EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.14.14.133 | 1,8-cineole + [reduced flavodoxin] + O2 |
- |
Citrobacter braakii |
(1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O |
- |
? |
1.14.14.133 | 1,8-cineole + [reduced flavodoxin] + O2 |
- |
Citrobacter braakii |
(1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O |
single product |
? |
1.14.14.133 | 1,8-cineole + [reduced flavodoxin] + O2 |
enzyme displays a high affinity for cineole 1 with KD 0.7 microM, and a large spin state change of the heme iron associated with binding of cineole |
Citrobacter braakii |
(1R)-6beta-hydroxycineole + [oxidized flavodoxin] + H2O |
- |
? |
1.14.14.133 | 1,8-cineole + [reduced flavodoxin] + O2 |
- |
Citrobacter braakii |
6beta-hydroxycineole + [oxidized flavodoxin] + H2O |
- |
? |
1.14.14.133 | 1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2 |
- |
Citrobacter braakii |
2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O |
- |
? |
1.14.14.133 | 2,2-dimethylbicyclo[2.2.2]octane + [reduced flavodoxin] + O2 |
i.e. cinane |
Citrobacter braakii |
? + [oxidized flavodoxin] + H2O |
identification of least seven oxidised derivatives |
? |
1.14.14.133 | camphane + [reduced flavodoxin] + O2 |
- |
Citrobacter braakii |
camphor + [oxidized flavodoxin] + H2O |
main product in presence of excess NADPH, plus epi-camphor at a rate of 3:1, and several minor products |
? |
1.14.14.133 | more |
a hydroxyl group on the substrate is vital, and in its absence catalytic turnover is effectively abolished. In the absence of the ethereal oxygen there is still a significant amount of coupling of the NADPH-reducing equivalents to the formation of oxidised product. The substrate itself is not important in controlling oxygen activation, but is essential for regio- and stereoselective substrate oxidation |
Citrobacter braakii |
? |
- |
? |
1.14.14.133 | more |
P450cin catalyzes the stereoselective hydoxylation of 1,8-cineole to 2beta-hydroxy-1,8-cineole. The two electrons necessary for the conversion of 1,8-cineole to 2beta-hydroxy-1,8-cineole are supplied by NADPH and transferred via a FAD-containing cindoxin reductase (CinB), and an FMN-containing cindoxin (CinC) to the heme iron in the active site of P450cin (CinA). The flow of electrons in this multicomponent P450cin system is from NADPH to Fpr via CinC to CinA |
Citrobacter braakii |
? |
- |
? |