (2019) 487–494. [DOI] [PMID: 30520200]
[EC 2.1.1.137 created 2000, (EC 2.1.1.138 incorporated 2003), modified 2003, modified 2021]
 
 
EC 2.1.1.163     
Accepted name: demethylmenaquinone methyltransferase
Reaction: a demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine
For diagram of vitamin-K biosynthesis, click here
Other name(s): S-adenosyl-L-methione—DMK methyltransferase; demethylmenaquinone C-methylase; 2-heptaprenyl-1,4-naphthoquinone methyltransferase; 2-demethylmenaquinone methyltransferase; S-adenosyl-L-methione:2-demethylmenaquinone methyltransferase
Systematic name: S-adenosyl-L-methione:demethylmenaquinone methyltransferase
Comments: The enzyme catalyses the last step in menaquinone biosynthesis. It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase)[1]. The enzyme from Escherichia coli also catalyses the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3-octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone [4]. The enzyme probably acts on menaquinol rather than menaquinone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Koike-Takeshita, A., Koyama, T. and Ogura, K. Identification of a novel gene cluster participating in menaquinone (vitamin K2) biosynthesis. Cloning and sequence determination of the 2-heptaprenyl-1,4-naphthoquinone methyltransferase gene of Bacillus stearothermophilus. J. Biol. Chem. 272 (1997) 12380–12383. [DOI] [PMID: 9139683]
2.  Wissenbach, U., Ternes, D. and Unden, G. An Escherichia coli mutant containing only demethylmenaquinone, but no menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration. Arch. Microbiol. 158 (1992) 68–73. [PMID: 1444716]
3.  Catala, F., Azerad, R. and Lederer, E. Sur les propriétés de la desméthylménaquinone C-méthylase de Mycobacterium phlei. Int. Z. Vitaminforsch. 40 (1970) 363–373. [PMID: 5450997]
4.  Lee, P.T., Hsu, A.Y., Ha, H.T. and Clarke, C.F. A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol. 179 (1997) 1748–1754. [DOI] [PMID: 9045837]
[EC 2.1.1.163 created 2009]
 
 
EC 2.1.1.201     
Accepted name: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase
Reaction: S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
For diagram of ubiquinol biosynthesis, click here
Other name(s): ubiE (gene name, ambiguous)
Systematic name: S-adenosyl-L-methionine:2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol 5-C-methyltransferase
Comments: This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant [3]. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Lee, P.T., Hsu, A.Y., Ha, H.T. and Clarke, C.F. A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol. 179 (1997) 1748–1754. [DOI] [PMID: 9045837]
2.  Young, I.G., McCann, L.M., Stroobant, P. and Gibson, F. Characterization and genetic analysis of mutant strains of Escherichia coli K-12 accumulating the biquinone precursors 2-octaprenyl-6-methoxy-1,4-benzoquinone and 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone. J. Bacteriol. 105 (1971) 769–778. [PMID: 4323297]
3.  Dibrov, E., Robinson, K.M. and Lemire, B.D. The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain. J. Biol. Chem. 272 (1997) 9175–9181. [DOI] [PMID: 9083048]
4.  Barkovich, R.J., Shtanko, A., Shepherd, J.A., Lee, P.T., Myles, D.C., Tzagoloff, A. and Clarke, C.F. Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis. J. Biol. Chem. 272 (1997) 9182–9188. [DOI] [PMID: 9083049]
[EC 2.1.1.201 created 2011]
 
 
EC 2.1.1.222     
Accepted name: 2-polyprenyl-6-hydroxyphenol methylase
Reaction: S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
For diagram of ubiquinol biosynthesis, click here
Other name(s): ubiG (gene name, ambiguous); ubiG methyltransferase (ambiguous); 2-octaprenyl-6-hydroxyphenol methylase
Systematic name: S-adenosyl-L-methionine:3-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase
Comments: UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) [2]. In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Poon, W.W., Barkovich, R.J., Hsu, A.Y., Frankel, A., Lee, P.T., Shepherd, J.N., Myles, D.C. and Clarke, C.F. Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 274 (1999) 21665–21672. [DOI] [PMID: 10419476]
2.  Hsu, A.Y., Poon, W.W., Shepherd, J.A., Myles, D.C. and Clarke, C.F. Complementation of coq3 mutant yeast by mitochondrial targeting of the Escherichia coli UbiG polypeptide: evidence that UbiG catalyzes both O-methylation steps in ubiquinone biosynthesis. Biochemistry 35 (1996) 9797–9806. [DOI] [PMID: 8703953]
[EC 2.1.1.222 created 2011, modified 2013]
 
