Information on EC 1.14.15.15 - cholestanetriol 26-monooxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.14.15.15
-
RECOMMENDED NAME
GeneOntology No.
cholestanetriol 26-monooxygenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
1c
-
-
-
(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
show the reaction diagram
1b
-
-
-
5beta-cholestane-3alpha,7alpha,12alpha-triol + 2 reduced adrenodoxin + 2 H+ + O2 = (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + 2 oxidized adrenodoxin + H2O
show the reaction diagram
1a
-
-
-
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bile acid biosynthesis, neutral pathway
-
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Primary bile acid biosynthesis
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Metabolic 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.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-77-7
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62213-60-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
gene CYP27A1
UniProt
Manually annotated by BRENDA team
gene CYP125A4
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
show the reaction diagram
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
1alpha-hydroxyvitamin D3 + reduced adrenodoxin + O2
1alpha,25-dihydroxyvitamin D3 + oxidized adrenodoxin + H2O
show the reaction diagram
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2
?
show the reaction diagram
5-cholestene-3beta,7alpha-diol + reduced adrenodoxin + O2
5-cholestene-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
show the reaction diagram
5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestane-27-oic acid + oxidized adrenodoxin + H2O
show the reaction diagram
-
oxidation to the corresponding C27-acid
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,27-tetrol + oxidized adrenodoxin + H2O
show the reaction diagram
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
show the reaction diagram
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
?
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha-ol + reduced adrenodoxin + O2
?
show the reaction diagram
-
-
-
-
?
7-dehydrocholesterol + 4 reduced adrenodoxin + 2 H+ + 2 O2
25-hydroxy-7-dehydrocholesterol + 26/27-hydroxy-7-dehydrocholesterol + 4 oxidzed adrenodoxin + 2 H2O
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
-
?
beta-sitosterol + reduced adrenodoxin + O2
26-hydroxy-beta-sitosterol + 29-hydroxy-beta-sitosterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
cholesterol + reduced adrenodoxin + H+ + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cholesterol + reduced adrenodoxin + O2
24-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cholesterol + reduced adrenodoxin + O2
25-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cholesterol + reduced adrenodoxin + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
cholesterol + reduced adrenodoxin + O2
?
show the reaction diagram
-
-
-
-
?
ergosterol + reduced adrenodoxin + O2
24-hydroxyergosterol + 26-hydroxyergosterol + 28-hydroxyergosterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one + reduced adrenodoxin + H+ + O2
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one + reduced adrenodoxin + H+ + O2
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-al + oxidized adrenodoxin + H2O
show the reaction diagram
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + H+ + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + oxidzed adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
?
show the reaction diagram
5beta-cholestane-3alpha,7alpha-diol + reduced adrenodoxin + O2
5beta-cholestane-3alpha,7alpha,26-triol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
7alpha-hydroxy-4-cholesten-3-one + reduced adrenodoxin + O2
7alpha,26-dihydroxy-4-cholesten-3-one + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cholesterol + reduced adrenodoxin + H+ + O2
26-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
-
-
-
-
?
