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Information on EC 1.14.14.23 - cholesterol 7alpha-monooxygenase and Organism(s) Homo sapiens and UniProt Accession P22680

for references in articles please use BRENDA:EC1.14.14.23
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IUBMB Comments
A P-450 heme-thiolate liver protein that catalyses the first step in the biosynthesis of bile acids. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH---hemoprotein reductase.
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This record set is specific for:
Homo sapiens
UNIPROT: P22680
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cyp7a1, cholesterol 7 alpha-hydroxylase, cholesterol 7alpha-hydroxylase, 7alpha-hydroxylase, cyp7a, hepatic cholesterol 7alpha-hydroxylase, cholesterol 7-alpha hydroxylase, cholesterol 7-alpha-hydroxylase, cholesterol 7a-hydroxylase, c7alphaoh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cholesterol 7 alpha-hydroxylase
-
cholesterol 7alpha-hydroxylase
-
C7alphaOH
-
-
cholesterol 7 alpha-hydroxylase
-
-
Cholesterol 7-alpha-hydroxylase
-
-
-
-
Cholesterol 7-alpha-monooxygenase
-
-
-
-
cholesterol 7alpha-hydroxylase
cholesterol-NADPH oxidoreductase, 7alpha-hydroxylating
-
-
CYPVII
-
-
-
-
hepatic cholesterol 7alpha-hydroxylase
-
-
oxygenase, cholesterol 7alpha-mono-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
cholesterol,NADPH-hemoprotein reductase:oxygen oxidoreductase (7alpha-hydroxylating)
A P-450 heme-thiolate liver protein that catalyses the first step in the biosynthesis of bile acids. The direct electron donor to the enzyme is EC 1.6.2.4, NADPH---hemoprotein reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
9037-53-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
25-hydroxycholesterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
27-hydroxycholesterol + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
cholest-4-en-3-one + [reduced NADPH-hemoprotein reductase] + O2
?
show the reaction diagram
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
7-dehydrocholesterol + NADPH + H+
7-oxocholesterol + NADP+ + H2O
show the reaction diagram
-
-
minor product: 7alpha,8alpha-epoxide, reaction with 7-[2H1]dehydrocholesterol yields complete migration of deuterium in the product 7-oxocholesterol. Minor product: 7alpha8alpha-epoxide
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lathosterol + NADPH + H+
7-oxocholestanol + cholestanol-7alpha,8alpha-epoxide + NADP+ + H2O
show the reaction diagram
-
i.e. DELTA-dihydro-7-dehydrocholesterol
about 1:2 ratio of 7-oxo and epoxide products, the epoxide does not rearrange to the ketone
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
7-dehydrocholesterol + NADPH + H+
7-oxocholesterol + NADP+ + H2O
show the reaction diagram
-
-
minor product: 7alpha,8alpha-epoxide
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
lathosterol + NADPH + H+
7-oxocholestanol + cholestanol-7alpha,8alpha-epoxide + NADP+ + H2O
show the reaction diagram
-
i.e. DELTA-dihydro-7-dehydrocholesterol
about 1:2 ratio of 7-oxo and epoxide products, the epoxide does not rearrange to the ketone
-
?
additional information
?