 
EC 2.1.1.230     
Accepted name: 23S rRNA (adenosine1067-2′-O)-methyltransferase
Reaction: S-adenosyl-L-methionine + adenosine1067 in 23S rRNA = S-adenosyl-L-homocysteine + 2′-O-methyladenosine1067 in 23S rRNA
Other name(s): 23S rRNA A1067 2′-methyltransferase; thiostrepton-resistance methylase; nosiheptide-resistance methyltransferase
Systematic name: S-adenosyl-L-methionine:23S rRNA (adenosine1067-2′-O)-methyltransferase
Comments: The methylase that is responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bechthold, A. and Floss, H.G. Overexpression of the thiostrepton-resistance gene from Streptomyces azureus in Escherichia coli and characterization of recognition sites of the 23S rRNA A1067 2′-methyltransferase in the guanosine triphosphatase center of 23S ribosomal RNA. Eur. J. Biochem. 224 (1994) 431–437. [DOI] [PMID: 7925357]
2.  Thompson, J., Schmidt, F. and Cundliffe, E. Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton. J. Biol. Chem. 257 (1982) 7915–7917. [PMID: 6806287]
3.  Thompson, J. and Cundliffe, E. Purification and properties of an RNA methylase produced by Streptomyces azureus and involved in resistance to thiostrepton. J. Gen. Microbiol. 124 (1981) 291–297.
4.  Yang, H., Wang, Z., Shen, Y., Wang, P., Jia, X., Zhao, L., Zhou, P., Gong, R., Li, Z., Yang, Y., Chen, D., Murchie, A.I. and Xu, Y. Crystal structure of the nosiheptide-resistance methyltransferase of Streptomyces actuosus. Biochemistry 49 (2010) 6440–6450. [DOI] [PMID: 20550164]
[EC 2.1.1.230 created 2011]
 
 
EC 2.1.1.315     
Accepted name: 27-O-demethylrifamycin SV methyltransferase
Reaction: S-adenosyl-L-methionine + 27-O-demethylrifamycin SV = S-adenosyl-L-homocysteine + rifamycin SV
Glossary: rifamycin SV = (7S,9E,11S,12R,13S,14R,15R,16R,17S,18S,19E,21Z)-2,15,17,27,29-pentahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-6,23-dioxo-8,30-dioxa-24-azatetracyclo[23.3.1.14,7.05,28]triaconta-1(28),2,4,9, 19,21,25(29),26-octaen-13-yl acetate
Other name(s): AdoMet:27-O-demethylrifamycin SV methyltransferase
Systematic name: S-adenosyl-L-methionine:27-O-demethylrifamycin-SV 27-O-methyltransferase
Comments: The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the antitubercular drug rifamycin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Xu, J., Mahmud, T. and Floss, H.G. Isolation and characterization of 27-O-demethylrifamycin SV methyltransferase provides new insights into the post-PKS modification steps during the biosynthesis of the antitubercular drug rifamycin B by Amycolatopsis mediterranei S699. Arch. Biochem. Biophys. 411 (2003) 277–288. [DOI] [PMID: 12623077]
[EC 2.1.1.315 created 2015]
 
 
EC 2.1.1.351     
Accepted name: nocamycin O-methyltransferase
Reaction: S-adenosyl-L-methionine + nocamycin E = S-adenosyl-L-homocysteine + nocamycin I
For diagram of reaction, click here
Glossary: nocamycin E = (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
nocamycin I = methyl (2R,3S,3aS,5R,6R,7S,9aS)-5-[(2R,3E,5E)-7-hydroxy-4-methyl-7-(2,4-dioxopyrroliden-3-ylidene)hepta-3,5-dien-2-yl]-2,6,9a-trimethyl-8-oxooctahydro-3a,7-epoxyfuro[3,2-b]oxocine-3-carboxylate
Other name(s): ncmP (gene name)
Systematic name: S-adenosyl-L-methionine:nocamycin E O-methyltransferase
Comments: The enzyme, isolated from the bacterium Saccharothrix syringae, is involved in the biosynthesis of nocamycin I and nocamycin II.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mo, X., Gui, C. and Wang, Q. Elucidation of a carboxylate O-methyltransferase NcmP in nocamycin biosynthetic pathway. Bioorg. Med. Chem. Lett. 27 (2017) 4431–4435. [PMID: 28818448]
[EC 2.1.1.351 created 2018]
 
 
EC 2.1.1.353     
Accepted name: demethylluteothin O-methyltransferase
Reaction: S-adenosyl-L-methionine + demethylluteothin = S-adenosyl-L-homocysteine + luteothin
Glossary: luteothin = 2-[(3E,5E)-3,5-dimethyl-6-(4-nitrophenyl)hexa-3,5-dien-1-yl]-6-methoxy-3,5-dimethyl-4H-pyran-4-one
aureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E)-2-methyl-3-(4-nitrophenyl)prop-2-en-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
spectinabilin = neoaureothin = 2-methoxy-3,5-dimethyl-6-[(2R,4Z)-4-[(2E,4E,6E)-2,4,6-trimethyl-7-(4-nitrophenyl)hepta-2,4,6-trien-1-ylidene]oxolan-2-yl]-4H-pyran-4-one
Other name(s): aurI (gene name)
Systematic name: S-adenosyl-L-methionine:demethylluteothin O-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces thioluteus, participates in the biosynthesis of the antibiotic aureothin. An orthologous enzyme in the bacteria Streptomyces orinoci and Streptomyces spectabilis catalyses a similar reaction in the biosynthesis of spectinabilin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  He, J., Muller, M. and Hertweck, C. Formation of the aureothin tetrahydrofuran ring by a bifunctional cytochrome P450 monooxygenase. J. Am. Chem. Soc. 126 (2004) 16742–16743. [PMID: 15612710]
2.  Muller, M., He, J. and Hertweck, C. Dissection of the late steps in aureothin biosynthesis. ChemBioChem 7 (2006) 37–39. [PMID: 16292785]
[EC 2.1.1.353 created 2019]
 
