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Information on EC 1.14.15.15 - cholestanetriol 26-monooxygenase and Organism(s) Homo sapiens
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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
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lipid-storage
-
lxralpha
-
7alpha-hydroxylated
- cholestyramine
- 7-ketocholesterol
- 7alpha-hydroxy-4-cholesten-3-one
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alpha-hydroxyvitamin
- medicine
-
lithogenic
The taxonomic range for the selected organisms is: Homo sapiens
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
topSYNONYM 
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 hydroxylase
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cholestanetriol 26-hydroxylase
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cholestanetriol 27-hydroxylase
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-
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CYP27A1
cytochrome P-450A
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-
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dehydrogenase, cholestanetetrol 26-
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-
-
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hydroxylase, 5beta-cholestane-3alpha,7alpha,12alpha-triol
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oxygenase, cholestanetriol 26-mono-
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-
-
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sterol 27-hydroxylase
TEHC-NAD oxidoreductase
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vitamin D3 25-hydroxylase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
-
-
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
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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
?
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 + 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
-
-
-
-
?
7-dehydrocholesterol + 4 reduced adrenodoxin + 2 H+ + 2 O2
25-hydroxy-7-dehydrocholesterol + 26/27-hydroxy-7-dehydrocholesterol + 4 oxidzed adrenodoxin + 2 H2O
-
-
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
-
?
beta-sitosterol + reduced adrenodoxin + O2
26-hydroxy-beta-sitosterol + 29-hydroxy-beta-sitosterol + 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
?
-
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
-
?
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
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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
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?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
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-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
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-
-
?
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
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?
additional information
?
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CYP27A1 catalyzes sterol 27-hydroxylation in many extrahepatic tissues and metabolizes bile acid intermediates in the liver, and vitamin D3 in the kidney
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?
additional information
?
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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
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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
-
-
?
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
-
-
?
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-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
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?
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
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
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-
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-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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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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
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3 - 11.2
-
pH 8.3: about 20% of activity maximum, pH 11.2: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
both alcohol:NAD+ oxidoreductase activity, EC 1.1.1.1, and 5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol:NAD+ 26-oxidoreductase activity, EC 1.1.1.161, are catalyzed by the same active side of the same enzyme protein
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
membrane topology of CYP27A1, mapping of interacting peptides in the enzyme sequence, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme initiates the biosynthesis of bile acids, pathway overview
physiological function
additional information
malfunction
CYP27A1 deficiency may upregulate the activity of 11beta-hydroxysteroid dehydrogenase 1, and downregulate the activity of 11beta-hydroxysteroid dehydrogenase 2. In a patient with cerebrotendinous xanthomatosis carrying a loss-of-function mutation in CYP27A1, the plasma concentrations of 27-hydroxycholesterol are dramatically reduced, with enhanced HSD11B1 and diminished HSD11B2 activities
malfunction
post-transcriptional silencing of the CYP27A1 gene in human trophoblast reduces the expression of CYP27A1 mRNA by 70%, reduces total bile acids by 2fold, and marinobufagenin levels by 67% when compared with nontreated cells or cells transfected with nontargeting siRNA
physiological function
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CYP27A! catalyzes sterol 27-hydroxylation in many extrahepatic tissues and metabolizes bile acid intermediates in the liver, and vitamin D3 in the kidney
physiological function
bioactive steroid marinobufagenin, an endogenous Na/K-ATPase bufadienolide inhibitor that is synthesized by adrenocortical and placental cells, is derived from cholesterol through the traditional steroidogenesis pathway initiated by enzyme CYP11A1, and via the acidic bile acid pathway, which is controlled by enzyme CYP27A1
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
physiological function
the enzyme forms 26-hydroxycholesterolthat acts as an endogenous selective estrogen receptor modulator and has, among multiple other functions, a strong influence on the promotion of estrogen receptor dependent breast cancer, the bone mineralization as well as the cardiovascular system
additional information
-
cerebrotendinous xanthomatosis, CTX, is a rare autosomal recessive sterol storage disease caused by a mutated sterol 27-hydroxylase CYP27A1 gene
