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Literature summary for 1.14.14.1 extracted from
- Organization of NADPH-cytochrome P450 reductase and CYP1A2 in the endoplasmic reticulum - microdomain localization affects monooxygenase function (2011), Mol. Pharmacol., 79, 549-557.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Oryctolagus cuniculus | 5783 | - |
| microsome | - |
Oryctolagus cuniculus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | heme protein | Oryctolagus cuniculus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| CYP1A2 with NADPH-cytochrome P450 reductase preparation of endoplasmic reticulum membranes from microsomes, formation into lipid vesicles. the lipid composition of purified lipid vesicles affects CYP1A2 substrate metabolism and NADPH-cytochrome P450 reductase-CYP1A2 binding | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7-ethoxy-4-trifluoromethylcoumarin + [reduced NADPH-hemoprotein reductase] + O2 | CYP1A2 cooperates with NADPH-cytochrome P450 reductase, which provides NADPH for the reaction. Interaction with their redox partner, NADPH-cytochrome P450 reductase, i.e. CPR, in a 1:1 molar ratio | Oryctolagus cuniculus | 7-hydroxy-4-trifluoromethylcoumarin + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| 7-ethoxyresorufin + [reduced NADPH-hemoprotein reductase] + O2 | - |
Oryctolagus cuniculus | resorufin + ethanol + [oxidized NADPH-hemoprotein reductase] + H2O | - |
? | |
| additional information | CYP1A2 cooperates with NADPH-cytochrome P450 reductase, CPR. Differential sensitivity of CPR binding to CYP1A2 depending on the substrate present, overview | Oryctolagus cuniculus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYP1A2 | - |
Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Oryctolagus cuniculus | |
| NADPH | - |
Oryctolagus cuniculus | |
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Release 2023.1 (January 2023)
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