| Accepted Name |
|---|
| [Co(II) methylated amine-specific corrinoid protein] reductase
|
| Reaction catalysed |
|---|
- 2 Co(II)-[methylamine-specific corrinoid protein] + AH2 + ATP + H2O = 2 Co(I)-[methylamine-specific corrinoid protein] + A + ADP + phosphate + 3 H(+)
- 2 Co(II)-[dimethylamine-specific corrinoid protein] + AH2 + ATP + H2O = 2 Co(I)-[dimethylamine-specific corrinoid protein] + A + ADP + phosphate + 3 H(+)
- 2 Co(II)-[trimethylamine-specific corrinoid protein] + AH2 + ATP + H2O = 2 Co(I)-[trimethylamine-specific corrinoid protein] + A + ADP + phosphate + 3 H(+)
|
| 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 | 1.16.99.1 |
| EC2PDB | 1.16.99.1 |
| ExplorEnz | 1.16.99.1 |
| PRIAM enzyme-specific profiles | 1.16.99.1 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.16.99.1 |
| IUBMB Enzyme Nomenclature | 1.16.99.1 |
| IntEnz | 1.16.99.1 |
| MEDLINE | Find literature relating to 1.16.99.1 |
| MetaCyc | 1.16.99.1 |
| Rhea expert-curated reactions | 1.16.99.1 |
| UniProtKB/Swiss-Prot | B8Y445, RAMA_METBA
|