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Information on EC 1.14.15.29 - cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]
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1.14.15.29 cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein found in several bacterial pathogens. The enzyme is involved in degradation of the host's 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 (25S) configuration. The enzyme is part of a two-component system that also includes a ferredoxin reductase (most likely KshB, which also interacts with EC 1.14.15.30, 3-ketosteroid 9alpha-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.15.28, cholest-4-en-3-one 27-monooxygenase.
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Word Map
- 1.14.15.29
- tuberculosis
- mycobacterium
- cholesterol
- sterol
- heme
- azole
-
high-spin
-
low-spin
-
antitubercular
- ferredoxins
-
methyl-branched
- 4-cholesten-3-one
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
3
+
3
+
3
=
+
3
+
4
Synonyms
cyp125, cyp125a1, cyp125a3, steroid c26-monooxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cholest-4-en-3-one 26-monooxygenase
-
-
-
-
CYP125
CYP125A1
CYP125A3
CYP125A4
cytochrome P450 125
EC 1.14.13.141
-
-
formerly
-
Rv3545c
steroid C26-monooxygenase
CYP125
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
-
cytochrome P450 125
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
-
Rv3545c
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(25S)-26-hydroxycholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = (25S)-26-oxocholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
(1b)
-
-
-
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = (25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1a)
-
-
-
cholest-4-en-3-one + 3 NADH + 3 H+ + 3 O2 = (25S)-3-oxocholest-4-en-26-oate + 3 NAD+ + 4 H2O
overall reaction
-
-
-
cholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2 = (25S)-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
(1c)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
cholest-4-en-3-one,[reduced ferredoxin]:oxygen oxidoreductase [(25S)-3-oxocholest-4-en-26-oate forming]
A cytochrome P-450 (heme-thiolate) protein found in several bacterial pathogens. The enzyme is involved in degradation of the host's 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 [4]. The products are exclusively in the (25S) configuration. The enzyme is part of a two-component system that also includes a ferredoxin reductase (most likely KshB, which also interacts with EC 1.14.15.30, 3-ketosteroid 9alpha-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.15.28, cholest-4-en-3-one 27-monooxygenase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(25S)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
7alpha-hydroxycholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-7alphahydroxy-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholest-5-en-3beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
cholesterol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholesterol + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
(25S)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
(25S)-25-bromo-27-norcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-25-bromo-27-norcholesterol-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
26-methylcholesterol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-27-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
-
-
-
?
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
-
-
-
?
7alpha-hydroxycholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-7alphahydroxy-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
7alpha-hydroxycholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-7alphahydroxy-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
(25S)-26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
CYP125A1 generates oxidized sterols of the (25S)-26-hydroxy configuration
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
26-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
cholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
cholest-4-en-3-one + 6 reduced ferredoxin [iron-sulfur] cluster + 6 H+ + 3 O2
(25S)-3-oxocholest-4-en-26-oate + 6 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O
-
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-5-en-3beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-5-en-3beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
cholesterol + reduced ferredoxin [iron-sulfur] cluster + O2
26-hydroxycholesterol + oxidized ferredoxin [iron-sulfur] cluster + H2O
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
hydroxylation occurs at carbon 26 of the steroid side chain
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
-
-
-
?
27-hydroxycholest-4-en-3-one + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2
cholest-4-en-3-one-27-oic acid + 4 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
-
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
cholest-4-en-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
27-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
physiological substrate, the enzyme hydroxylates cholest-4-en-3-one at C-27
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
cholest-5-en-3-beta-ol + 6 reduced [2Fe-2S] ferredoxin + 3 O2
(25S)-3beta-hydroxycholest-5-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H2O
-
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
additional information
?
-
no substrates: 25-thia-27-norcholesterol, 24-bromochol-5-enol, 26-methylcholesta-5,25(26)-dienol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-[(4-methylcyclohexyl)carbonyl amino]-N-4-pyridinyl-1H-indole-3-propanamide
LP10, 30% inhibition at 0.2 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The Mycobacterium tuberculosis cytochromes P450: physiology, biochemistry & molecular intervention.
Infections
The structure of Mycobacterium tuberculosis CYP125: Molecular basis for cholesterol binding in a P450 needed for host infection.
Tuberculosis
A comparison of steroid and lipid binding cytochrome P450s from Mycobacterium marinum and Mycobacterium tuberculosis.
Tuberculosis
Acyl-Carbon Bond Cleaving Cytochrome P450 Enzymes: CYP17A1, CYP19A1 and CYP51A1.
Tuberculosis
Cytochrome P450 125 (CYP125) catalyzes C26-hydroxylation to initiate sterol side chain degradation in Rhodococcus jostii RHA1.
