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

BRENDA

EC2PDB

ExplorEnz

PRIAM enzyme-specific profiles

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

IntEnz

MEDLINE

MetaCyc

Rhea expert-curated reactions

UniProtKB/Swiss-Prot

B8Y445, RAMA_METBA

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