Any feedback?
Information on EC 1.14.15.15 - cholestanetriol 26-monooxygenase and Organism(s) Mus musculus and UniProt Accession Q9DBG1
for references in articles please use BRENDA:EC1.14.15.15Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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
-
alpha-hydroxyvitamin
- medicine
-
lithogenic
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
+
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, 
more
top
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5beta-cholestane-3 alpha,7alpha,12alpha,26-tetrol dehydrogenase
-
-
-
-
5beta-cholestane-3 alpha,7alpha,12alpha-triol-26-al oxidoreductase
-
-
-
-
5beta-cholestane-3alpha,7alpha,12alpha-triol 26-hydroxylase
-
-
-
-
5beta-cholestane-3alpha,7alpha,12alpha-triol hydroxylase
-
-
-
-
cholestanetriol 26-hydroxylase
-
-
-
-
cholestanetriol 27-hydroxylase
-
-
-
-
cytochrome P-450A
-
-
-
-
dehydrogenase, cholestanetetrol 26-
-
-
-
-
hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol
-
-
-
-
oxygenase, cholestanetriol 26-mono-
-
-
-
-
TEHC-NAD oxidoreductase
-
-
-
-
vitamin D3 25-hydroxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY
52227-77-7
-
62213-60-9
-
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
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
-
-
-
-
?
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
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
in Cyp27a1 knockout mice, the plasma concentrations of 27-hydroxycholesterol are undetectable. In the liver of the mutant mice, the increase in concentrations of active glucocorticoids is due to increased liver weight as a consequence of Cyp27a1 deficiency
physiological function
in the liver, CYP27A1 catalyses the first step of the alternative pathway of bile acid biosynthesis and intermediate reactions in the classical pathway initiated by CYP7A1. In extrahepatic tissues, CYP27A1 plays a role in reverse cholesterol transport because its product 27-hydroxycholesterol is removed and carried to the liver, where it is converted to bile acids. 27-Hydroxycholesterol is a key regulator of cholesterol homeostasis. Sterol 27-hydroxylase (CYP27A1) catalyses the first step in the alternative pathway of bile acid synthesis by hydroxylating cholesterol to 27-hydroxycholesterol, which is a natural ligand for liver X receptor. In vitro agonist treatment of liver X receptor downregulates the activity of 11beta-hydroxysteroid dehydrogenase 1, HSD11B1, that is involved in regulation of intracellular availability of glucocorticoids
additional information
-
the rare disease cerebrotendinous xanthomatosis, CTX, is caused by a lack of CYP27A1 in humans, characterized by cholestanol-containing xanthomas in brain and tendons, but mice with the same defect do not develop xanthomas. Female cyp27a1 knockout mice have an increase of cholestanol of about 2.5fold in plasma, 6fold in tendons, and 12fold in brain. Treatment of cyp27a1-/- mice with 0.05% cholic acid normalizes the cholestanol levels in tendons and plasma and reduces the content in the brain. No significant difference between cyp27a1 knockout mice and wild-type mice with respect to content of cholesterol in the brain. 7alpha-Hydroxy-4-cholesten-3-one is an important precursor of cholestanol in the brain of the cyp27a1 knockoout mice
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CP27A_MOUSE
533
0
60720
Swiss-Prot
Mitochondrion (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R104/R441QQ
-
naturally occuring mutations, cause cerebrotendinous xanthomatosis
additional information
additional information
-
naturally occuring mutations in the CYP27A1 gene cause cerebrotendinous xanthomatosis, CTX. One of two Japanese patients is a compound heterozygote for Arg104Gln in exon 2 and Arg441Gln in exon 8, the other patient is a compound heterozygote for Arg441Trp in exon 8 and a second mutation not identified
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CYP27A1, DNA and amino acid sequence determination and analysis, genotyping, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuda, K.; Hoshita, N.
Oxidation of 5-beta-cholestane-3alpha,7alpha, 12alpha-triol by rat-liver mitochondria
Biochim. Biophys. Acta
164
381-388
1968
Mus musculus, Rattus norvegicus
Bavner, A.; Shafaati, M.; Hansson, M.; Olin, M.; Shpitzen, S.; Meiner, V.; Leitersdorf, E.; Bjoerkhem, I.
On the mechanism of accumulation of cholestanol in the brain of mice with a disruption of sterol 27-hydroxylase
J. Lipid Res.
51
2722-2730
2010
Mus musculus
EXTERNAL LINKS (specific for EC-Number 1.14.15.15)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
