Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + a [Co(II) dimethylamine-specific corrinoid protein] + reduced acceptor + H2O | Acetobacterium dehalogenans | - |
ADP + phosphate + a [Co(I) dimethylamine-specific corrinoid protein] + acceptor | - |
? | |
ATP + a [Co(II) methylamine-specific corrinoid protein] + reduced acceptor + H2O | Acetobacterium dehalogenans | - |
ADP + phosphate + a [Co(I) methylamine-specific corrinoid protein] + acceptor | - |
? | |
ATP + a [Co(II) trimethylamine-specific corrinoid protein] + reduced acceptor + H2O | Acetobacterium dehalogenans | - |
ADP + phosphate + a [Co(I) trimethylamine-specific corrinoid protein] + acceptor | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetobacterium dehalogenans | B8R2M5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + a [Co(II) dimethylamine-specific corrinoid protein] + reduced acceptor + H2O | - |
Acetobacterium dehalogenans | ADP + phosphate + a [Co(I) dimethylamine-specific corrinoid protein] + acceptor | - |
? | |
ATP + a [Co(II) methylamine-specific corrinoid protein] + reduced acceptor + H2O | - |
Acetobacterium dehalogenans | ADP + phosphate + a [Co(I) methylamine-specific corrinoid protein] + acceptor | - |
? | |
ATP + a [Co(II) trimethylamine-specific corrinoid protein] + reduced acceptor + H2O | - |
Acetobacterium dehalogenans | ADP + phosphate + a [Co(I) trimethylamine-specific corrinoid protein] + acceptor | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OdmC | - |
Acetobacterium dehalogenans |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme activates methyltrophic corrinoid proteins by reducing cobalt(II) back to cobalt(I). The transfer of electrons to the corrinoid as the electron-accepting site is achieved by increasing the potential of the corrinoid cofactor from -530 mV to -250 mV. The first 50 to 100 mV of the shift of the redox potential are caused by the interaction of nucleotide-bound enzyme with the corrinoid protein or its cofactor. The remaining 1500-200 mV have to be overcome by the chemical energy of ATP hydrolysis | Acetobacterium dehalogenans |