|Gene:||mttB||Accession Numbers: G-9437 (MetaCyc), Mbar_A1502|
Species: Methanosarcina barkeri
Subunit composition of
trimethylamine--corrinoid protein Co-methyltransferase = [MttB]
trimethylamine methyltransferase mttB subunit = MttB
Reconstitution of trimethylamine-dependent coenzyme M (CoM) methylation showed that three polypeptides were involved - trimethylamine--corrinoid protein Co-methyltransferase, trimethylamine-specific corrinoid protein and methylated [methylamine-specific corrinoid protein]:coenzyme M methyltransferase.
The first two proteins, of sizes 52 and 26 kDa, respectively, copurified as a single trimethylamine methyltransferase (TMA-MT). Gel permeation of the TMA-MT fraction demonstrated that the 52- kDa polypeptide eluted with an apparent molecular mass of 280 kDa. The 26-kDa protein eluted primarily as a monomer, but some 26-kDa polypeptides also eluted with the 280-kDa peak, indicating that the two proteins weakly associate [Ferguson97].
Molecular Weight of Polypeptide: 53.855 kD (from nucleotide sequence)
Enzymatic reaction of: trimethylamine methyltransferase (trimethylamine--corrinoid protein Co-methyltransferase)
EC Number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
Ferguson97: Ferguson DJ, Krzycki JA (1997). "Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri." J Bacteriol 179(3);846-52. PMID: 9006042
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