additional information
-
mutations of gene CYP27A1 cause defects in the cholesterol pathway to bile acids that lead to the storage of cholestanol and cholesterol in tendons, lenses and the central nervous system. This disorder is the cause of a clinical syndrome known as cerebrotendinous xanthomatosis, CTX, phenotype, overview
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_HUMAN
531
0
60235
Swiss-Prot
Mitochondrion (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the region between helices F and G, the F-G loop, is proposed to contribute to membrane binding in microsomal P450s
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F207A/I211A/F215A
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
F207K
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
F207K/I211K/F215K
-
site-directed mutagenesis, nearly no expression of the mutant in Escherichia coli
F215A
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
F215K
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
I211K
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
I211K/F215K
-
site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
R104/R441QQ
-
naturally occuring mutations, cause cerebrotendinous xanthomatosis
W235A
-
site-directed mutagenesis, the mutant is partly expressed as cytosolic enzyme, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
Y238A
-
site-directed mutagenesis, the mutant is partly expressed as cytosolic enzyme, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme
additional information
additional information
-
expression and subcellular distribution of the P450 27A1 mutants, overview
additional information
-
naturally occuring mutations in the CYP27A1 gene cause cerebrotendinous xanthomatosis, CTX. A German patient is a compound heterozygote carrying two mutations both located in exon 8, phenotypes, overview. One mutation is a novel four nucleotide deletion, c.1330-1333delTTCC, that results in a frameshift and the occurrence of a premature stop codon leading to the formation of a truncated protein of 448 amino acids. The other mutation, previously reported, is a C - > T transition, c.c.1381C-T, that converts the glutamine codon at position 461 into a termination codon, p.Q461X
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CYP27A1, DNA and amino acid sequence determination and analysis, genotyping, overview
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gene CYP27A1, DNA and amino acid sequence determination and genomic analysis, genotyping
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gene CYP27A1, recombinant expression of His-tagged enzyme in Bacillus megaterium
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dexamethasone increases CYP27A1-mediated enzyme activity in HepG2 cells by CYP27A1 promoter activity more than 4fold as compared with untreated cells, mediated by glucocorticoid receptor alpha, glucocorticoid receptor alpha-antagonist mifepristone almost completely abolishes the dexamethasone-induced effect on the CYP27A1 promoter activity
-
ritonavir increases CYP27 expression in in differentiated THP-1 macrophages, but not in undifferentiated monocytes
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
7-dehydrocholesterol is catabolized by isoform CYP27A1 to metabolites that act as selective liver X receptor LXR modulators. Metabolites detected in serum of a patient with Smith-Lemli-Opitz syndrome are 25-hydroxy-7-dehydrocholesterol which activates liver X receptors LXRalpha, LXRbeta and vitamin D receptor and 26/27-hydroxy-7-dehydrocholesterol which induces activation of LXRalpha and LXRbeta, although the activities of both compounds on LXRs are weak
medicine
the endogenous steroidal Na/K-ATPase inhibitor, marinobufagenin, is synthesized in mammalian placenta and adrenal cortex from cholesterol through the novel acidic bile acid pathway, role of marinobufagenin in highly prevalent human cardiovascular diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuda, A.; Okuda, K.
Physiological function and kinetic mechanism of human liver alcohol dehydrogenase as 5beta-cholestane-3alpha,7alpha,12alpha,26-tetrol dehydrogenase
J. Biol. Chem.
258
2899-2905
1983
Homo sapiens
Pikuleva, I.A.; Puchkaev, A.; Bjoerkhem, I.
Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A
Biochemistry
40
7621-7629
2001
Homo sapiens
Pettersson, H.; Norlin, M.; Andersson, U.; Pikuleva, I.; Bjoerkhem, I.; Misharin, A.; Wikvall, K.
Metabolism of a novel side chain modified DELTA8(14)-15-ketosterol, a potential cholesterol lowering drug: 28-hydroxylation by CYP27A1
Biochim. Biophys. Acta
1781
383-390
2008
Homo sapiens
Tang, W.; Norlin, M.; Wikvall, K.
Glucocorticoid receptor-mediated upregulation of human CYP27A1, a potential anti-atherogenic enzyme
Biochim. Biophys. Acta
1781
718-723
2008
Homo sapiens
Pou, J.; Rebollo, A.; Roglans, N.; Sanchez, R.M.; Vazquez-Carrera, M.; Laguna, J.C.; Pedro-Botet, J.; Alegret, M.
Ritonavir increases CD36, ABCA1 and CYP27 expression in THP-1 macrophages
Exp. Biol. Med.
233
1572-1582
2008
Homo sapiens
Pikuleva, I.A.; Mast, N.; Liao, W.L.; Turko, I.V.
Studies of membrane topology of mitochondrial cholesterol hydroxylases CYPs 27A1 and 11A1
Lipids
43
1127-1132
2008
Homo sapiens
Nozue, T.; Higashikata, T.; Inazu, A.; Kawashiri, M.A.; Nohara, A.; Kobayashi, J.; Koizumi, J.; Yamagishi, M.; Mabuchi, H.
Identification of a novel missense mutation in the sterol 27-hydroxylase gene in two Japanese patients with cerebrotendinous xanthomatosis
Intern. Med.
49
1127-1131
2010
Homo sapiens
Schneider, H.; Lingesleben, A.; Vogel, H.P.; Garuti, R.; Calandra, S.
A novel mutation in the sterol 27-hydroxylase gene of a woman with autosomal recessive cerebrotendinous xanthomatosis
Orphanet J. Rare Dis.
5
27
2010
Homo sapiens
Endo-Umeda, K.; Yasuda, K.; Sugita, K.; Honda, A.; Ohta, M.; Ishikawa, M.; Hashimoto, Y.; Sakaki, T.; Makishima, M.
7-Dehydrocholesterol metabolites produced by sterol 27-hydroxylase (CYP27A1) modulate liver X receptor activity
J. Steroid Biochem. Mol. Biol.
140
7-16
2013
Homo sapiens
Ehrhardt, M.; Gerber, A.; Zapp, J.; Hannemann, F.; Bernhardt, R.
Human CYP27A1 catalyzes hydroxylation of beta-sitosterol and ergosterol
Biol. Chem.
397
513-518
2016
Homo sapiens (Q02318)
Fedorova, O.V.; Zernetkina, V.I.; Shilova, V.Y.; Grigorova, Y.N.; Juhasz, O.; Wei, W.; Marshall, C.A.; Lakatta, E.G.; Bagrov, A.Y.
Synthesis of an endogenous steroidal Na pump inhibitor marinobufagenin, implicated in human cardiovascular diseases, is initiated by CYP27A1 via bile acid pathway
Circ. Cardiovasc. Genet.
8
736-745
2015
Homo sapiens (Q02318), Rattus norvegicus (P17178)
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