×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

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 3VRM
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A single mutation at the ferredoxin binding site of p450 vdh enables efficient biocatalytic production of 25-hydroxyvitamin d3.
Yasutake, Y., Nishioka, T., Imoto, N., Tamura, T.
Chembiochem
CATH-Gene3D is a Global Biodata Core Resource Learn more...