cholesterol + reduced adrenodoxin + O2
27-hydroxycholesterol + oxidized adrenodoxin + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adrenodoxin
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ATP
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peroxisomal and mitochondrial enzyme require ATP
cytochrome P450
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NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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peroxisomal and mitochondrial enzyme requires Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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1alpha-hydroxyvitamin D3
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competes with 5beta-cholestane-3alpha,7alpha,12alpha-triol
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
7,8-Benzoflavone
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68% inhibition at 0.04 mM
Aminoglutethimide
-
slight inhibition
Ca2+
-
complete inhibition at 1 mM
dicoumarol
-
10% inhibition at 0.05 mM
Isobutyramide
-
-
Metyrapone
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slight inhibition of 27-monooxygenase
N-bromosuccinimide
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50% loss of activity at 0.1 mM
p-chloromercuribenzoate
p-Chloromercuriphenyl sulfonate
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80% inhibition at 0.1 mM
Phenyl isocyanide
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
-
pH 7.4, 37C
0.0047
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one
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pH 7.4, 37C
0.0045 - 0.06
5beta-cholestane-3alpha,7alpha,12alpha-triol
0.01
5beta-cholestane-3alpha,7alpha-diol
-
-
0.01 - 0.02
O2
-
-
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0183
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
Homo sapiens
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pH 7.4, 37C, kcat for the conversion of (24S)-3beta-hydroxy-methyl-5alpha-cholesta-8(14),22-dien-15-one into side chain oxygenated products
0.00233 - 0.0233
1alpha-hydroxyvitamin D3
0.073
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one
Homo sapiens
-
pH 7.4, 37C, kcat for the conversion of (24S)-3beta-hydroxy-methyl-5alpha-cholesta-8(14),22-dien-15-one into side chain oxygenated products
0.333 - 0.6
5beta-cholestane-3alpha,7alpha,12alpha-triol
0.217
5beta-cholestane-3alpha,7alpha-diol
Rattus norvegicus
-
-
0.0117
cholesterol
Rattus norvegicus
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0157
(24S)-3beta-hydroxy-24-methyl-5alpha-cholesta-8(14),22-dien-15-one
Homo sapiens
-
pH 7.4, 37C
40025
0.001
3beta-hydroxy-5alpha-cholest-8(14)-en-15-one
Homo sapiens
-
pH 7.4, 37C
40026
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
5beta-cholestane-3alpha,7alpha,12alpha-triol
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-
2
Isobutyramide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00233
-
1alpha-hydroxyvitamin D3 as substrate
0.114
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5beta-cholestane-3alpha,7alpha,12alpha-triol as substrate
0.672
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.6
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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27-hydroxylation
8.3 - 11.2
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pH 8.3: about 20% of activity maximum, pH 11.2: about 60% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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primary astrocytes express different sterol hydroxylases and are able to uptake exogenous 27-hydroxycholesterol
Manually annotated by BRENDA team
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Mycobacterium smegmatis can grow on cholesterol as the sole carbon source
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
truncated enzyme form
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
only the mitochondrial hydroxylase system is specific for C-26 position, the microsomal system is unspecific for C-26 position but rather more active for other adjacent positions
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52500
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease
side-chain modification
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treatment of enzyme with iso[4]levuglandin E2 in vitro diminishes enzyme activity. Lys residues Lys134, Lys358, and Lys476, readily interact iso[4]levuglandin E2 in vitro, and modified CYP27A1 is present in the retina
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
90% loss of activity after 2 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, no loss of activity for 5 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full-length and truncated enzyme forms from liver mitochondria
-
native enzyme partially by mitochondria preparation
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partial purification of a ferredoxin-like iron-sulfur protein and a NADPH-ferredoxin reductase which are functional for 26-hydroxylation when reconstituted with partially purified liver mitochondrial cytochrome P-450
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recombinant His-tagged enzyme from Bacillus megaterium
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recombinant wild-type and mutant enzymes from Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CYP27 expression analysis in the brain
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DNA and amino acid sequence determinationa nd analysis, functional expression in COS-M6 cells, overview
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expression analysis
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expression of wild-type and mutant enzymes in Escherichia coli
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gene CYP27A1, cloned from liver cDNA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene CYP27A1, DNA and amino acid sequence determination and analysis, genotyping, overview
gene CYP27A1, DNA and amino acid sequence determination and genomic analysis, genotyping
-
gene CYP27A1, quantitative real-time PCR enzyme expression analysis
gene CYP27A1, recombinant expression of His-tagged enzyme in Bacillus megaterium
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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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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
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in vivo, in a high-salt administration experiment, male and female Dahl salt-sensitive rats become hypertensive after 4 weeks on a high-NaCl diet, their plasma marinobufagenin levels double, and adrenocortical CYP27A1 mRNA and protein increase 1.6fold and 2.0fold, respectively
ritonavir increases CYP27 expression in in differentiated THP-1 macrophages, but not in undifferentiated monocytes
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F207A/I211A/F215A
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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
R441W
-
naturally occuring mutation, involved in 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
R104/R441QQ
-
naturally occuring mutations, cause cerebrotendinous xanthomatosis
R441W
-
naturally occuring mutation, involved in cerebrotendinous xanthomatosis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine