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MetaCyc Enzyme: trimethylamine--corrinoid protein Co-methyltransferase

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

Summary:
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)

Unification Links: Entrez-gene:3627689 , UniProt:O93658

Relationship Links: Entrez-Nucleotide:RELATED-TO:AF102623 , InterPro:IN-FAMILY:IPR010426 , InterPro:IN-FAMILY:IPR012740 , Pfam:IN-FAMILY:PF06253

Gene-Reaction Schematic: ?

Gene-Reaction Schematic


Enzymatic reaction of: trimethylamine methyltransferase (trimethylamine--corrinoid protein Co-methyltransferase)

EC Number: 2.1.1.250

trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] + H+ <=> a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine

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.

In Pathways: superpathway of methanogenesis , methanogenesis from trimethylamine


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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