| EC |
2.1.1.247 |
| Accepted name: |
[methyl-Co(III) methylamine-specific corrinoid protein]—coenzyme M methyltransferase |
| Reaction: |
a [methyl-Co(III) methylamine-specific corrinoid protein] + 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 2.1.1.248, methylamine—corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine—corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine—corrinoid protein Co-methyltransferase) to 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, PDB |
| References: |
| 1. |
Burke, S.A. and Krzycki, J.A. Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine. J. Bacteriol. 177 (1995) 4410–4416. [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] |
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| [EC 2.1.1.247 created 2012] |
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