Expasy logo

ENZYME

ENZYME entry: EC 2.1.1.379

Accepted Name
[methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
Alternative Name(s)
methanogenesis marker protein 10
Reaction catalysed
AH2 + L-arginyl-[methyl-coenzyme M reductase] + 2 S-adenosyl-L-methionine <=> (5S)-C-methyl-L-arginyl-[methyl-coenzyme M reductase] + 5'-deoxyadenosine + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Comment(s)
  • The enzyme, present in methanogenic archaea, catalyzes a modification of an L-arginine residue at the active site of EC 2.8.4.1, which catalyzes the last and methane-releasing step of methanogenesis.
  • The enzyme is a radical AdoMet (radical SAM) enzyme and contains an [4Fe-4S] cluster and a Coalpha-[alpha-(5-hydroxybenzimidazolyl)]- cobamide cofactor.
  • The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue.
Cross-references
BRENDA2.1.1.379
EC2PDB2.1.1.379
ExplorEnz2.1.1.379
PRIAM enzyme-specific profiles2.1.1.379
KEGG Ligand Database for Enzyme Nomenclature2.1.1.379
IUBMB Enzyme Nomenclature2.1.1.379
IntEnz2.1.1.379
MEDLINEFind literature relating to 2.1.1.379
MetaCyc2.1.1.379
Rhea expert-curated reactions2.1.1.379
UniProtKB/Swiss-Prot
Q8THG6, MCRAM_METACQ58251, MCRAM_METJA

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-