CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.630 | Cytochrome p450 |
|
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
| Superfamily | Cytochrome P450 |
| Functional Family | Cytochrome P450 monooxygenase |
Enzyme Information
| 1.14.15.15 |
Cholestanetriol 26-monooxygenase.
based on mapping to UniProt C4B644
5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + 6 reduced adrenodoxin + 6 H(+) + 3 O(2) = (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta- cholestan-26-oate + 6 oxidized adrenodoxin + 4 H(2)O.
-!- Catalyzes the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. -!- Can also act on cholesterol, cholest-5-en-3-beta,7-alpha-diol, 7-alpha-hydroxycholest-4-en-3-one, and 5-beta-cholestane-3-alpha,7- alpha-diol. -!- The enzyme can also hydroxylate cholesterol at positions 24 and 25. -!- The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6. -!- Formerly EC 1.14.13.15.
|
UniProtKB Entries (1)
| C4B644 |
CPVDH_PSEAH
Pseudonocardia autotrophica
Vitamin D(3) 25-hydroxylase
|
PDB Structure
| PDB | 5GNM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural insights into the mechanism of the drastic changes in enzymatic activity of the cytochrome P450 vitamin D3 hydroxylase (CYP107BR1) caused by a mutation distant from the active site
Acta Crystallogr F Struct Biol Commun
|
