Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.250 extracted from

  • Ferguson, T.; Soares, J.; Lienard, T.; Gottschalk, G.; Krzycki, J.
    RamA, a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea (2009), J. Biol. Chem., 284, 2285-2295.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.250

Activating Compound

Activating Compound Comment Organism Structure
RamA a 60-kDa monomeric iron sulfur protein, is a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea, it is required for in vitro ATP-dependent reductive activation of trimethylamine:CoM methyl transfer mediating the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the trimethylamine corrinoid protein, MttC, overview Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trimethylamine + a [Co(I) methylamine-specific corrinoid protein] Methanosarcina barkeri
-
 a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri O93658 gene mttB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine + a [Co(I) methylamine-specific corrinoid protein]
-
 Methanosarcina barkeri a [methyl-Co(III) methylamine-specific corrinoid protein] + dimethylamine
-
 ?

Synonyms

Synonyms Comment Organism
MttB
-
 Methanosarcina barkeri
TMA:CoM methyltransferase
-
 Methanosarcina barkeri

General Information

General Information Comment Organism
metabolism archaeal methane formation from methylamines is initiated by distinct methyltransferases with specificity for monomethylamine, dimethylamine, or trimethylamine. Each methylamine methyltransferase methylates a cognate corrinoid protein, which is subsequently demethylated by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor Methanosarcina barkeri