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Literature summary extracted from
- Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin (2007), J. Biol. Chem., 282, 27006-27011.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.133 | Citrobacter braakii | Q8VQF6 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.133 | 1,8-cineole + [reduced flavodoxin] + O2 | - |
Citrobacter braakii | (1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O | - |
? |  |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.133 | FMN | the FAD/FMN reductase consists of two separate polypeptides where the FMN protein, cindoxin, shuttles electrons between the FAD-containing cindoxin reductase and P450cin. Reaction is highly ionic strength-dependent. The fully reduced hydroquinone is the electron-donating species. Surface interactions are rather different from other P450 proteins | Citrobacter braakii | |
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Release 2023.1 (January 2023)
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