-
-
the cholesterol 7alpha-hydroxylase is critical in bile acid and cholesterol metabolism, polymorphisms of CP7A1 are of no physiologic significance, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
heme
-
cytochrome P-450 dependent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
taurochenodeoxycholate
70% inhibition at 0.1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4,6-trihydroxyacetophenone
-
CYP7A1 induction, 166%, and activation, 160%, by 2,4,6-trihydroxyacetophenone, which also antagonizes the inhibition of CYP7A1 expression by chenodeoxycholic acid
dithiothreitol
-
-
additional information
enzyme expression is induced by cholesterol, bile acids, cytokines, steroid hormones, and thyroid hormone
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
7-dehydrocholesterol
-
pH 7.4, 30°C
0.0018 - 0.0021
lathosterol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
25-hydroxycholesterol
pH 7.2, 37°C, wild-type enzyme
0.0685 - 0.117
27-Hydroxycholesterol
0.003 - 0.117
cholest-4-en-3-one
0.008 - 0.023
cholesterol
0.04
7-dehydrocholesterol
-
pH 7.4, 30°C
0.06 - 0.12
lathosterol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
30
7-dehydrocholesterol
-
pH 7.4, 30°C
30 - 50
lathosterol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000034
wild-type Hep-G2 cell microsomes
0.000092
recombinant enzyme in transformed Hep-G2 cells
0.00015
-
-
0.00077
-
after incubation with 1 unit alkaline phosphatase for 30 min
0.00196
-
-
0.00294
-
after incubation with 5 units cAMP-dependent protein kinase for 30 min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
HepG2 cell transformed with a cyp7alpha-reporter gene (promoter fragment fused to firefly luciferase)
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the cytochrome P450 family
metabolism
physiological function
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CP7A1_HUMAN
504
1
57661
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
x * 50000, approximately, SDS-PAGE
51000
-
x * 51000, SDS-PAGE, expressed in Escherichia coli
58000
-
x * 58000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 50000, approximately, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the enzyme is phosphorylated at multiple amino acids, overview
side-chain modification
-
enzyme activity decreases after dephosphorylation with alkaline phosphatase and increases after phosphorylation with cAMP-dependent protein kinase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type CYP7A1 in the ligand-free state, structure-based mutation T104L in the B' helix, corresponding to the nonpolar residue of CYP7B1, is used to obtain crystals of complexes with cholest-4-en-3 -one and with cholesterol oxidation product 7-ketocholesterol, hanging drop vapor diffusion method, mixing 0f 0.001 ml of protein solution with 0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.1 M trisodium citrate, pH 5.5, and 20% PEG 400, 18°C, to obtain a complex with cholest-4-en-3-one, a T104L mutant is used, and the crystals are grown in conditions containing 0.1 M MES, pH 6.0, and 18% PEG 550 monomethylether and soaked with 20% glycerol. For the T104L mutant-7KCh complex, crystals are grown in 0.1 M sodium chloride, 0.1 M tri-sodium citrate, pH 5.6, and 20% PEG 400, room temperature, X-ray diffraction structure determination and analysis at 1.90-2.75 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A204C
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene, the genetic variant shows less total cholesterol level decrease in response to dietary changes in different types of dietary intervention studies compared to C204 homozygotes, overview
A278C
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene
C554T
nucleotide exchange, a naturally occuring promoter polymorphism in the CYP7A1 gene
T104L
the mutant is similar to the wild-type in ligand binding and catalytic properties and readily crystallizes with substrates. The structure of the T104L mutant in complex with cholest-4-en-3-one explicitly identifies key residues involved in 7alpha-hydroxylation
C16A
-
strongly decreased activity
C175A
-
decreased activity
C17A
-
increased activity
C444A
-
no activity
C44A
-
decreased activity
C476A
-
no activity
C69A
-
no effect on activity
C90A
-
decreased activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation upon incubating microsomes with NADPH, half-life: 1 h, addition of dithiothreitol partially protects against inactivation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and recombinant enzyme partially by microsome preparation
partially from Hep-G2 cells by microsome preparation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), stable expression of CYP7A cDNA using the cytomegalovirus promoter and the bovine growth hormone polyadenylation signal in Hep-G2 cells
gene Cyp7a1, enzyme expression analysis
gene CYP7A1, genetic structure, the gene contains six exons and five introns and is located on chromosome 8 at 8q11-q12, CYP7A1 mRNA levels are regulated through the farnesoid X receptor and the liver X receptor by many stimuli including cholesterol, bile acids, cytokines, steroid hormones, and thyroid hormone
gene CYP7A1, transient expression in Hep-G2 cells
expressed in Mus musculus liver
-
expression in Escherichia coli
-
