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Literature summary for 1.14.13.25 extracted from
- Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) (1985), Eur. J. Biochem., 147, 291-296.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | copper genetically regulates the enzyme activity of the soluble and membrane-bound form | Methylococcus capsulatus |  |
| Iron | characterization of [Fe2-S2] redox centre of component C | Methylococcus capsulatus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylococcus capsulatus | - |
Bath | - |
| Methylococcus capsulatus Bath | - |
Bath | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methane + NAD(P)H + O2 | - |
Methylococcus capsulatus | methanol + NAD(P)+ + H2O | - |
? | |
| methane + NAD(P)H + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD(P)+ + H2O | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | characterization of FAD redox centre of component C | Methylococcus capsulatus | |
| NADH | - |
Methylococcus capsulatus | |
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