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Literature summary for 1.2.7.4 extracted from
- Substrate and cofactor reactivity of a carbon monoxide dehydrogenase-corrinoid enzyme complex: stepwise reduction of iron-sulfur and corrinoid centers, the corrinoid Co2+/1+ redox midpoint potential, and overall synthesis of acetyl-CoA (1993), Biochemistry, 32, 10786-10793.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme is part of a high molecular mass multienzyme complex that contains a corrinoid protein and carbon monoxide dehydrogenase and requires tetrahydrosarcinapterin as methyl group acceptor | Methanosarcina barkeri |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Methanosarcina barkeri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| tetrahydrosarcinapterin + acetyl-SCoA + H2O | carbon monoxide dehydrogenase-corrinoid enzyme complex, enzyme complex functions in synthesis of acetyl-CoA | Methanosarcina barkeri | methyltetrahydrosarcinapterin + CO2 + CoASH | - |
r |  |
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