The Enzyme Database

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EC 2.1.1.25     
Accepted name: phenol O-methyltransferase
Reaction: S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole
Other name(s): PMT
Systematic name: S-adenosyl-L-methionine:phenol O-methyltransferase
Comments: Acts on a wide variety of simple alkyl-, methoxy- and halo-phenols.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37256-94-3
References:
1.  Axelrod, J. and Daly, J. Phenol-O-methyltransferase. Biochim. Biophys. Acta 159 (1968) 472–478. [DOI] [PMID: 5657870]
[EC 2.1.1.25 created 1972]
 
 
EC 2.1.1.250     
Accepted name: trimethylamine—corrinoid protein Co-methyltransferase
Reaction: trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Other name(s): mttB (gene name); trimethylamine methyltransferase
Systematic name: trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [DOI] [PMID: 9006042]
2.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490]
[EC 2.1.1.250 created 2012]
 
 
EC 2.1.1.251     
Accepted name: methylated-thiol—coenzyme M methyltransferase
Reaction: methanethiol + CoM = methyl-CoM + hydrogen sulfide (overall reaction)
(1a) methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
(1b) a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
Glossary: CoM = coenzyme M = 2-mercaptoethanesulfonate
Other name(s): mtsA (gene name)
Systematic name: methylated-thiol:CoM methyltransferase
Comments: The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-S-methylmercaptopropionate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to CoM. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol—corrinoid protein Co-methyltransferase, and EC 2.1.1.246, methylated methanol-specific corrinoid protein:coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Paul, L. and Krzycki, J.A. Sequence and transcript analysis of a novel Methanosarcina barkeri methyltransferase II homolog and its associated corrinoid protein homologous to methionine synthase. J. Bacteriol. 178 (1996) 6599–6607. [DOI] [PMID: 8932317]
2.  Tallant, T.C. and Krzycki, J.A. Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate. J. Bacteriol. 179 (1997) 6902–6911. [DOI] [PMID: 9371433]
3.  Tallant, T.C., Paul, L. and Krzycki, J.A. The MtsA subunit of the methylthiol:coenzyme M methyltransferase of Methanosarcina barkeri catalyses both half-reactions of corrinoid-dependent dimethylsulfide: coenzyme M methyl transfer. J. Biol. Chem. 276 (2001) 4485–4493. [DOI] [PMID: 11073950]
[EC 2.1.1.251 created 2012]
 
 
EC 2.1.1.252     
Accepted name: tetramethylammonium—corrinoid protein Co-methyltransferase
Reaction: tetramethylammonium + a [Co(I) tetramethylammonium-specific corrinoid protein] = a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + trimethylamine
Other name(s): mtqB (gene name); tetramethylammonium methyltransferase
Systematic name: tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435]
[EC 2.1.1.252 created 2012]
 
 
EC 2.1.1.253     
Accepted name: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase
Reaction: a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) tetramethylammonium-specific corrinoid protein]
Glossary: CoM = coenzyme M = 2-mercaptoethanesulfonate
Other name(s): methyltransferase 2 (ambiguous); mtqA (gene name)
Systematic name: methylated tetramethylammonium-specific corrinoid protein:CoM methyltransferase
Comments: The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium—corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Asakawa, S., Sauer, K., Liesack, W. and Thauer, R.K. Tetramethylammonium:coenzyme M methyltransferase system from methanococcoides s. Arch. Microbiol. 170 (1998) 220–226. [PMID: 9732435]
[EC 2.1.1.253 created 2012]
 
 
EC 2.1.1.254     
Accepted name: erythromycin 3′′-O-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + erythromycin C = S-adenosyl-L-homocysteine + erythromycin A
(2) S-adenosyl-L-methionine + erythromycin D = S-adenosyl-L-homocysteine + erythromycin B
For diagram of erythromycin biosynthesis, click here
Other name(s): EryG
Systematic name: S-adenosyl-L-methionine:erythromycin C 3′′-O-methyltransferase
Comments: The enzyme methylates the 3 position of the mycarosyl moiety of erythromycin C, forming the most active form of the antibiotic, erythromycin A. It can also methylate the precursor erythromycin D, forming erythromycin B, which is then converted to erythromycin A by EC 1.14.13.154, erythromycin 12 hydroxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Paulus, T.J., Tuan, J.S., Luebke, V.E., Maine, G.T., DeWitt, J.P. and Katz, L. Mutation and cloning of eryG, the structural gene for erythromycin O-methyltransferase from Saccharopolyspora erythraea, and expression of eryG in Escherichia coli. J. Bacteriol. 172 (1990) 2541–2546. [DOI] [PMID: 2185226]
2.  Summers, R.G., Donadio, S., Staver, M.J., Wendt-Pienkowski, E., Hutchinson, C.R. and Katz, L. Sequencing and mutagenesis of genes from the erythromycin biosynthetic gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose and D-desosamine production. Microbiology 143 (1997) 3251–3262. [DOI] [PMID: 9353926]
[EC 2.1.1.254 created 2012]
 