gene CYP7A1, genotyping, overview. Expression of promoter constructs in HepG2 cells
-
gene CYP7AI, genotyping, overexpression of genetic variants in Hep-G2 cells
-
native and mutated genes expressed in COS-1 cells
-
recombinant enzyme expressed in transgenic mice
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cyp7a1 is a direct thyroid hormone target gene that responds to physiologic thyroid hormone levels through a set of distinct response elements in its promoter
in farnesoid X receptor-deficient and wild-type mice with hypercholesterolemia, injection of 1alpha,25-dihydroxyvitamin D3 consistently reduces levels of plasma and liver cholesterol and farnesoid X receptor small heterodimer partner Shp mRNA, and increases hepatic Cyp7a1 mRNA and protein. The transcription factors, liver receptor homolog-1 (NR5A2) and hepatocyte nuclear factor 4a (NR2A1), are essential for CYP7A1 expression
activation of an AMP-activated protein kinase decreases CYP7A1 mRNA, hepatocyte nuclear factor 4alpha protein, and binding to CYP7A1 chromatin
-
bile acid-activated farnesoid X receptor, FXR, inhibits CYP7A1 transcription via activation of FGF15 receptor 4 signaling in hepatocytes, or via FGF19, that strongly inhibits CYP7A1 mRNA expression, overview. miR-122a and miR-422a may destabilize CYP7A1 mRNA to inhibit CYP7A1 expression, putative recognition sequences for miR-122a and miR-422a are localized in the 3'-UTR of human CYP7A1 mRNA
-
Chlamydia pneumoniae and human cytomegalovirus infections significantly decrease isoform CYP7A1 promoter activity in a dose-dependent manner, with maximal inhibitions of 33% and 32%, respectively
-
CYP7A1 mRNAs have very short half-lives, and bile acids destabilize CYP7A1 mRNA via the 3'-untranslated region
-
fibroblast growth factor 19 inhibits cholesterol 7alpha-hydroxylase mRNA expression
-
Forkhead box transcription factor O1 inhibits cholesterol 7alpha-hydroxylase mRNA expression
-
high glucose stimulates bile acid synthesis and induces mRNA expression of cholesterol 7alpha-hydroxylase, the key regulatory gene in bile acid synthesis. Glucose increased ATP levels to inhibit AMPK and induce HNF4alpha to stimulate CYP7A1 gene transcription. Knockdown of ATP-citrate lyase, which converts citrate to acetyl-CoA, decreases histone acetylation, and attenuates glucose induction of CYP7A1 mRNA expression
-
lithocholic acid-acetate and 1alpha,25-dihydroxy-vitamin D3 inhibit cholesterol 7alpha-hydroxylase mRNA expression
-
several nutritive peptides inhibit luciferase expression (cyp7alpha-reporter gene (promoter fragment fused to firefly luciferase))
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
manipulation of hormone signaling pathways can provide a strategy to enhance Cyp7a1 activity in human patients
analysis
-
development of a straightforward dual-reporter bioluminescent assay to simultaneously monitor isoform CYP7A1 transcriptional regulation and cell viability in Chlamydia pneumoniae and human cytomegalovirus infected human hepatoblastoma Hep-G2 cells
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Erickson, S.K.; Bsterling, B.
Cholesterol 7alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles
J. Lipid Res.
22
872-876
1981
Homo sapiens
Manually annotated by BRENDA team
Nguyen, L.B.; Shefer, S.; Salen, G.; Ness, G.; Tanaka, R.D.; Packin, V.; Thomas, P.; Shore, V.; Batta, A.
Purification of cholesterol 7alpha-hydroxylase from human and rat liver and production of inhibiting polyclonal antibodies
J. Biol. Chem.
265
4541-4546
1990
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Nguyen, L.B.; Shefer, S.; Salen, G.; Chiang, J.Y.L.; Patel, M.
Cholesterol 7alpha-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation
Hepatology
24
1468-1474
1996
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Galman, C.; Arvidsson, I.; Angelin, B.; Rudling, M.
Monitoring hepatic cholesterol 7alpha-hydroxylase activity by assay of the stable bile acid intermediate 7alpha-hydroxy-4-cholesten-3-one in peripheral blood
J. Lipid Res.
44
859-866
2003
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kinowaki, M.; Tanaka, S.; Maeda, Y.; Higashi, S.; Okuda, K.; Setoguchi, T.
Half-life of cholesterol 7alpha-hydroxylase activity and enzyme mass differ in animals and humans when determined by a monoclonal antibody against human cholesterol 7alpha-hydroxylase
J. Steroid Biochem. Mol. Biol.
81
377-380
2002
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Tanaka, S.; Kinowaki, M.; Eto, T.A.; Ota, Y.; Maeda, Y.; Okuda, K.; Setoguchi, T.; Chijiiwa, K.
Sulfhydryl groups responsible for extreme lability of human cholesterol 7alpha-hydroxylase identified by site-directed mutagenesis
J. Steroid Biochem. Mol. Biol.
86
35-40
2003
Cricetulus griseus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Tiemann, M.; Han, Z.; Soccio, R.; Bollineni, J.; Shefer, S.; Sehayek, E.; Breslow, J.L.
Cholesterol feeding of mice expressing cholesterol 7alpha-hydroxylase increases bile acid pool size despite decreased enzyme activity
Proc. Natl. Acad. Sci. USA
101
1846-1851
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Abrahamsson, A.; Krapivner, S.; Gustafsson, U.; Muhrbeck, O.; Eggertsen, G.; Johansson, I.; Persson, I.; Angelin, B.; Ingelman-Sundberg, M.; Bjoerkhem, I.; Einarsson, C.; vant Hooft, F.M.
