CATH Classification

Domain Context

CATH Clusters

Superfamily Cytochrome P450
Functional Family Cytochrome P450 monooxygenase PikC

Enzyme Information

1.14.13.221
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 + 3 NADPH + 3 O(2) = (25R)-3-oxocholest-4-en-26-oate + 3 NADP(+) + 4 H(2)O.
-!- This 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. EC 1.14.13.141. -!- The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
1.14.-.-
Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O(2).
based on mapping to UniProt P9WPP3
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.

UniProtKB Entries (1)

P9WPP3
CP124_MYCTU
Mycobacterium tuberculosis H37Rv
Methyl-branched lipid omega-hydroxylase

PDB Structure

PDB 2WM4
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Biochemical and structural characterization of CYP124: a methyl-branched lipid omega-hydroxylase from Mycobacterium tuberculosis.
Johnston, J.B., Kells, P.M., Podust, L.M., Ortiz de Montellano, P.R.
Proc. Natl. Acad. Sci. U.S.A.