 
EC 2.1.1.255     
Accepted name: geranyl diphosphate 2-C-methyltransferase
Reaction: S-adenosyl-L-methionine + geranyl diphosphate = S-adenosyl-L-homocysteine + (E)-2-methylgeranyl diphosphate
For diagram of reaction, click here
Other name(s): SCO7701; GPP methyltransferase; GPPMT; 2-methyl-GPP synthase; MGPPS; geranyl pyrophosphate methyltransferase
Systematic name: S-adenosyl-L-methionine:geranyl-diphosphate 2-C-methyltransferase
Comments: This enzyme, along with EC 4.2.3.118, 2-methylisoborneol synthase, produces 2-methylisoborneol, an odiferous compound produced by soil microorganisms with a strong earthy/musty odour.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wang, C.M. and Cane, D.E. Biochemistry and molecular genetics of the biosynthesis of the earthy odorant methylisoborneol in Streptomyces coelicolor. J. Am. Chem. Soc. 130 (2008) 8908–8909. [DOI] [PMID: 18563898]
2.  Ariyawutthiphan, O., Ose, T., Tsuda, M., Gao, Y., Yao, M., Minami, A., Oikawa, H. and Tanaka, I. Crystallization and preliminary X-ray crystallographic study of a methyltransferase involved in 2-methylisoborneol biosynthesis in Streptomyces lasaliensis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 417–420. [DOI] [PMID: 21393856]
3.  Komatsu, M., Tsuda, M., Omura, S., Oikawa, H. and Ikeda, H. Identification and functional analysis of genes controlling biosynthesis of 2-methylisoborneol. Proc. Natl. Acad. Sci. USA 105 (2008) 7422–7427. [DOI] [PMID: 18492804]
4.  Giglio, S., Chou, W.K., Ikeda, H., Cane, D.E. and Monis, P.T. Biosynthesis of 2-methylisoborneol in cyanobacteria. Environ. Sci. Technol. 45 (2011) 992–998. [DOI] [PMID: 21174459]
[EC 2.1.1.255 created 2012]
 
 
EC 2.1.1.256     
Accepted name: tRNA (guanine6-N2)-methyltransferase
Reaction: S-adenosyl-L-methionine + guanine6 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine6 in tRNA
Other name(s): methyltransferase Trm14; m2G6 methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (guanine6-N2)-methyltransferase
Comments: The enzyme specifically methylates guanine6 at N2 in tRNA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Menezes, S., Gaston, K.W., Krivos, K.L., Apolinario, E.E., Reich, N.O., Sowers, K.R., Limbach, P.A. and Perona, J.J. Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14. Nucleic Acids Res. 39 (2011) 7641–7655. [DOI] [PMID: 21693558]
[EC 2.1.1.256 created 2012]
 
 
EC 2.1.1.257     
Accepted name: tRNA (pseudouridine54-N1)-methyltransferase
Reaction: S-adenosyl-L-methionine + pseudouridine54 in tRNA = S-adenosyl-L-homocysteine + N1-methylpseudouridine54 in tRNA
Other name(s): TrmY; m1Ψ methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA (pseudouridine54-N1)-methyltransferase
Comments: While this archaeal enzyme is specific for the 54 position and does not methylate pseudouridine at position 55, the presence of pseudouridine at position 55 is necessary for the efficient methylation of pseudouridine at position 54 [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, H.Y. and Yuan, Y.A. Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J. Mol. Cell. Biol. 2 (2010) 366–374. [DOI] [PMID: 21098051]
2.  Wurm, J.P., Griese, M., Bahr, U., Held, M., Heckel, A., Karas, M., Soppa, J. and Wohnert, J. Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs. RNA 18 (2012) 412–420. [DOI] [PMID: 22274954]
3.  Chatterjee, K., Blaby, I.K., Thiaville, P.C., Majumder, M., Grosjean, H., Yuan, Y.A., Gupta, R. and de Crecy-Lagard, V. The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together with pseudouridine synthase Pus10, catalyze the formation of 1-methylpseudouridine at position 54 of tRNA. RNA 18 (2012) 421–433. [DOI] [PMID: 22274953]
[EC 2.1.1.257 created 2012]
 
 
EC 2.1.1.258     
Accepted name: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase
Reaction: a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
Other name(s): acsE (gene name)
Systematic name: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
Comments: Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Roberts, D.L., Zhao, S., Doukov, T. and Ragsdale, S.W. The reductive acetyl coenzyme A pathway: sequence and heterologous expression of active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum. J. Bacteriol. 176 (1994) 6127–6130. [DOI] [PMID: 7928975]
2.  Doukov, T., Seravalli, J., Stezowski, J.J. and Ragsdale, S.W. Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase. Structure 8 (2000) 817–830. [DOI] [PMID: 10997901]
3.  Doukov, T.I., Hemmi, H., Drennan, C.L. and Ragsdale, S.W. Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. J. Biol. Chem. 282 (2007) 6609–6618. [DOI] [PMID: 17172470]
[EC 2.1.1.258 created 2012]
 
 
EC 2.1.1.259     
Accepted name: [fructose-bisphosphate aldolase]-lysine N-methyltransferase
Reaction: 3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Other name(s): rubisco methyltransferase; ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase; ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit εN-methyltransferase; S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine 6-N-methyltransferase
Systematic name: S-adenosyl-L-methionine:[fructose-bisphosphate aldolase]-lysine N6-methyltransferase
Comments: The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13). The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39) [2], but that from Arabidopsis thaliana does not.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Magnani, R., Nayak, N.R., Mazarei, M., Dirk, L.M. and Houtz, R.L. Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase. J. Biol. Chem. 282 (2007) 27857–27864. [DOI] [PMID: 17635932]
2.  Mininno, M., Brugiere, S., Pautre, V., Gilgen, A., Ma, S., Ferro, M., Tardif, M., Alban, C. and Ravanel, S. Characterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plants. J. Biol. Chem. 287 (2012) 21034–21044. [DOI] [PMID: 22547063]
[EC 2.1.1.259 created 2012]
 
 


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