EC Number   |
General Information |
Reference |
|---|
    1.14.14.1 | metabolism |
cytochrome P450-dependent metabolism of omega-6 polyunsaturated fatty acids, overview |
710821 |
| 1.14.14.1 | metabolism |
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification by Cyp3A enzymes. The okadaic acid toxicity is enhanced in the presence of rat CYP1A2 |
744184 |
| 1.14.14.1 | metabolism |
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification by Cyp3A enzymes. The rate of detoxification by rat Cyp3a1 is lower compared to human CYP3A enzymes |
744184 |
| 1.14.14.1 | metabolism |
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification which is mainly catalyzed by human CYP3A4 and CYP3A5. Human isoform CYP1A2 seems to activate okadaic acid into cytotoxic intermediates |
744184 |
| 1.14.14.1 | metabolism |
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification which is mainly catalyzed by human CYP3A4 and CYP3A5. The coincubation of okadaic acid with human CYP3A4 results in an increase in HepG2 cell viability. Human isoform CYP1A2 seems to activate okadaic acid into cytotoxic intermediates |
744184 |
| 1.14.14.1 | metabolism |
metabolism of okadaic acid to oxygenated metabolites correlates with detoxification which is mainly catalyzed by human CYP3A4 and CYP3A5. The okadaic acid toxicity is enhanced in the presence of human CYP1A2 |
744184 |
| 1.14.14.1 | metabolism |
upon binding NADPH-cytochrome P450 oxidoreductase CPR, the interaction between CYP1A1 and the membrane becomes weaker, as the CYP1A1-FMN domain interface area increases. The CYP1A1 catalytic domain reorients in the membrane. This reorientation affects ligand access and egress pathways between the active site and the membrane. CPR rearranges in the membrane and undergoes a large conformational change from the open to the semi-open form, which enables the formation of an additional interface between the distal side of CYP1A1 and the CPR NADP domain |
764521 |
| 1.14.14.1 | more |
loss of CYP3A4 activity may result in increased risk of drug toxicities and adverse drug reactions in patients with NADPH-P450 reductase mutations |
711114 |
| 1.14.14.1 | more |
multifunctional properties of versatile P450s from the basidiomycete |
711544 |
| 1.14.14.1 | physiological function |
chimeric P450cam-RhFRed reductase domain enzyme shows improved biotransformation of 80% conversion at 30 mM substrate concentration |
703178 |
