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
| 1.14.15.28 |
Cholest-4-en-3-one 26-monooxygenase ((25R)-3-oxocholest-4-en-26-oate forming).
based on mapping to UniProt P9WPL5
Cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O(2) = (25R)-3- oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H(2)O.
-!- This cytochrome P450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. -!- It catalyzes the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. -!- The products are exclusively in the (25R) conformation. -!- The enzyme also accepts cholesterol as a substrate. -!- cf. 1.14.15.29. -!- The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet. -!- Formerly EC 1.14.13.221.
|
UniProtKB Entries (1)
| P9WPL5 |
CP142_MYCTU
Mycobacterium tuberculosis H37Rv
Steroid C26-monooxygenase
|
PDB Structure
| PDB | 2XKR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and Biochemical Characterization of Mycobacterium Tuberculosis Cyp142: Evidence for Multiple Cholesterol 27-Hydroxylase Activities in a Human Pathogen.
J.Biol.Chem.
|
