Entry |
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Name |
cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming];
CYP142
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Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
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Sysname |
cholest-4-en-3-one,reduced [2Fe-2S] ferredoxin:oxygen oxidoreductase [(25R)-3-oxocholest-4-en-26-oate forming]
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Reaction(IUBMB) |
cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O2 = (25R)-3-oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O (overall reaction) [RN: R11361];
(1a) cholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-hydroxycholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + H2O [RN: R11358];
(1b) (25R)-26-hydroxycholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-26-oxocholest-4-en-3-one + 2 oxidized [2Fe-2S] ferredoxin + 2 H2O [RN: R11359];
(1c) (25R)-26-oxocholest-4-en-3-one + 2 reduced [2Fe-2S] ferredoxin + O2 = (25R)-3-oxocholest-4-en-26-oate + 2 oxidized [2Fe-2S] ferredoxin + H2O [RN: R11360]
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Reaction(KEGG) |
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Substrate |
cholest-4-en-3-one [CPD: C00599];
reduced [2Fe-2S] ferredoxin [CPD: C22150];
O2 [CPD: C00007];
(25R)-26-hydroxycholest-4-en-3-one [CPD: C21303];
(25R)-26-oxocholest-4-en-3-one [CPD: C21305]
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Product |
(25R)-3-oxocholest-4-en-26-oate [CPD: C20839];
oxidized [2Fe-2S] ferredoxin [CPD: C22151];
H2O [CPD: C00001];
(25R)-26-hydroxycholest-4-en-3-one [CPD: C21303];
(25R)-26-oxocholest-4-en-3-one [CPD: C21305]
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Comment |
This cytochrome P-450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol. It catalyses 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 1.14.15.29, cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]. The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
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History |
EC 1.14.15.28 created 2016 as EC 1.14.13.221, transferred 2018 to EC 1.14.15.28
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Pathway |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K16046 | cholest-4-en-3-one 26-monooxygenase |
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Genes |
» show all
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Reference |
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Authors |
Driscoll MD, McLean KJ, Levy C, Mast N, Pikuleva IA, Lafite P, Rigby SE, Leys D, Munro AW |
Title |
Structural and biochemical characterization of Mycobacterium tuberculosis CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen. |
Journal |
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Sequence |
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Reference |
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Authors |
Johnston JB, Ouellet H, Ortiz de Montellano PR |
Title |
Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses. |
Journal |
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Sequence |
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Other DBs |
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