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Information on EC 1.14.14.23 - cholesterol 7alpha-monooxygenase
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1.14.14.23 cholesterol 7alpha-monooxygenaseIUBMB 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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Word Map
- 1.14.14.23
- lipoprotein
- hepatocytes
- triglyceride
- biliary
- hmg-coa
-
farnesoid
-
fecal
-
low-density
- hypercholesterolemia
-
cholic
-
high-fat
-
chenodeoxycholic
-
3-hydroxy-3-methylglutaryl
- ba
- cyp8b1
- cholestyramine
-
enterohepatic
- cholestasis
- hdl
- gallstone
-
hypocholesterolemic
-
27-hydroxylase
- oxysterols
-
cholesteryl
- hmgcr
- cyp27a1
- taurocholate
-
cholesterol-lowering
-
hypolipidemic
-
ldl-cholesterol
-
acyl-coa:cholesterol
- 27-hydroxycholesterol
-
alpha-hydroxylation
-
lithogenic
-
ursodeoxycholic
-
lxralpha
-
hnf4alpha
- cyp3a11
- sult2a1
- 4alpha
-
cholesterogenesis
-
gut-liver
-
npc1l1
-
cholesterol-free
-
srebp2
-
ldl-receptor
-
c1-like
- medicine
- analysis
-
obeticholic
- cholestanol
-
guggulsterone
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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, cholesterol 7alpha hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bile acid-synthetic enzyme
C7alphaOH
cholesterol 7 alpha-hydroxylase
Cholesterol 7-alpha-hydroxylase
-
-
-
-
Cholesterol 7-alpha-monooxygenase
-
-
-
-
cholesterol 7alpha-hydroxylase
cholesterol-NADPH oxidoreductase, 7alpha-hydroxylating
CYP7A1
CYPVII
-
-
-
-
EC 1.14.13.17
-
-
formerly
-
oxygenase, cholesterol 7alpha-mono-
-
-
-
-
cholesterol 7alpha-hydroxylase
-
-
-
-
cholesterol 7alpha-hydroxylase
-
-
CYP7A1
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cholesterol + [reduced NADPH-hemoprotein reductase] + O2 = 7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9037-53-0
-
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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
25-hydroxycholesterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
27-hydroxycholesterol + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
5alpha-cholestan-3beta-ol + NADPH + O2
5alpha-cholestan-3beta,7alpha-diol + NADP+ + H2O
-
-
-
?
7-dehydrocholesterol + NADPH + H+
7-oxocholesterol + NADP+ + H2O
-
-
minor product: 7alpha,8alpha-epoxide, reaction with 7-[2H1]dehydrocholesterol yields complete migration of deuterium in the product 7-oxocholesterol. Minor product: 7alpha8alpha-epoxide
-
?
cholest-4-en-3-one + [reduced NADPH-hemoprotein reductase] + O2
?
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
lathosterol + NADPH + H+
7-oxocholestanol + cholestanol-7alpha,8alpha-epoxide + NADP+ + H2O
-
i.e. DELTA-dihydro-7-dehydrocholesterol
about 1:2 ratio of 7-oxo and epoxide products, the epoxide does not rearrange to the ketone
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
the gene encoding CYP7A1 is tightly regulated in order to control intrahepatic cholesterol and bile acid levels, ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression, bile acids regulate CYP7A1 via small heterodimer partner and liver receptor homolog-1, drugs repress chicken hepatic nuclear factor 4alpha transcript levels concomitant with a reduction in CYP7A1 expression, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting enzyme in the classical pathway of bile acid synthesis
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
CYP7A1 is a rate-limiting enzyme in bile acid synthesis and therefore plays an important role in maintaining cholesterol homeostasis, cholesterol metabolism, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first and rate-limiting step in the neutral pathway of cholesterol metabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
insulin, forkhead box O1, and sterol regulatory element-binding protein 1c are involved in regulation of expression of gene CYP7A1, genetic mechanism, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
stereospecific hydroxylation of cholesterol
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting enzyme in the classical pathway of bile acid synthesis
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
hydroxylation of cholesterol with strict regio- and stereoselectivity, inert towards other sterols and intermediates in conversion of cholesterol to bile acids
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting enzyme in cholesterol conversion to bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in bile acid biosynthesis in liver
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting enzyme in cholesterol conversion to bile acids
-
-
?
additional information
?
-
-
the cholesterol 7alpha-hydroxylase is critical in bile acid and cholesterol metabolism, polymorphisms of CP7A1 are of no physiologic significance, overview
-
-
?
additional information
?
