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Literature summary for 1.14.15.6 extracted from
- Kinetic and optical biosensor study of adrenodoxin mutant AdxS112W displaying an enhanced interaction towards the cholesterol side chain cleavage enzyme (CYP11A1) (2011), Eur. Biophys. J., 40, 1275-1282.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cholesterol + 6 reduced adrenodoxin + 3 O2 | Homo sapiens | overall reaction | pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cholesterol + 6 reduced adrenodoxin + 3 O2 | overall reaction | Homo sapiens | pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O | - |
? | |
| cholesterol + 6 reduced adrenodoxin mutant S112W + 3 O2 | overall reaction, adrenodoxin mutant S112W gives a 14fold higher catalytic efficiency compared to wild-type adrenodoxin | Homo sapiens | pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin mutant S112W + 4 H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cholesterol side chain cleavage enzyme | - |
Homo sapiens |
| CYP11A1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.3 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| adrenodoxin | i.e. Adx , mechanism of the redox partner interactions, role of adrenodoxin electrostatic contributions, overview. Contruction of an Adx mutant lacking the C-terminal amino acids 113-128 and bearing a S112W point mutation, the mutant shows increased effciency towards CYP11A1-dependent cholesterol conversion. The complex between AdxS112W and CYP11A1 is about 4fold stronger than the respective complex with wild-type Adx, stopped flow kinetics, overview | Homo sapiens | |
| cytochrome P450 | - |
Homo sapiens |
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