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Literature summary for 2.1.1.250 extracted from

  • Krzycki, J.
    Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases (2004), Curr. Opin. Chem. Biol., 8, 484-491.
    View publication on PubMed
Search for more literature for 2.1.1.250

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 1 * 50000 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
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 50000 Methanosarcina barkeri

Synonyms

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

General Information

General Information Comment Organism
metabolism biochemistry of methane formation by Methanosarcina species from monomethylamine, dimethylamine, and trimethylamine: methanogenesis from these substrates is initiated by three methyltransferases that specifically methylate their cognate corrinoid proteins with one of these methylamines, cf. EC 2.1.1.248 and EC 2.1.1.249, overview Methanosarcina barkeri
physiological function the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation Methanosarcina barkeri