The Enzyme Database

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Accepted name: [methyl-Co(III) methylamine-specific corrinoid protein]—coenzyme M methyltransferase
Reaction: a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
Glossary: CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
Other name(s): methyltransferase 2 (ambiguous); MT2 (ambiguous); MT2-A; mtbA (gene name); [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
Systematic name: methylated monomethylamine-specific corrinoid protein:CoM methyltransferase
Comments: Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC, methylamine—corrinoid protein Co-methyltransferase, EC, dimethylamine—corrinoid protein Co-methyltransferase, and EC, trimethylamine—corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Burke, S.A. and Krzycki, J.A. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177 (1995) 4410–4416. [DOI] [PMID: 7635826]
2.  LeClerc, G.M. and Grahame, D.A. Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression. J. Biol. Chem. 271 (1996) 18725–18731. [DOI] [PMID: 8702528]
3.  Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [DOI] [PMID: 9006042]
4.  Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198]
5.  Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [DOI] [PMID: 10852929]
[EC created 2012]

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