 
EC 2.1.1.363     
Accepted name: pre-sodorifen synthase
Reaction: S-adenosyl-L-methionine + (2E,6E)-farnesyl diphosphate = S-adenosyl-L-homocysteine + pre-sodorifen diphosphate
Glossary: pre-sodorifen diphosphate = [(2E)-3-methyl-5-[(1S,4R,5R)-1,2,3,4,5-pentamethylcyclopent-2-en-1-yl]pent-2-en-1-yl phosphonato]oxyphosphonate
sodorifen = (1S,2S,4R,5S,8s)-1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo[3.2.1]oct-6-ene
Other name(s): sodC (gene name)
Systematic name: (2E,6E)-farnesyl diphosphate 10-C-methyltransferase (cyclyzing, pre-sodorifen diphosphate producing)
Comments: The enzyme, characterized from the bacterium Serratia plymuthica, participates in biosynthesis of sodorifen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Domik, D., Magnus, N. and Piechulla, B. Analysis of a new cluster of genes involved in the synthesis of the unique volatile organic compound sodorifen of Serratia plymuthica 4Rx13. FEMS Microbiol. Lett. 363(14): fnw139 (2016). [DOI] [PMID: 27231241]
2.  Schmidt, R., Jager, V., Zuhlke, D., Wolff, C., Bernhardt, J., Cankar, K., Beekwilder, J., Ijcken, W.V., Sleutels, F., Boer, W., Riedel, K. and Garbeva, P. Fungal volatile compounds induce production of the secondary metabolite sodorifen in Serratia plymuthica PRI-2C. Sci. Rep. 7:862 (2017). [PMID: 28408760]
3.  von Reuss, S., Domik, D., Lemfack, M.C., Magnus, N., Kai, M., Weise, T. and Piechulla, B. Sodorifen biosynthesis in the rhizobacterium Serratia plymuthica involves methylation and cyclization of MEP-derived farnesyl pyrophosphate by a SAM-dependent C-methyltransferase. J. Am. Chem. Soc. 140 (2018) 11855–11862. [PMID: 30133268]
[EC 2.1.1.363 created 2019]
 
 
EC 2.1.1.374     
Accepted name: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Reaction: S-adenosyl-L-methionine + 2-heptyl-1-hydroxyquinolin-4(1H)-one = S-adenosyl-L-homocysteine + 2-heptyl-1-methoxyquinolin-4(1H)-one
Other name(s): htm (gene name)
Systematic name: S-adenosyl-L-methionine:2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase
Comments: The enzyme, found in mycobacteria, is a member of a family of heterocyclic toxin methyltransferases. It is involved in defense against several antimicrobial natural compounds and drugs. 4-Hydroxyquinolin-2(1H)-one, 2-heptylquinolin-4(1H)-one, 2-heptyl-3-hydroxyquinolin-4(1H)-one (the "Pseudomonas quinolone signal", PQS) and the flavonol quercetin are also O-methylated, albeit with lower activity [2]. The enzyme also N-methylates the bactericidal compound 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1-yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Warrier, T., Kapilashrami, K., Argyrou, A., Ioerger, T.R., Little, D., Murphy, K.C., Nandakumar, M., Park, S., Gold, B., Mi, J., Zhang, T., Meiler, E., Rees, M., Somersan-Karakaya, S., Porras-De Francisco, E., Martinez-Hoyos, M., Burns-Huang, K., Roberts, J., Ling, Y., Rhee, K.Y., Mendoza-Losana, A., Luo, M. and Nathan, C.F. N-methylation of a bactericidal compound as a resistance mechanism in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 113 (2016) E4523–E4530. [DOI] [PMID: 27432954]
2.  Sartor, P., Bock, J., Hennecke, U., Thierbach, S. and Fetzner, S. Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-hydroxyquinolin-4(1H)-one and other secondary metabolites by methyltransferases from mycobacteria. FEBS J. (2020) . [DOI] [PMID: 33064871]
[EC 2.1.1.374 created 2020]
 
