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Information on EC 1.14.15.15 - cholestanetriol 26-monooxygenase
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1.14.15.15 cholestanetriol 26-monooxygenaseIUBMB Comments
This mitochondrial cytochrome P-450 enzyme requires adrenodoxin. It catalyses the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. Can also act on cholesterol, cholest-5-ene-3beta,7alpha-diol, 7alpha-hydroxycholest-4-en-3-one, and 5beta-cholestane-3alpha,7alpha-diol. The enzyme can also hydroxylate cholesterol at positions 24 and 25. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
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Word Map
- 1.14.15.15
- bile
- xanthomatosis
-
cerebrotendinous
- 27-hydroxycholesterol
-
chenodeoxycholic
- cholestanol
- tendon
- xanthomas
- oxysterols
- cataract
- cyp7a1
-
27-hydroxylation
-
cholic
-
12alpha-hydroxylase
- cholecalciferol
-
lipid-storage
-
lxralpha
-
7alpha-hydroxylated
- cholestyramine
- 7-ketocholesterol
- 7alpha-hydroxy-4-cholesten-3-one
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alpha-hydroxyvitamin
- medicine
-
lithogenic
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
6
+
6
+
3
=
+
6
+
4
+
6
reduced adrenodoxin
+
6
+
3
=
+
6
oxidized adrenodoxin
+
4
Synonyms
sterol 27-hydroxylase, cyp27, vitamin d3 25-hydroxylase, cyp27a, cytochrome p-450a, p450 27a1, cytochrome p450c27, 5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5beta-cholestane-3 alpha,7alpha,12alpha,26-tetrol dehydrogenase
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5beta-cholestane-3 alpha,7alpha,12alpha-triol-26-al oxidoreductase
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5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase
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5beta-cholestane-3alpha,7alpha,12alpha-triol 27-monooxygenase
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enzyme was renamed into 27-monooxygenase because it hydroxylates the methyl group in position 27
5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase
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cholestanetriol 26-hydroxylase
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cholestanetriol 27-hydroxylase
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CYP27
CYP27A1
cytochrome P-450A
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dehydrogenase, cholestanetetrol 26-
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EC 1.1.1.161
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formerly
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EC 1.14.13.15
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formerly
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EC 1.2.1.40
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formerly
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hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol
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oxygenase, cholestanetriol 26-mono-
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sterol 27-hydroxylase
TEHC-NAD oxidoreductase
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vitamin D3 25-hydroxylase
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additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + 2 reduced adrenodoxin + 2 H+ + O2 = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 2 oxidized adrenodoxin + H2O
1c
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-
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(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + 2 reduced adrenodoxin + 2 H+ + O2 = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + 2 oxidized adrenodoxin + 2 H2O
1b
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-
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5beta-cholestane-3alpha,7alpha,12alpha-triol + 2 reduced adrenodoxin + 2 H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + 2 oxidized adrenodoxin + H2O
1a
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-
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5beta-cholestane-3alpha,7alpha,12alpha-triol + 6 reduced adrenodoxin + 6 H+ + 3 O2 = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 6 oxidized adrenodoxin + 4 H2O
5beta-cholestane-3alpha,7alpha,12alpha-triol + 6 reduced adrenodoxin + 6 H+ + 3 O2 = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 6 oxidized adrenodoxin + 4 H2O
reaction mechanism
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5beta-cholestane-3alpha,7alpha,12alpha-triol + 6 reduced adrenodoxin + 6 H+ + 3 O2 = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + 6 oxidized adrenodoxin + 4 H2O
overall reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
5beta-cholestane-3alpha,7alpha,12alpha-triol,adrenodoxin:oxygen oxidoreductase (26-hydroxylating)
This mitochondrial cytochrome P-450 enzyme requires adrenodoxin. It catalyses the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. Can also act on cholesterol, cholest-5-ene-3beta,7alpha-diol, 7alpha-hydroxycholest-4-en-3-one, and 5beta-cholestane-3alpha,7alpha-diol. The enzyme can also hydroxylate cholesterol at positions 24 and 25. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
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CAS REGISTRY NUMBER
COMMENTARY
52227-77-7
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62213-60-9
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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
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O
-
-
-
-
?
1alpha-hydroxyvitamin D3 + reduced adrenodoxin + O2
1alpha,25-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O
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-
-
-
?
5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2
5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestane-27-oic acid + oxidized adrenodoxin + H2O
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oxidation to the corresponding C27-acid
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-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
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-
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-
?
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
?
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?