-
substrate spcecificity and recognition structure, CYP7A1 can bind and hydroxylate cholesterol and cholest-4-en-3-one with high efficiency as well as oxysterols, overview. Cholest-4-en-3-one bound parallel to the heme with the alpha-side of the steroid nucleus facing the heme plane at a distance of about 3.5 A, substrate binding strutcure, detailed overview
-
-
?
additional information
?
-
-
substrate spcecificity and recognition structure, CYP7A1 can bind and hydroxylate cholesterol and cholest-4-en-3-one with high efficiency as well as oxysterols, overview. Cholest-4-en-3-one bound parallel to the heme with the alpha-side of the steroid nucleus facing the heme plane at a distance of about 3.5 A, substrate binding strutcure, detailed overview
-
-
?
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
?
-
-
specificity of reconstituted enzyme system
-
-
?
additional information
?
-
-
specificity of reconstituted enzyme system
-
-
?
additional information
?
-
-
specificity of reconstituted enzyme system
-
-
?
additional information
?
-
-
specificity of reconstituted enzyme system
-
-
?
additional information
?
-
-
the sex difference in plasma cholesterol content diminishes after ovariectomy, hypercholesterolemia is more severe in the female than in the male Nagase analbuminemic rats, molecular mechanism
-
-
?
additional information
?
-
-
TGFbeta stimulates rat Cyp7a1 reporter activity. Smad3, FoxO1 and HNF4alpha synergistically stimulate rat Cyp7a1 gene transcription. TNFalpha and cJun attenuate TGFbeta1 stimulation of rat Cyp7a1
-
-
?
additional information
?
-
-
the sex difference in plasma cholesterol content diminishes after ovariectomy, hypercholesterolemia is more severe in the female than in the male Nagase analbuminemic rats, molecular mechanism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
7-dehydrocholesterol + NADPH + H+
7-oxocholesterol + NADP+ + H2O
-
-
minor product: 7alpha,8alpha-epoxide
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
lathosterol + NADPH + H+
7-oxocholestanol + cholestanol-7alpha,8alpha-epoxide + NADP+ + H2O
-
i.e. DELTA-dihydro-7-dehydrocholesterol
about 1:2 ratio of 7-oxo and epoxide products, the epoxide does not rearrange to the ketone
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
the gene encoding CYP7A1 is tightly regulated in order to control intrahepatic cholesterol and bile acid levels, ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression, bile acids regulate CYP7A1 via small heterodimer partner and liver receptor homolog-1, drugs repress chicken hepatic nuclear factor 4alpha transcript levels concomitant with a reduction in CYP7A1 expression, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting enzyme in the classical pathway of bile acid synthesis
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
CYP7A1 is a rate-limiting enzyme in bile acid synthesis and therefore plays an important role in maintaining cholesterol homeostasis, cholesterol metabolism, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first and rate-limiting step in the neutral pathway of cholesterol metabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
insulin, forkhead box O1, and sterol regulatory element-binding protein 1c are involved in regulation of expression of gene CYP7A1, genetic mechanism, overview
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting enzyme in the classical pathway of bile acid synthesis
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting step in bile acid formation
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
first step of cholesterol catabolism, rate-limiting and major regulatory enzyme in the synthesis of bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting enzyme in cholesterol conversion to bile acids
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
the enzyme is involved in bile acid biosynthesis in liver
-
-
?
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
rate-limiting enzyme in cholesterol conversion to bile acids
-
-
?
additional information
?
-
-
the cholesterol 7alpha-hydroxylase is critical in bile acid and cholesterol metabolism, polymorphisms of CP7A1 are of no physiologic significance, overview
-
-
?
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 sex difference in plasma cholesterol content diminishes after ovariectomy, hypercholesterolemia is more severe in the female than in the male Nagase analbuminemic rats, molecular mechanism
-
-
?
additional information
?
-
-
TGFbeta stimulates rat Cyp7a1 reporter activity. Smad3, FoxO1 and HNF4alpha synergistically stimulate rat Cyp7a1 gene transcription. TNFalpha and cJun attenuate TGFbeta1 stimulation of rat Cyp7a1
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-
?
additional information
?