Tuberculosis
Deletion of cyp125 Confers Increased Sensitivity to Azoles in Mycobacterium tuberculosis.
Tuberculosis
Drug Modulation of Water-Heme Interactions in Low-Spin P450 Complexes of CYP2C9d and CYP125A1.
Tuberculosis
Functional redundancy of steroid C26-monooxygenase activity in mycobacterium tuberculosis revealed by biochemical and genetic analyses.
Tuberculosis
Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27-steroids.
Tuberculosis
Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one.
Tuberculosis
Potential drug targets in the Mycobacterium tuberculosis cytochrome P450 system.
Tuberculosis
Proximal ligand electron donation and reactivity of the cytochrome P450 ferric-peroxo anion.
Tuberculosis
Small-Molecule Scaffolds for CYP51 Inhibitors Identified by High-Throughput Screening and Defined by X-Ray Crystallography.
Tuberculosis
Substrate analog studies of the ?-regiospecificity of Mycobacterium tuberculosis cholesterol metabolizing cytochrome P450 enzymes CYP124A1, CYP125A1 and CYP142A1.
Tuberculosis
The structure of Mycobacterium tuberculosis CYP125: Molecular basis for cholesterol binding in a P450 needed for host infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0107
cholesterol
-
pH and temperature not specified in the publication
1.2
O2
-
apparent value, Km above 1.2 mM, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
0.0041
7alpha-hydroxycholest-4-en-3-one
wild-type, pH 7.4, temperature not specified in the publication
0.0051
7alpha-hydroxycholest-4-en-3-one
mutant Y87W, pH 7.4, temperature not specified in the publication
0.0208
cholest-4-en-3-one
-
pH and temperature not specified in the publication
0.0241
cholest-4-en-3-one
mutant W87Y, pH 7.4, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.92
cholest-4-en-3-one
-
pH and temperature not specified in the publication
0.47
cholesterol
-
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11000
O2
-
apparent value, in 0.1 M potassium phosphate at pH 7.0, temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
CYP125 performs an obligate first step in cholesterol degradation. CYP125 is involved in steroid C26-carboxylic acid formation, catalysing the oxidation of C26 either to the corresponding carboxylic acid or to an intermediate state
metabolism
CYP125A1 is a key enzyme in cholesterol metabolism and plays a crucial role in circumventing the deleterious effect of cholest-4-en-3-one
metabolism
-
CYP125A1 is a key enzyme in cholesterol metabolism and plays a crucial role in circumventing the deleterious effect of cholest-4-en-3-one
-
physiological function
-
cyp125 is essential for Rhodococcus jostii strain RHA1 to grow on 3-hydroxysterols such as cholesterol, but not on 3-oxo sterol derivatives
physiological function
-
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
physiological function
-
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
physiological function
CYP125A1 is required to incorporate the cholesterol side chain carbon atoms into cellular lipids. CYP125A1 is essential for growth of CDC1551 in media containing cholesterol or cholest-4-en-3-one
physiological function
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
Cyp125 is essential for the growth of Mycobacterium bovis strain bacillus Calmette-Guerin on cholesterol
-
physiological function
-
Cyp125 is not essential for the growth of Mycobacterium tuberculosis on cholesterol
-
physiological function
-
CYP125A1 is required to incorporate the cholesterol side chain carbon atoms into cellular lipids. CYP125A1 is essential for growth of CDC1551 in media containing cholesterol or cholest-4-en-3-one
-
Show AA Sequence and Transmembrane Helices (302 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to cholest-4-en-3-one, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris, pH 5.5, and 25% (w/v) PEG 3350
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate, 0.1 M bis-Tris (pH 5.5) and 0.5 M NaCl (truncated enzyme C429L in complex with inhibitor) or 0.1 M ammonium acetate, 0.1 M bis-Tris (pH 5.5) and 17% PEG 10000, or 2.0 M ammonium sulfate and 0.1 M Tris HCl pH 8.5 (truncated enzyme C429L without any ligand)
sitting drop vapor diffusion method, using MgCl2 with 0.1 M HEPES, pH 7.0 or 7.5, and 20% (w/v) PEG 6000 or 25% (w/v) PEG 3350, respectively
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C429L
W83Y
mutation to the corresponding residue of isoform CYP125A4. Mutation reduces the size of the binding pocket, reducing the ability to bind 7alpha-hydroxylated substrates
Y83W
mutation to the corresponding residue of isoform CYP125A3. Mutation increases the size of the binding pocket, increasing the ability to bind 7alpha-hydroxylated substrates. Enzyme shows activity toward 4-cholesten-3-one, albeit with sigmoidal kinetics
W83Y
-
mutation to the corresponding residue of isoform CYP125A4. Mutation reduces the size of the binding pocket, reducing the ability to bind 7alpha-hydroxylated substrates
-
Y83W
-
mutation to the corresponding residue of isoform CYP125A3. Mutation increases the size of the binding pocket, increasing the ability to bind 7alpha-hydroxylated substrates. Enzyme shows activity toward 4-cholesten-3-one, albeit with sigmoidal kinetics
-
C429L
the modification affect neither the binding nor the catalytic properties of the enzyme
C429L
-
the modification affect neither the binding nor the catalytic properties of the enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
65
-
the enzyme is heat inactivated by incubation at 65°C for 30 min
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography, Resource-Q column chromatography, and Sephacryl S-200 gel filtration
-
Ni2+-affinity column chromatography and Q Sepharose column chromatography
-
Source 15Q column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha cells
expressed in Rhodococcus jostii strain RHA1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cyp125 is up-regulated 7.1fold with growth on cholesterol
expression is not upregulated in response to cholesterol
cyp125 is up-regulated 7.1fold with growth on cholesterol
-
cyp125 is up-regulated 7.1fold with growth on cholesterol
Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin
-
-
expression is not upregulated in response to cholesterol
expression is not upregulated in response to cholesterol
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ouellet, H.; Lang, J.; Couture, M.; De Montellano, P.