7-dehydrocholesterol + 4 reduced adrenodoxin + 2 H+ + 2 O2
25-hydroxy-7-dehydrocholesterol + 26/27-hydroxy-7-dehydrocholesterol + 4 oxidzed adrenodoxin + 2 H2O
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metabolites detected in serum of a patient with Smith-Lemli-Opitz syndrome. 25-hydroxy-7-dehydrocholesterol activates liver X receptors LXRalpha, LXRbeta and vitamin D receptor and 26/27-hydroxy-7-dehydrocholesterol induces activation of LXRalpha and LXRbeta, although the activities of both compounds on LXRs are weak. 26/27-Hydroxy-7-dehydrocholesterol is (3S,25S)-cholesta-5,7-diene-3,26-diol or (3S,25R)-cholesta-5,7-diene-3,26-diol
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?
7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2
7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O
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?
beta-sitosterol + reduced adrenodoxin + O2
26-hydroxy-beta-sitosterol + 29-hydroxy-beta-sitosterol + oxidized adrenodoxin + H2O
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?
cholesterol + reduced adrenodoxin + H+ + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
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?
cholesterol + reduced adrenodoxin + O2
24-hydroxycholesterol + oxidized adrenodoxin + H2O
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?
cholesterol + reduced adrenodoxin + O2
25-hydroxycholesterol + oxidized adrenodoxin + H2O
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?
cholesterol + reduced adrenodoxin + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
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?
ergosterol + reduced adrenodoxin + O2
24-hydroxyergosterol + 26-hydroxyergosterol + 28-hydroxyergosterol + oxidized adrenodoxin + H2O
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?
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
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the substrate is a potential drug for lowering cholesterol in the treatment and/or prevention of coronary artery disease, but it is rapidly metabolized in the liver
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?
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
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28-hydroxylation by CYP27A1, enzyme activity assay in presence of adrenodoxin, adrenodoxin reductase and NADPH
massspectrometric product analysis, 2 products, overview
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?
1alpha-hydroxyvitamin D3 + reduced adrenodoxin + O2
1alpha,25-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O
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25-hydroxylation
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?
1alpha-hydroxyvitamin D3 + reduced adrenodoxin + O2
1alpha,25-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O
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25-hydroxylation
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?
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2
?
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the substrate is a potential drug for lowering cholesterol in the treatment and/or prevention of coronary artery disease, but it is rapidly metabolized in the liver
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?
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2
?
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28-hydroxylation by CYP27A1, enzyme activity assay in presence of adrenodoxin, adrenodoxin reductase and NADPH
massspectrometric product analysis, 2 products, overview
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
-
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?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
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r
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
-
microsomal enzyme also catalyzes 25-hydroxylation of 5beta-cholestane-3alpha,7 alpha,12alpha-triol
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
-
isocitrate can act as electron donor
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
-
microsomal enzyme also catalyzes 25-hydroxylation of 5beta-cholestane-3alpha,7 alpha,12alpha-triol
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
-
mitochondrial enzyme is specific for 26-hydroxylation whereas the reaction with the microsomal enzyme hydroxylates at position 23, 24, 25 and 26
-
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
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-
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
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conversion of cholesterol to cholic acid
-
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
-
metabolism of cholesterol
-
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?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
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mitochondrial cytochrome P450 forms a complex with the substrate
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
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?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
-
?
additional information
?
-
-
the regioselectivity of the reaction is determined by residues of the helix F loop, e.g. F207, I211, and F215, substrate regiospecificity of wild-type and mutant enzymes, overview, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid and 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al are poor substrates
-
-
?
additional information
?
-
-
CYP27A1 catalyzes sterol 27-hydroxylation in many extrahepatic tissues and metabolizes bile acid intermediates in the liver, and vitamin D3 in the kidney
-
-
?
additional information
?
-
human CYP27A1 catalyzes hydroxylation of beta-sitosterol and ergosterol, CYP27A1 catalyzes the 26-hydroxylation of cholesterol to form the physiologically active product 26-hydroxycholesterol. CYP27A1 is also able to accept other steroids with structural similarity to cholesterol as substrates such as vitamin D3 and its precursor 7-dehydrocholesterol. NMR spectroscopic product analysis
-
-
?
additional information
?
-
-
enzyme CYP125A4 also oxidizes cholesterol, although it has a much higher activity for the oxidation of 7alpha-hydroxycholesterol, EC 1.14.14.23. The enzyme forms 7alpha,26-dihydroxycholesterol
-
-
?
additional information
?
-
-
the enzyme catalyzes the first step in the oxidation of the side chain of sterol intermediates in the biosynthesis of bile acids
-
-
?
additional information
?