Common polymorphisms in the CYP7A1 gene do not contribute to variation in rates of bile acid synthesis and plasma LDL cholesterol concentration
Atherosclerosis
182
37-45
2005
Homo sapiens
Manually annotated by BRENDA team
Stroup, D.; Ramsaran, J.R.
Cholesterol 7alpha-hydroxylase is phosphorylated at multiple amino acids
Biochem. Biophys. Res. Commun.
329
957-965
2005
Homo sapiens (P22680), Homo sapiens
Manually annotated by BRENDA team
Charoenteeraboon, J.; Nithipatikom, K.; Campbell, W.B.; Piyachaturawat, P.; Wilairat, P.; Rongnoparut, P.
Induction of human cholesterol 7alpha-hydroxylase in HepG2 cells by 2,4,6-trihydroxyacetophenone
Eur. J. Pharmacol.
515
43-46
2005
Homo sapiens
Manually annotated by BRENDA team
Li, T.; Kong, X.; Owsley, E.; Ellis, E.; Strom, S.; Chiang, J.Y.
Insulin regulation of cholesterol 7alpha-hydroxylase expression in human hepatocytes: roles of forkhead box O1 and sterol regulatory element-binding protein 1c
J. Biol. Chem.
281
28745-28754
2006
Homo sapiens (P22680), Homo sapiens
Manually annotated by BRENDA team
Hubacek, J.A.; Bobkova, D.
Role of cholesterol 7alpha-hydroxylase (CYP7A1) in nutrigenetics and pharmacogenetics of cholesterol lowering
Mol. Diagn. Ther.
10
93-100
2006
Homo sapiens (P22680)
Manually annotated by BRENDA team
Lee, M.S.; Park, J.Y.; Freake, H.; Kwun, I.S.; Kim, Y.
Green tea catechin enhances cholesterol 7alpha-hydroxylase gene expression in HepG2 cells
Br. J. Nutr.
99
1182-1185
2008
Homo sapiens
Manually annotated by BRENDA team
Mitro, N.; Godio, C.; De Fabiani, E.; Scotti, E.; Galmozzi, A.; Gilardi, F.; Caruso, D.; Chacon, A.B.; Crestani, M.
Insights in the regulation of cholesterol 7alpha-hydroxylase gene reveal a target for modulating bile acid synthesis
Hepatology
46
885-897
2007
Homo sapiens (P22680)
Manually annotated by BRENDA team
Srivastava, A.; Pandey, S.N.; Choudhuri, G.; Mittal, B.
Role of genetic variant A-204C of cholesterol 7alpha-hydroxylase (CYP7A1) in susceptibility to gallbladder cancer
Mol. Genet. Metab.
94
83-89
2008
Homo sapiens
Manually annotated by BRENDA team
Gilardi, F.; Mitro, N.; Godio, C.; Scotti, E.; Caruso, D.; Crestani, M.; De Fabiani, E.
The pharmacological exploitation of cholesterol 7alpha-hydroxylase, the key enzyme in bile acid synthesis: from binding resins to chromatin remodelling to reduce plasma cholesterol
Pharmacol. Ther.
116
449-472
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Li, T.; Ma, H.; Park, Y.J.; Lee, Y.K.; Strom, S.; Moore, D.D.; Chiang, J.Y.
Forkhead box transcription factor O1 inhibits cholesterol 7alpha-hydroxylase in human hepatocytes and in high fat diet-fed mice
Biochim. Biophys. Acta
1791
991-996
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Han, S.; Chiang, J.Y.
Mechanism of vitamin D receptor inhibition of cholesterol 7alpha-hydroxylase gene transcription in human hepatocytes
Drug Metab. Dispos.
37
469-478
2009
Homo sapiens
Manually annotated by BRENDA team
Song, K.H.; Li, T.; Owsley, E.; Strom, S.; Chiang, J.Y.
Bile acids activate fibroblast growth factor 19 signaling in human hepatocytes to inhibit cholesterol 7alpha-hydroxylase gene expression
Hepatology
49
297-305
2009
Homo sapiens
Manually annotated by BRENDA team
Nass, N.; Schoeps, R.; Ulbrich-Hofmann, R.; Simm, A.; Hohndorf, L.; Schmelzer, C.; Raith, K.; Neubert, R.H.; Eder, K.