-
-
the sex difference in plasma cholesterol content diminishes after ovariectomy, hypercholesterolemia is more severe in the female than in the male Nagase analbuminemic rats, molecular mechanism
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b5
-
essential component of the cholesterol 7alpha-hydroxylase system
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bile acid
-
feedback inhibition preventing the accumulation of cytotoxic hydrophobic bile acids
additional information
ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression, molecular mechanisms underlying CYP7A1 inhibition, drugs repress chicken hepatic nuclear factor 4alpha transcript levels concomitant with a reduction in CYP7A1 expression
-
additional information
-
ligands of the xenobiotic-sensing pregnane X receptor inhibit CYP7A1 expression, molecular mechanisms underlying CYP7A1 inhibition, drugs repress chicken hepatic nuclear factor 4alpha transcript levels concomitant with a reduction in CYP7A1 expression
-
additional information
mechanism of insulin regulation of CYP7A1 gene expression in human hepatocytes, physiological concentrations of insulin rapidly stimulate CYP7A1 mRNA expression in primary human hepatocytes but inhibit CYP7A1 expression after extended treatment, forkhead box O1 and sterol regulatory element-binding protein 1c are involved, overview
-
additional information
-
mechanism of insulin regulation of CYP7A1 gene expression in human hepatocytes, physiological concentrations of insulin rapidly stimulate CYP7A1 mRNA expression in primary human hepatocytes but inhibit CYP7A1 expression after extended treatment, forkhead box O1 and sterol regulatory element-binding protein 1c are involved, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
Thiol-containing substances
-
e.g. mercaptoethanol, dithiothreitol or cysteamine enhance activity
-
additional information
enzyme expression is induced by cholesterol, bile acids, cytokines, steroid hormones, and thyroid hormone
-
additional information
-
a protein purified from rat liver cytosol with minumum molecular weight of 25000 stimulates cholesterol 7alpha-hydroxylase activity in presence of glutathione or thioredoxin
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
-
enzyme activity depends on circadian rhythm, minimum activity at 2 p.m.
0.001
-
enzyme activity depends on circadian rhythm, maximum activity at 10 p.m.
0.00294
-
after incubation with 5 units cAMP-dependent protein kinase for 30 min
0.00315
-
after incubation with 5 units cAMP-dependent protein kinase for 30 min
additional information
additional information
-
enzyme activity during liver regeneration after hepatectomy, 7alpha-hydroxylase activities recover after day 3 and are not reduced on days 3, 5, or 7 compared to those of sham-operated rats
additional information
-
enzyme activity in rats of different strains and with different sexes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
golden syrian hamster, 3fold higher activity in males compared to females
-
-
brenda
wild-type C57Bl/6 and male Cyp8b1 knockout mice on a mixed 129Sv/Ev-C57Bl/6 background
-
-
brenda
enzyme complex reconstituted from cytochrome P-450, NADPH-cytochrome P-450 reductase
-
-
brenda
-
285296, 285297, 285298, 285299, 285300, 285302, 285303, 285304, 285305, 285306, 285307, 285308, 285312, 659806, 659809, 686834, 687259, 688228, 695473, 699703, 700572
-
-
brenda
enzyme complex reconstituted from cytochrome P-450 and NADPH-cytochrome P-450 reductase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Mycobacterium smegmatis can grow on cholesterol as the sole carbon source
brenda
-
HepG2 cell transformed with a cyp7alpha-reporter gene (promoter fragment fused to firefly luciferase)
brenda
additional information
enzyme expression analysis, increased levels of Cyp7a1/CYP7A1 mRNA in human hepatocytes treated with 1alpha,25-dihydroxyvitamin D3
brenda
-
different catechins, (-)-epicatechin gallate, (-)-epigallocatechin-3-gallate, (-)-epigallocatechin and (-)-epicatechin, up-regulates the CYP7A1 mRNA level by 5.5-, 4.2-, 2.9- and 1.9-fold, respectively, compared with the control
brenda
importance of histone deacetylases in the feedback regulation of CYP7A1 transcription
brenda
-
HepG2 cell transformed with a cyp7alpha-reporter gene (promoter fragment fused to firefly luciferase)
brenda
primary, CYP7A1 expression analysis in absence or presence of isnulin
brenda
-
wheat antioxidants significantly up-regulate the mRNA of cholesterol 7alpha-hydroxylase, the key enzyme for cholesterol metabolism, in primary rat hepatocytes
brenda
-
-
brenda
-
Cyp7a1 expression pattern in wild-type and Cyp8b1 null mice livers, Cyp7a1 expression in wild type mice shows a zonal distribution pattern, Cyp8b1 knockout mice show increased expression of Cyp7a1, overview
brenda
