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 Cyp124 |
Enzyme Information
| 1.14.15.14 |
Methyl-branched lipid omega-hydroxylase.
based on mapping to UniProt P9WPP3
A methyl-branched lipid + O(2) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) = an omega-hydroxy-methyl-branched lipid + H(2)O + 2 oxidized ferredoxin [iron-sulfur] cluster.
-!- The enzyme, found in pathogenic and nonpathogenic mycobacteria species, actinomycetes, and some proteobacteria, hydroxylates the omega-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate.
|
| 1.14.15.28 |
Cholest-4-en-3-one 26-monooxygenase ((25R)-3-oxocholest-4-en-26-oate forming).
based on mapping to UniProt P9WPP3
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)
| P9WPP3 |
CP124_MYCTU
Mycobacterium tuberculosis H37Rv
Methyl-branched lipid omega-hydroxylase
|
PDB Structure
| PDB | 2WM5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Biochemical and structural characterization of CYP124: a methyl-branched lipid omega-hydroxylase from Mycobacterium tuberculosis.
Proc. Natl. Acad. Sci. U.S.A.
|