Reaction of Mycobacterium tuberculosis Cytochrome P450 enzymes with nitric oxide
Biochemistry
48
863-872
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Ouellet, H.; Kells, P.; Ortiz De Montellano, P.; Podust, L.
Reverse type I inhibitor of Mycobacterium tuberculosis CYP125A1
Bioorg. Med. Chem. Lett.
21
332-337
2011
Mycobacterium tuberculosis (P9WPP1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP1)
brenda
McLean, K.; Lafite, P.; Levy, C.; Cheesman, M.; Mast, N.; Pikuleva, I.; Leys, D.; Munro, A.
The structure of Mycobacterium tuberculosis CYP125: Molecular basis for cholesterol binding in a P450 needed for host infection
J. Biol. Chem.
284
35524-35533
2009
Mycobacterium tuberculosis
brenda
Capyk, J.; Kalscheuer, R.; Stewart, G.; Liu, J.; Kwon, H.; Zhao, R.; Okamoto, S.; Jacobs Jr., W.; Eltis, L.; Mohn, W.
Mycobacterial cytochrome P450 125 (Cyp125) catalyzes the terminal hydroxylation of C27 steroids
J. Biol. Chem.
284
35534-35542
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycobacterium tuberculosis variant bovis bacillus Calmette-Guerin, Mycobacterium tuberculosis H37Rv
brenda
Johnston, J.B.; Ouellet, H.; Ortiz de Montellano, P.R.
Functional redundancy of steroid C26-monooxygenase activity in Mycobacterium tuberculosis revealed by biochemical and genetic analyses
J. Biol. Chem.
285
36352-36360
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycobacterium tuberculosis CDC 1551
brenda
Rosloniec, K.; Wilbrink, M.; Capyk, J.; Mohn, W.; Ostendorf, M.; Van Der Geize, R.; Dijkhuizen, L.; Eltis, L.
Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1
Mol. Microbiol.
74
1031-1043
2009
Rhodococcus jostii
brenda
Ouellet, H.; Guan, S.; Johnston, J.; Chow, E.; Kells, P.; Burlingame, A.; Cox, J.; Podust, L.; De Montellano, P.
Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one
Mol. Microbiol.
77
730-742
2010
Mycobacterium tuberculosis (P9WPP0), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (P9WPP0)
brenda
Frank, D.J.; Waddling, C.A.; La, M.; Ortiz de Montellano, P.R.
Cytochrome P450 125A4, the third cholesterol C-26 hydroxylase from Mycobacterium smegmatis
Biochemistry
54
6909-6916
2015
Mycolicibacterium smegmatis (A0QY38), Mycolicibacterium smegmatis (A0R4Y3), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0QY38), Mycolicibacterium smegmatis ATCC 700084 (A0R4Y3)
brenda
Johnston, J.B.; Singh, A.A.; Clary, A.A.; Chen, C.K.; Hayes, P.Y.; Chow, S.; De Voss, J.J.; Ortiz de Montellano, P.R.
Substrate analog studies of the omega-regiospecificity of Mycobacterium tuberculosis cholesterol metabolizing cytochrome P450 enzymes CYP124A1, CYP125A1 and CYP142A1
Bioorg. Med. Chem.
20
4064-4081
2012
Mycobacterium tuberculosis (P9WPP1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPP1)
brenda
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