-
-
a multifunctional enzyme catalyzing also the reaction of 25-hydroxyvitamin D3 1alpha-hydroxylase, EC 1.14.13.13, as well as the 24- and 25-hydroxylation of cholesterol, the truncated enzyme form is less efficient than the full-length CYP27A in the 27-hydroxylation of C27-sterols, and much less efficient in the 25-hydroxylation of 1alpha-hydroxyvitamin D3
-
-
?
additional information
?
-
-
the enzyme does not perform 7alpha-, 12alpha-, or 25-hydroxylations on C27-steroids
-
-
?
additional information
?
-
-
the sterol 27-hydroxylase performs multiple monooxygenations in the conversion of 58-cholestane-3alpha,7alpha,12alpha-triol into 3alpha,7alpha,l2alpha-trihydroxy-5beta-cholestanoic acid, product identification by gas spectrometry
-
-
?
additional information
?
-
-
sterol 27-hydroxylase is regulated by liver X receptor signaling, overview
-
-
?
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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
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
-
the substrate is a potential drug for lowering cholesterol in the treatment and/or prevention of coronary artery disease, but it is rapidly metabolized in the liver
-
-
?
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O
-
-
-
-
?
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2
?
-
the substrate is a potential drug for lowering cholesterol in the treatment and/or prevention of coronary artery disease, but it is rapidly metabolized in the liver
-
-
?
5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2
5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
-
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2
7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O
-
-
-
-
?
cholesterol + reduced adrenodoxin + H+ + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
-
-
-
r
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
-
conversion of cholesterol to cholic acid
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
-
metabolism of cholesterol
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
-
mitochondrial cytochrome P450 forms a complex with the substrate
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
additional information
?
-
-
CYP27A1 catalyzes sterol 27-hydroxylation in many extrahepatic tissues and metabolizes bile acid intermediates in the liver, and vitamin D3 in the kidney
-
-
?
additional information
?
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enzyme CYP125A4 also oxidizes cholesterol, although it has a much higher activity for the oxidation of 7alpha-hydroxycholesterol, EC 1.14.14.23. The enzyme forms 7alpha,26-dihydroxycholesterol
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additional information
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the enzyme catalyzes the first step in the oxidation of the side chain of sterol intermediates in the biosynthesis of bile acids
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additional information
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sterol 27-hydroxylase is regulated by liver X receptor signaling, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome P450
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involvement of a cytochrome-P450-dependent monooxygenase in the 26-hydroxylation of 5beta-cholestane-3alpha,7alpha,12alpha-triol
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cytochrome P450
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possible function of a cytochrome-P450-like entity in the intramitochondrial 26-hydroxylase system
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cytochrome P450
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mitochondrial cytochrome-P450 forms an enzyme-substrate complex with 5beta-cholestane-3alpha,7alpha,12alpha-triol with Km value very similar to the Km value of 26-hydroxylation
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cytochrome P450
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inner mitochondrial membrane houses a species of cytochrome-P450 functional in 5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1alpha-hydroxyvitamin D3
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competes with 5beta-cholestane-3alpha,7alpha,12alpha-triol
5beta-cholestane-3alpha,7alpha-diol
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inhibits 5beta-cholestane-3alpha,7alpha,12alpha-triol 27-monooxygenase activity only slightly
5beta-cholestane-3alpha,7alpha,12alpha-triol
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inhibits 5beta-cholestane-3alpha,7alpha-diol 27-monooxygenase activity
5beta-cholestane-3alpha,7alpha,12alpha-triol
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competes with 1alpha-hydroxyvitamin D3
additional information
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the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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endogenous and pharmacological glucocorticoids may have a strong impact on several aspects of cholesterol homeostasis and other processes related to CYP27A1-mediated metabolism
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additional information
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the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine
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additional information
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astrocyte-restricted upregulation of Cyp27a1 due to to differential expression of transcriptional co-activators, increase of enzyme mRNA and protein levels in treated astrocytes is paralleled by transactivation of the proximal Cyp27a1 promoter in transfected astrocytes
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
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pH 7.4, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0183
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
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pH 7.4, 37°C, kcat for the conversion of (24S)-3beta-hydroxy-methyl-5alpha-cholesta-8(14),22-dien-15-one into side chain oxygenated products
0.073
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one
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pH 7.4, 37°C, kcat for the conversion of (24S)-3beta-hydroxy-methyl-5alpha-cholesta-8(14),22-dien-15-one into side chain oxygenated products
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0157
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
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pH 7.4, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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27-hydroxylation activity of the full-length enzyme form is about 4fold higher than the activity of the truncated enzyme form
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4