 
EC 2.1.1.390     
Accepted name: gentamicin X2 methyltransferase
Reaction: gentamicin X2 + 2 S-adenosyl-L-methionine + reduced acceptor = geneticin + 5′-deoxyadenosine + L-methionine + S-adenosyl-L-homocysteine + oxidized acceptor (overall reaction)
(1a) S-adenosyl-L-methionine + cob(I)alamin = S-adenosyl-L-homocysteine + methylcob(III)alamin
(1b) methylcob(III)alamin + gentamicin X2 + S-adenosyl-L-methionine = cob(III)alamin + geneticin + 5′-deoxyadenosine + L-methionine
(1c) cob(III)alamin + reduced acceptor = cob(I)alamin + oxidized acceptor
Glossary: geneticin = G418 = (1R,2S,3S,4R,6S)-4,6-diamino-3-{[3-deoxy-4-C-methyl-3-(methylamino)-β-L-arabinopyranosyl]oxy}-2-hydroxycyclohexyl 2-amino-2,7-dideoxy-D-glycero-α-D-gluco-heptopyranoside
Other name(s): genK (gene name); gntK (gene name); gentamicin C-methyltransferase (ambiguous)
Systematic name: S-adenosyl-L-methionine:gentamicin X2 C6′-methyltransferase
Comments: The enzyme, isolated from the bacterium Micromonospora echinospora, has a single [4Fe-4S] cluster per monomer. It is a radical S-adenosyl-L-methionine (SAM) enzyme with a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5′-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. It catalyses methylation of the 6′-carbon of gentamicin X2 (GenX2) to produce genetricin (G418) during the biosynthesis of gentamicins. The 6′-pro-R-hydrogen atom of GenX2 is stereoselectively abstracted by the 5′-deoxyadenosyl radical and methylation occurs with retention of configuration at C6′. The regeneration of cob(I)alamin from cob(III)alamin is carried out with an as yet unidentified electron donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, J.Y., Suh, J.W., Kang, S.H., Phan, T.H., Park, S.H. and Kwon, H.J. Gene inactivation study of gntE reveals its role in the first step of pseudotrisaccharide modifications in gentamicin biosynthesis. Biochem. Biophys. Res. Commun. 372 (2008) 730–734. [DOI] [PMID: 18533111]
2.  Hong, W. and Yan, L. Identification of gntK, a gene required for the methylation of purpurosamine C-6′ in gentamicin biosynthesis. J. Gen. Appl. Microbiol. 58 (2012) 349–356. [DOI] [PMID: 23149679]
3.  Kim, H.J., McCarty, R.M., Ogasawara, Y., Liu, Y.N., Mansoorabadi, S.O., LeVieux, J. and Liu, H.W. GenK-catalyzed C-6′ methylation in the biosynthesis of gentamicin: isolation and characterization of a cobalamin-dependent radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 8093–8096. [DOI] [PMID: 23679096]
4.  Kim, H.J., Liu, Y.N., McCarty, R.M. and Liu, H.W. Reaction Catalyzed by GenK, a Cobalamin-Dependent Radical S-Adenosyl-l-methionine Methyltransferase in the Biosynthetic Pathway of Gentamicin, Proceeds with Retention of Configuration. J. Am. Chem. Soc. 139 (2017) 16084–16087. [DOI] [PMID: 29091410]
[EC 2.1.1.390 created 2023]
 
 
EC 2.1.3.2     
Accepted name: aspartate carbamoyltransferase
Reaction: carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
For diagram of pyrimidine biosynthesis, click here
Other name(s): carbamylaspartotranskinase; aspartate transcarbamylase; aspartate carbamyltransferase; aspartic acid transcarbamoylase; aspartic carbamyltransferase; aspartic transcarbamylase; carbamylaspartotranskinase; L-aspartate transcarbamoylase; L-aspartate transcarbamylase; carbamoylaspartotranskinase; aspartate transcarbamylase; aspartate transcarbamoylase; ATCase
Systematic name: carbamoyl-phosphate:L-aspartate carbamoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-49-1
References:
1.  Lowenstein, J.M. and Cohen, P.P. Studies on the biosynthesis of carbamylaspartic acid. J. Biol. Chem. 220 (1956) 57–70. [PMID: 13319326]
2.  Reichard, P. and Hanshoff, G. Aspartate carbamyl transferase from Escherichia coli. Acta Chem. Scand. 10 (1956) 548–566.
3.  Shepherson, M. and Pardee, A.B. Production and crystallization of aspartate transcarbamylase. J. Biol. Chem. 235 (1960) 3233–3237.
[EC 2.1.3.2 created 1961]
 
 
EC 2.2.1.1     
Accepted name: transketolase
Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
For diagram of reaction, click here, for diagram of the calvin cycle, click here, for diagram of the calvin cycle, click here, for diagram of the calvin cycle, click here and for diagram of the pentose phosphate pathway (later stages), click here
Glossary: thiamine diphosphate
Other name(s): glycolaldehydetransferase
Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glycolaldehydetransferase
Comments: A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-48-6
References:
1.  De La Haba, G., Leder, I.G and Racker, E. Crystalline transketolase from bakers' yeast: isolation and properties. J. Biol. Chem. 214 (1955) 409–426. [PMID: 14367398]
2.  Domagk, G.F. and Horecker, B.L. Fructose and erythrose metabolism in Alcaligenes faecalis. Arch. Biochem. Biophys. 109 (1965) 342–349.
3.  Horecker, B.L., Smyrniotis, P.Z. and Hurwitz, J. The role of xylulose 5-phosphate in the transketolase reaction. J. Biol. Chem. 223 (1956) 1009–1019. [PMID: 13385248]
4.  Racker, E. Transketolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 397–412.
[EC 2.2.1.1 created 1961]
 
 
EC 2.2.1.2     
Accepted name: transaldolase
Reaction: sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
For diagram of reaction, click here, of mechanism, click here and for diagram of the later stages of the pentose-phosphate pathway, click here
Other name(s): dihydroxyacetonetransferase; dihydroxyacetone synthase (incorrect); formaldehyde transketolase (incorrect)
Systematic name: sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-46-4
References:
1.  Horecker, B.L. and Smyrniotis, P.Z. Purification and properties of yeast transaldolase. J. Biol. Chem. 212 (1955) 811–825. [PMID: 14353883]
2.  Racker, E. Transaldolase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 5, Academic Press, New York, 1961, pp. 407–412.
3.  Tsolas, O. and Horecker, B.L. Transaldolase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 7, Academic Press, New York, 1972, pp. 259–280.
[EC 2.2.1.2 created 1961]
 
