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Literature summary for 2.1.1.249 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

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 dimethylamine:CoM methyl transfer mediating the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the trimethylamine corrinoid protein, MtbC, overview Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
-
gene mtbB
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
DMA:CoM methyltransferase
-
Methanosarcina barkeri
MtcB
-
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