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ENZYME entry: EC 1.16.99.1

Accepted Name
[Co(II) methylated amine-specific corrinoid protein] reductase.
Reaction catalysed
  • AH2 + ATP + 2 Co(II)-[methylamine-specific corrinoid protein] + H2O <=> A + ADP + 2 Co(I)-[methylamine-specific corrinoid protein] + 3 H(+) + phosphate
  • AH2 + ATP + 2 Co(II)-[dimethylamine-specific corrinoid protein] + H2O <=> A + ADP + 2 Co(I)-[dimethylamine-specific corrinoid protein] + 3 H(+) + phosphate
  • AH2 + ATP + 2 Co(II)-[trimethylamine-specific corrinoid protein] + H2O <=> A + ADP + 2 Co(I)-[trimethylamine-specific corrinoid protein] + 3 H(+) + phosphate
Comment(s)
  • Methyltrophic corrinoid proteins must have the cobalt atom in the active cobalt(I) state to become methylated.
  • Because the cobalt(I)/cobalt(II) transformation has a very low redox potential the corrinoid cofactor is subject to adventitious oxidation to the cobalt(II) state, which renders the proteins inactive.
  • This enzyme, characterized from the methanogenic archaeon Methanosarcina barkeri, reduces cobalt(II) back to cobalt(I), restoring activity.
  • The enzyme acts on the corrinoid proteins involved in methanogenesis from methylamine, dimethylamine, and trimethylamine, namely MtmC, MtbC, and MttC, respectively.
  • While in vitro the enzyme can use Ti(III)-citrate as the electron donor, the in vivo donor is not known.
  • The enzyme from Methanosarcina barkeri contains a C-terminal [4Fe-4S] ferredoxin-like domain.
Cross-references
BRENDA1.16.99.1
EC2PDB1.16.99.1
ExplorEnz1.16.99.1
PRIAM enzyme-specific profiles1.16.99.1
KEGG Ligand Database for Enzyme Nomenclature1.16.99.1
IUBMB Enzyme Nomenclature1.16.99.1
IntEnz1.16.99.1
MEDLINEFind literature relating to 1.16.99.1
MetaCyc1.16.99.1
Rhea expert-curated reactions1.16.99.1

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