 
EC 2.2.1.4     
Accepted name: acetoin—ribose-5-phosphate transaldolase
Reaction: 3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde + 1-deoxy-D-altro-heptulose 7-phosphate
For diagram of reaction, click here
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): 1-deoxy-D-altro-heptulose-7-phosphate synthetase; 1-deoxy-D-altro-heptulose-7-phosphate synthase; 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase [wrong substrate name]
Systematic name: 3-hydroxybutan-2-one:D-ribose-5-phosphate aldehydetransferase
Comments: A thiamine-diphosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 87843-76-3
References:
1.  Yokota, A. and Sasajima, K. Enzymatic formation of a new monosaccharide, 1-deoxy-D-altro-heptulose phosphate, from DL-acetoin and D-ribose 5-phosphate by a transketolase mutant of Bacillus pumilus. Agric. Biol. Chem. 47 (1983) 1545–1553.
[EC 2.2.1.4 created 1989]
 
 
EC 2.2.1.10     
Accepted name: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Reaction: L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
For diagram of 3-dehydroquinate biosynthesis in archaea, click here
Glossary: 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate
Other name(s): ADH synthase; ADHS; MJ0400 (gene name)
Systematic name: L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase
Comments: The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  White, R.H. L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii. Biochemistry 43 (2004) 7618–7627. [DOI] [PMID: 15182204]
2.  Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36–41. [DOI] [PMID: 18318840]
3.  Morar, M., White, R.H. and Ealick, S.E. Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids. Biochemistry 46 (2007) 10562–10571. [DOI] [PMID: 17713928]
[EC 2.2.1.10 created 2012]
 
 
EC 2.2.1.14     
Accepted name: 6-deoxy-6-sulfo-D-fructose transaldolase
Reaction: 6-deoxy-6-sulfo-D-fructose + D-glyceraldehyde 3-phosphate = (2S)-3-sulfolactaldehyde + β-D-fructofuranose 6-phosphate
Glossary: (2S)-3-sulfolactaldehyde = (2S)-2-hydroxy-3-oxopropane-1-sulfonate
Other name(s): sftT (gene name)
Systematic name: 6-deoxy-6-sulfo-D-fructose:D-glyceraldehyde-3-phosphate glyceronetransferase
Comments: The enzyme, characterized from the bacterium Bacillus aryabhattai SOS1, is involved in a degradation pathway for 6-sulfo-D-quinovose. The enzyme can also use D-erythrose 4-phosphate as the acceptor, forming D-sedoheptulose 7-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Frommeyer, B., Fiedler, A.W., Oehler, S.R., Hanson, B.T., Loy, A., Franchini, P., Spiteller, D. and Schleheck, D. Environmental and intestinal phylum Firmicutes bacteria metabolize the plant sugar sulfoquinovose via a 6-deoxy-6-sulfofructose transaldolase pathway. iScience 23:101510 (2020). [DOI] [PMID: 32919372]
[EC 2.2.1.14 created 2021]
 
 
EC 2.3.1.26     
Accepted name: sterol O-acyltransferase
Reaction: a long-chain acyl-CoA + a sterol = CoA + a long-chain 3-hydroxysterol ester
Other name(s): cholesterol acyltransferase; sterol-ester synthase; acyl coenzyme A-cholesterol-O-acyltransferase; acyl-CoA:cholesterol acyltransferase; ACAT; acylcoenzyme A:cholesterol O-acyltransferase; cholesterol ester synthase; cholesterol ester synthetase; cholesteryl ester synthetase; SOAT1 (gene name); SOAT2 (gene name); ARE1 (gene name); ARE2 (gene name); acyl-CoA:cholesterol O-acyltransferase
Systematic name: long-chain acyl-CoA:sterol O-acyltransferase
Comments: The enzyme catalyses the formation of sterol esters from a sterol and long-chain fatty acyl-coenzyme A. The enzyme from yeast, but not from mammals, prefers monounsaturated acyl-CoA. In mammals the enzyme acts mainly on cholesterol and forms cholesterol esters that are stored in cytosolic droplets, which may serve to protect cells from the toxicity of free cholesterol. In macrophages, the accumulation of cytosolic droplets of cholesterol esters results in the formation of `foam cells’, a hallmark of early atherosclerotic lesions. In hepatocytes and enterocytes, cholesterol esters can be incorporated into apolipoprotein B-containing lipoproteins for secretion from the cell.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-63-8
References:
1.  Spector, A.A., Mathur, S.N. and Kaduce, T.L. Role of acylcoenzyme A: cholesterol O-acyltransferase in cholesterol metabolism. Prog. Lipid Res. 18 (1979) 31–53. [DOI] [PMID: 42927]
2.  Taketani, S., Nishino, T. and Katsuki, H. Characterization of sterol-ester synthetase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 575 (1979) 148–155. [DOI] [PMID: 389289]
3.  Lee, O., Chang, C.C., Lee, W. and Chang, T.Y. Immunodepletion experiments suggest that acyl-coenzyme A:cholesterol acyltransferase-1 (ACAT-1) protein plays a major catalytic role in adult human liver, adrenal gland, macrophages, and kidney, but not in intestines. J. Lipid Res. 39 (1998) 1722–1727. [PMID: 9717734]
4.  Yang, H., Cromley, D., Wang, H., Billheimer, J.T. and Sturley, S.L. Functional expression of a cDNA to human acyl-coenzyme A:cholesterol acyltransferase in yeast. Species-dependent substrate specificity and inhibitor sensitivity. J. Biol. Chem. 272 (1997) 3980–3985. [PMID: 9020103]
5.  Chang, C.C., Lee, C.Y., Chang, E.T., Cruz, J.C., Levesque, M.C. and Chang, T.Y. Recombinant acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) purified to essential homogeneity utilizes cholesterol in mixed micelles or in vesicles in a highly cooperative manner. J. Biol. Chem. 273 (1998) 35132–35141. [PMID: 9857049]
6.  Das, A., Davis, M.A. and Rudel, L.L. Identification of putative active site residues of ACAT enzymes. J. Lipid Res. 49 (2008) 1770–1781. [PMID: 18480028]
[EC 2.3.1.26 created 1972, modified 2019]
 
