EC Number   |
Cofactor |
Reference |
|---|
   1.14.14.133 | cytochrome P-450 |
- |
744316 |
| 1.14.14.133 | cytochrome P450 |
- |
746360 |
| 1.14.14.133 | FMN |
redox partner is cindoxin, containing FMN. Cindoxin might be different to other flavodoxins that interact with P450s, as both redox states of cindoxin could be catalytically relevant. Cindoxin supports regio- and stereoselective P450cin-catalysed cineole oxidation to (1R)-6beta-hydroxycineole with turnover rates up to 1500 per min |
717493 |
| 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 |
717774 |
| 1.14.14.133 | heme |
in the active site |
746360 |
| 1.14.14.133 | heme |
large spin state change of the heme iron associated with binding of cineole |
717765 |
| 1.14.14.133 | NADPH-hemoprotein reductase |
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._ |
744316, 746360 |