Screening for nutritive peptides that modify cholesterol 7alpha-hydroxylase expression
J. Agric. Food Chem.
56
4987-4994
2008
Homo sapiens
Manually annotated by BRENDA team
Kovar, J.; Lenicek, V.; Zimolova, M.; Vitek, L.; Jirsa, M.; Pitha, P.
Regulation of diurnal variation of cholesterol 7alpha-hydroxylase (CYP7A1) activity in healthy subjects
Physiol. Res.
59
233-238
2010
Homo sapiens
Manually annotated by BRENDA team
De Castro-Oros, I.; Pampin, S.; Cofan, M.; Mozas, P.; Pinto, X.; Salas-Salvado, J.; Rodriguez-Rey, J.C.; Ros, E.; Civeira, F.; Pocovi, M.
Promoter variant -204A>C of the cholesterol 7alpha-hydroxylase gene: Association with response to plant sterols in humans and increased transcriptional activity in transfected HepG2 cells
Clin. Nutr.
30
239-246
2010
Homo sapiens
Manually annotated by BRENDA team
Song, K.H.; Li, T.; Owsley, E.; Chiang, J.Y.
A putative role of micro RNA in regulation of cholesterol 7alpha-hydroxylase expression in human hepatocytes
J. Lipid Res.
51
2223-2233
2010
Homo sapiens
Manually annotated by BRENDA team
Li, T.; Chanda, D.; Zhang, Y.; -SikChoi, H.; Chiang, J.
Glucose stimulates cholesterol 7 alpha-hydroxylase gene transcription in human hepatocytes
J. Lipid Res.
51
832-842
2010
Homo sapiens
Manually annotated by BRENDA team
Michelini, E.; Donati, M.; Aldini, R.; Cevenini, L.; Mezzanotte, L.; Nardini, P.; Foschi, C.; Zvi, I.B.; Cevenini, M.; Montagnani, M.; Marangoni, A.; Roda, A.; Cevenini, R.
Dual-color bioluminescent assay using infected HepG2 cells sheds new light on Chlamydia pneumoniae and human cytomegalovirus effects on human cholesterol 7alpha-hydroxylase (CYP7A1) transcription
Anal. Biochem.
430
92-96
2012
Homo sapiens
Manually annotated by BRENDA team
Li, T.; Francl, J.M.; Boehme, S.; Chiang, J.Y.
Regulation of cholesterol and bile acid homeostasis by the cholesterol 7alpha-hydroxylase/steroid response element-binding protein 2/microRNA-33a axis in mice
Hepatology
58
1111-1121
2013
Homo sapiens, Rattus norvegicus (P18125)
Manually annotated by BRENDA team
Shinkyo, R.; Xu, L.; Tallman, K.A.; Cheng, Q.; Porter, N.A.; Guengerich, F.P.
Conversion of 7-dehydrocholesterol to 7-ketocholesterol is catalyzed by human cytochrome P450 7A1 and occurs by direct oxidation without an epoxide intermediate
J. Biol. Chem.
286
33021-33028
2011
Homo sapiens
Manually annotated by BRENDA team
Chow, E.C.; Magomedova, L.; Quach, H.P.; Patel, R.; Durk, M.R.; Fan, J.; Maeng, H.J.; Irondi, K.; Anakk, S.; Moore, D.D.; Cummins, C.L.; Pang, K.S.
Vitamin D receptor activation down-regulates the small heterodimer partner and increases CYP7A1 to lower cholesterol
Gastroenterology
146
1048-1059
2014
Homo sapiens (P22680), Homo sapiens, Mus musculus (Q64505), Mus musculus, Mus musculus C57BL/6 (Q64505)
Manually annotated by BRENDA team
Tempel, W.; Grabovec, I.; MacKenzie, F.; Dichenko, Y.V.; Usanov, S.A.; Gilep, A.A.; Park, H.W.; Strushkevich, N.
Structural characterization of human cholesterol 7alpha-hydroxylase
J. Lipid Res.
55
1925-1932
2014
Homo sapiens (P22680), Homo sapiens
Manually annotated by BRENDA team
Lammel Lindemann, J.A.; Angajala, A.; Engler, D.A.; Webb, P.; Ayers, S.D.
Thyroid hormone induction of human cholesterol 7 alpha-hydroxylase (Cyp7a1) in vitro
Mol. Cell. Endocrinol.
388
32-40
2014
Homo sapiens (P22680), Homo sapiens
Manually annotated by BRENDA team