 
EC 2.3.1.78     
Accepted name: heparan-α-glucosaminide N-acetyltransferase
Reaction: acetyl-CoA + heparan sulfate α-D-glucosaminide = CoA + heparan sulfate N-acetyl-α-D-glucosaminide
Other name(s): acetyl-CoA:α-glucosaminide N-acetyltransferase
Systematic name: acetyl-CoA:heparan-α-D-glucosaminide N-acetyltransferase
Comments: Brings about the acetylation of glucosamine groups of heparan sulfate and heparin from which the sulfate has been removed. Also acts on heparin. Not identical with EC 2.3.1.3 glucosamine N-acetyltransferase or EC 2.3.1.4 glucosamine-phosphate N-acetyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79955-83-2
References:
1.  Klein, V., Kresse, H. and von Figura, K. Sanfilippo syndrome type C: deficiency of acetyl-CoA:α-glucosaminide N-acetyltransferase in skin fibroblasts. Proc. Natl. Acad. Sci. USA 75 (1978) 5185–5189. [DOI] [PMID: 33384]
2.  Pohlmann, R., Klein, U., Fromme, H.G. and von Figura, K. Localisation of acetyl-CoA: α-glucosaminide N-acetyltransferase in microsomes and lysosomes of rat liver. Hoppe-Seyler's Z. Physiol. Chem. 362 (1981) 1199–1207. [PMID: 7346380]
[EC 2.3.1.78 created 1984]
 
 
EC 2.3.1.89     
Accepted name: tetrahydrodipicolinate N-acetyltransferase
Reaction: acetyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + L-2-acetamido-6-oxoheptanedioate
Other name(s): tetrahydrodipicolinate acetylase; tetrahydrodipicolinate:acetyl-CoA acetyltransferase; acetyl-CoA:L-2,3,4,5-tetrahydrodipicolinate N2-acetyltransferase; acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate 2-N-acetyltransferase
Systematic name: acetyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N2-acetyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 83588-91-4
References:
1.  Chatterjee, S.P. and White, P.J. Activities and regulation of the enzymes of lysine biosynthesis in a lysine-excreting strain of Bacillus megaterium. J. Gen. Microbiol. 128 (1982) 1073–1081.
[EC 2.3.1.89 created 1986]
 
 
EC 2.3.1.101     
Accepted name: formylmethanofuran—tetrahydromethanopterin N-formyltransferase
Reaction: formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
For diagram of methane biosynthesis, click here
Glossary: methanofuran = 4-[4-(2-{[(4R*,5S*)-4,5,7-tricarboxyheptanoyl]-γ-L-glutamyl-γ-L-glutamylamino}ethyl)phenoxymethyl]furfurylamine
tetrahydromethanopterin = 1-(4-{(1R)-1-[(6S,7S)-2-amino-7-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]ethylamino}phenyl)-1-deoxy-5-O-{5-O-[(1S)-1,3-dicarboxypropylphosphonato]-α-D-ribofuranosyl}-D-ribitol
Other name(s): formylmethanofuran-tetrahydromethanopterin formyltransferase; formylmethanofuran:tetrahydromethanopterin formyltransferase; N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT) formyltransferase; FTR; formylmethanofuran:5,6,7,8-tetrahydromethanopterin N5-formyltransferase
Systematic name: formylmethanofuran:5,6,7,8-tetrahydromethanopterin 5-formyltransferase
Comments: Methanofuran is a complex 4-substituted furfurylamine and is involved in the formation of methane from CO2 in Methanobacterium thermoautotrophicum.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105669-83-8
References:
1.  Donnelly, M.I. and Wolfe, R.S. The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. J. Biol. Chem. 261 (1986) 16653–16659. [PMID: 3097011]
2.  Leigh, J.A., Rinehart, K.L. and Wolfe, R.S. Structure of methanofuran, the carbon-dioxide reduction factor of Methanobacterium thermoautotrophicum. J. Am. Chem. Soc. 106 (1984) 3636–3640.
[EC 2.3.1.101 created 1989]
 
