EC Number |
Cofactor |
Reference |
---|
1.14.15.24 | cytochrome P450 |
the enzyme is a cytochrome P450 monooxygenase |
748597 |
1.14.15.24 | FAD |
- |
715432 |
1.14.15.24 | Ferredoxin |
reduced ferredoxin is required for activity |
716977 |
1.14.15.24 | Ferredoxin |
the hydroxylase is strictly dependent upon reduced ferredoxin which cannot be replaced by NADPH |
714293 |
1.14.15.24 | heme |
- |
714018 |
1.14.15.24 | more |
NADPH (1 mM) yields 2.5fold elevation in activity |
715432 |
1.14.15.24 | more |
NADPH is not required for activity |
716977 |
1.14.15.24 | more |
non-heme hydroxylase |
715012 |
1.14.15.24 | more |
the beta-carotene hydroxylase reaction proceeds in the absence of externally added cofactors. However, electron donors, such as NAD, NADPH, and ascorbate were able to stimulate the reaction |
714995 |
1.14.15.24 | more |
the monooxygenase cofactors consist of FAD, NADPH, and ATP. This cofactor combination increases the activity of CrtZ about 1.5fold compared to the control |
715432 |