EC - [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
Other names:
methyltransferase 2 [ambiguous]
MT2 [ambiguous]
mtbA (gene name)
Systematic name:
methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase




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 coenzyme M, forming the substrate for EC, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0043833


  1. Burke, S. A., Krzycki, J. A.
    Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine.
    J. Bacteriol. 177 : 4410-4416 (1995). [PMID: 7635826]
  2. LeClerc, G. M., Grahame, D. A.
    Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression.
    J. Biol. Chem. 271 : 18725-18731 (1996). [PMID: 8702528]
  3. Ferguson, D. J., 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 : 846-852 (1997). [PMID: 9006042]
  4. Burke, S. A., Lo, S. L., Krzycki, J. A.
    Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine.
    J. Bacteriol. 180 : 3432-3440 (1998). [PMID: 9642198]
  5. Ferguson, D. J., Gorlatova, N., Grahame, D. A., 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 : 29053-29060 (2000). [PMID: 10852929]

[EC created 2012]