 
EC 2.3.1.108     
Accepted name: α-tubulin N-acetyltransferase
Reaction: acetyl-CoA + [α-tubulin]-L-lysine = CoA + [α-tubulin]-N6-acetyl-L-lysine
Other name(s): ATAT1 (gene name); MEC17 (gene name); α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase (ambiguous); acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase
Systematic name: acetyl-CoA:[α-tubulin]-L-lysine N6-acetyltransferase
Comments: The enzyme is conserved from protists to mammals and is present in flowering plants. In most organisms it acetylates L-lysine at position 40 of α-tubulin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 99889-90-4
References:
1.  Greer, K., Maruta, H., L'Hernault, S.W. and Rosenbaum, J.L. α-Tubulin acetylase activity in isolated Chlamydomonas flagella. J. Cell Biol. 101 (1985) 2081–2084. [PMID: 4066751]
2.  Akella, J.S., Wloga, D., Kim, J., Starostina, N.G., Lyons-Abbott, S., Morrissette, N.S., Dougan, S.T., Kipreos, E.T. and Gaertig, J. MEC-17 is an α-tubulin acetyltransferase. Nature 467 (2010) 218–222. [DOI] [PMID: 20829795]
3.  Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. and Nachury, M.V. The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107 (2010) 21517–21522. [DOI] [PMID: 21068373]
4.  Taschner, M., Vetter, M. and Lorentzen, E. Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA. Proc. Natl. Acad. Sci. USA 109 (2012) 19649–19654. [DOI] [PMID: 23071318]
5.  Friedmann, D.R., Aguilar, A., Fan, J., Nachury, M.V. and Marmorstein, R. Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. Proc. Natl. Acad. Sci. USA 109 (2012) 19655–19660. [DOI] [PMID: 23071314]
6.  Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C. and Heppenstall, P.A. αTAT1 is the major α-tubulin acetyltransferase in mice. Nat. Commun. 4:1962 (2013). [DOI] [PMID: 23748901]
[EC 2.3.1.108 created 1989, modified 2021]
 
 
EC 2.3.1.117     
Accepted name: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
Reaction: succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate
Glossary: dipicolinate = pyridine-2,6-dicarboxylate
Other name(s): tetrahydropicolinate succinylase; tetrahydrodipicolinate N-succinyltransferase; tetrahydrodipicolinate succinyltransferase; succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase; succinyl-CoA:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
Systematic name: succinyl-CoA:(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
Comments: Involved in the biosynthesis of lysine in bacteria (including cyanobacteria) and higher plants. The 1992 edition of the Enzyme List erroneously gave the name 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase to this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 88086-34-4
References:
1.  Simms, S.A., Voige, W.H. and Gilvarg, C. Purification and characterization of succinyl-CoA: tetrahydrodipicolinate N-succinyltransferase from Escherichia coli. J. Biol. Chem. 259 (1984) 2734–2741. [PMID: 6365916]
[EC 2.3.1.117 created 1989, modified 2001]
 
 
EC 2.3.1.161     
Accepted name: lovastatin nonaketide synthase
Reaction: 9 malonyl-CoA + 11 NADPH + 10 H+ + S-adenosyl-L-methionine + holo-[lovastatin nonaketide synthase] = dihydromonacolin L-[lovastatin nonaketide synthase] + 9 CoA + 9 CO2 + 11 NADP+ + S-adenosyl-L-homocysteine + 6 H2O
For diagram of polyketides biosynthesis, click here
Glossary: dihydromonacolin L acid = (3R,5R)-7-[(1S,2S,4aR,6R,8aS)-2,6-dimethyl-1,2,4a,5,6,7,8,8a-octahydronaphthalen-1-yl]-3,5-dihydroxyheptanoate
Other name(s): LNKS; LovB; LovC; acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing, thioester-hydrolysing)
Systematic name: acyl-CoA:malonyl-CoA C-acyltransferase (dihydromonacolin L acid-forming)
Comments: This fungal enzyme system comprises a multi-functional polyketide synthase (PKS) and an enoyl reductase. The PKS catalyses many of the chain building reactions of EC 2.3.1.85, fatty-acid synthase system, as well as a reductive methylation and a Diels-Alder reaction, while the reductase is responsible for three enoyl reductions that are necessary for dihydromonacolin L acid production.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 235426-97-8
References:
1.  Ma, S.M., Li, J.W., Choi, J.W., Zhou, H., Lee, K.K., Moorthie, V.A., Xie, X., Kealey, J.T., Da Silva, N.A., Vederas, J.C. and Tang, Y. Complete reconstitution of a highly reducing iterative polyketide synthase. Science 326 (2009) 589–592. [DOI] [PMID: 19900898]
2.  Kennedy, J., Auclair, K., Kendrew, S.G., Park, C., Vederas, J.C. and Hutchinson, C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 284 (1999) 1368–1372. [DOI] [PMID: 10334994]
3.  Auclair, K., Sutherland, A., Kennedy, J., Witter, D.J., van der Heever, J.P., Hutchinson, C.R. and Vederas, J.C. Lovastatin nonaketide synthase catalyses an intramolecular Diels-Alder reaction of a substrate analogue. J. Am. Chem. Soc. 122 (2000) 11519–11520.
[EC 2.3.1.161 created 2002, modified 2015, modified 2016, modified 2019]
 
 
EC 2.3.1.207     
Accepted name: β-ketodecanoyl-[acyl-carrier-protein] synthase
Reaction: octanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
Glossary: [acyl-carrier protein] = [acp]
Systematic name: octanoyl-CoA:malonyl-[acyl-carrier protein] C-heptanoylltransferase (decarboxylating, CoA-forming)
Comments: This enzyme, which has been characterized from the bacterium Pseudomonas aeruginosa PAO1, catalyses the condensation of octanoyl-CoA, obtained from exogenously supplied fatty acids via β-oxidation, with malonyl-[acp], forming 3-oxodecanoyl-[acp], an intermediate of the fatty acid elongation cycle. The enzyme provides a shunt for β-oxidation degradation intermediates into de novo fatty acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yuan, Y., Leeds, J.A. and Meredith, T.C. Pseudomonas aeruginosa directly shunts β-oxidation degradation intermediates into de novo fatty acid biosynthesis. J. Bacteriol. 194 (2012) 5185–5196. [DOI] [PMID: 22753057]
[EC 2.3.1.207 created 2012]
 
 
EC 2.3.1.211     
Accepted name: bisdemethoxycurcumin synthase
Reaction: 2 4-coumaroyl-CoA + malonyl-CoA + H2O = 3 CoA + bisdemethoxycurcumin + 2 CO2
For diagram of curcumin biosynthesis, click here
Glossary: bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
Other name(s): CUS; curcuminoid synthase (ambiguous)
Systematic name: 4-coumaroyl-CoA:malonyl-CoA 4-coumaryltransferase (bisdemethoxycurcumin-forming)
Comments: A polyketide synthase characterized from the plant Oryza sativa (rice) that catalyses the formation of the C6-C7-C6 diarylheptanoid scaffold of bisdemethoxycurcumin. Unlike the process in the plant Curcuma longa (turmeric), where the conversion is carried out via a diketide intermediate by two different enzymes (EC 2.3.1.218, phenylpropanoylacetyl-CoA synthase and EC 2.3.1.217, curcumin synthase), the diketide intermediate formed by this enzyme remains within the enzyme’s cavity and is not released to the environment.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Morita, H., Wanibuchi, K., Nii, H., Kato, R., Sugio, S. and Abe, I. Structural basis for the one-pot formation of the diarylheptanoid scaffold by curcuminoid synthase from Oryza sativa. Proc. Natl. Acad. Sci. USA 107 (2010) 19778–19783. [DOI] [PMID: 21041675]
[EC 2.3.1.211 created 2013]
 
 
EC 2.3.1.217     
Accepted name: curcumin synthase
Reaction: feruloyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + curcumin + CO2
For diagram of curcumin biosynthesis, click here
Glossary: curcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
Other name(s): CURS; CURS1 (gene name); CURS2 (gene name); CURS3 (gene name)
Systematic name: feruloyl-CoA:feruloylacetyl-CoA feruloyltransferase (curcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate, CURS3 can accept 4-coumaroyl-CoA equally well [2] (see EC 2.3.1.219, demethoxycurcumin synthase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Katsuyama, Y., Kita, T., Funa, N. and Horinouchi, S. Curcuminoid biosynthesis by two type III polyketide synthases in the herb Curcuma longa. J. Biol. Chem. 284 (2009) 11160–11170. [DOI] [PMID: 19258320]
2.  Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [DOI] [PMID: 19622354]
3.  Katsuyama, Y., Miyazono, K., Tanokura, M., Ohnishi, Y. and Horinouchi, S. Structural and biochemical elucidation of mechanism for decarboxylative condensation of β-keto acid by curcumin synthase. J. Biol. Chem. 286 (2011) 6659–6668. [DOI] [PMID: 21148316]
[EC 2.3.1.217 created 2013]
 
 
EC 2.3.1.219     
Accepted name: demethoxycurcumin synthase
Reaction: (1) 4-coumaroyl-CoA + feruloylacetyl-CoA + H2O = 2 CoA + demethoxycurcumin + CO2
(2) 4-coumaroyl-CoA + (4-coumaroyl)acetyl-CoA + H2O = 2 CoA + bisdemethoxycurcumin + CO2
For diagram of curcumin biosynthesis, click here
Glossary: demethoxycurcumin = (1E,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
bisdemethoxycurcumin = (1E,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
feruloylacetyl-CoA = feruloyl-diketide-CoA
(4-coumaroyl)acetyl-CoA = 4-coumaroyl-diketide-CoA
Other name(s): CURS3
Systematic name: 4-coumaroyl-CoA:feruloylacetyl-CoA feruloyltransferase (demethoxycurcumin-forming)
Comments: A polyketide synthase from the plant Curcuma longa (turmeric). Three isoforms exist, CURS1, CURS2 and CURS3. While CURS1 and CURS2 prefer feruloyl-CoA as a starter substrate (cf. EC 2.3.1.217, curcumin synthase), CURS3 can accept 4-coumaroyl-CoA equally well [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Katsuyama, Y., Kita, T. and Horinouchi, S. Identification and characterization of multiple curcumin synthases from the herb Curcuma longa. FEBS Lett. 583 (2009) 2799–2803. [DOI] [PMID: 19622354]
[EC 2.3.1.219 created 2013]
 
 


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