expression profile of the Cyp7a transcript in wild-type mice shows a strong circadian rhythm in both the 12L:12D light-dark cycle and constant darkness. In Clock/Clock mutant mice expression profile of the Cyp7a transcript also exhibits a circadian rhythm at an enhanced level with a lower amplitude, although its protein level becomes arrhythmic at a high level. Active CLOCK is essential for the robust circadian expression of Cyp7a. Clock-controlled genes - DBP, DEC2, and REV-ERBalpha/beta are direct regulators required for the robust circadian rhythm of Cyp7a. The circadian rhythm of Cyp7a is regulated by multiple transcription factors, including DBP, REV-ERBalpha/beta, LXRalpha, HNF4alpha DEC2, E4BP4, and PPARalpha
brenda
distribution of vitamin D receptor and enzyme proteins in the liver by immunostaining, overview
brenda
-
distribution of vitamin D receptor and enzyme proteins in the liver by immunostaining, overview
-
brenda
-
-
285296, 285297, 285298, 285300, 285302, 285303, 285304, 285305, 285306, 285307, 285308, 285309, 285314, 659666, 695473, 699703, 700572, 712117
brenda
-
enzyme activity during liver regeneration after hepatectomy, 7alpha-hydroxylase activities recover after day 3 and are not reduced on days 3, 5, or 7 compared to those of sham-operated rats
brenda
-
chlorella powder or cholesterol + bile acid increases enzyme activity significantly
brenda
-
the cyp7A1 gene plays an important role in development of hypercholesterolemia in PHHC rats
brenda
-
effects of gender on hepatic enzyme activity, overview
-
brenda
additional information
enzyme expression analysis in mice fed normal or Western diets for 3 weeks and then given intraperitoneal injections of vehicle (corn oil) or 1alpha,25-dihydroxyvitamin D3 in 4 doses of 0.0025 mg/kg, every other day. Increased levels of Cyp7a1/CYP7A1 mRNA in mouse hepatocytes treated with 1alpha,25-dihydroxyvitamin D3
brenda
additional information
-
enzyme expression analysis in mice fed normal or Western diets for 3 weeks and then given intraperitoneal injections of vehicle (corn oil) or 1alpha,25-dihydroxyvitamin D3 in 4 doses of 0.0025 mg/kg, every other day. Increased levels of Cyp7a1/CYP7A1 mRNA in mouse hepatocytes treated with 1alpha,25-dihydroxyvitamin D3
brenda
additional information
-
enzyme expression analysis in mice fed normal or Western diets for 3 weeks and then given intraperitoneal injections of vehicle (corn oil) or 1alpha,25-dihydroxyvitamin D3 in 4 doses of 0.0025 mg/kg, every other day. Increased levels of Cyp7a1/CYP7A1 mRNA in mouse hepatocytes treated with 1alpha,25-dihydroxyvitamin D3
-
brenda
additional information
-
enzyme activity in rats of different strains and with different sexes, the enzyme is upregulated in both female and male Nagase analbuminemic rats compared to Sprague-Dawley rats, overview
brenda
additional information
-
Cyp7a1 and the bile acid pool size are increased 2-3fold in lactating postpartum rats, the regulatory mechanism functions via altered interaction of nuclear receptors with the Cyp7a1 proximal promoter and altered expression of regulatory signaling pathways in postpartum rats at day 10
brenda
additional information
-
enzyme activity in rats of different strains and with different sexes, the enzyme is upregulated in both female and male Nagase analbuminemic rats compared to Sprague-Dawley rats, overview
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
heat shock factor-1 ablation not only eliminates heat shock response, but it also transcriptionally upregulates CYP7A1 and MDR1/P-gp axis in atherogenic western diet-diet fed HSF-1 and low density lipoproteins receptor double knock out mice to reduce atherosclerosis
metabolism
physiological function
additional information
metabolism
-
cholesterol 7alpha-hydroxylase, Cyp7a1, catalyzes the rate-limiting step of the classical pathway of bile acid synthesis and is the major mechanism for cholesterol catabolism and removal from the body. Cyp7a1 regulation, detailed overview
metabolism
-
the phosphorylation status of CYP7A1 chromatin is important in CYP7A1 regulation, overview
metabolism
bile acids such as chenodeoxycholic acid (CDCA) activate farnesoid X receptor FXR to increase transcription of small heterodimer partner SHP, an atypical nuclear receptor that lacks a DNA binding domain and represses CYP7A1 activation by suppression of transcription factors, liver receptor homolog-1 (NR5A2) and hepatocyte nuclear factor 4a (NR2A1), which are essential for CYP7A1 expression. A second negative feedback mechanism on CYP7A1 is found in the intestine, where activation of FXR induces fibroblast growth factor 15/19, a hormonal signaling molecule that represses CYP7A1 through interaction with the liver fibroblast growth factor receptor 4 via the c-Jun signaling pathway. Role for the vitamin D receptor on CYP7A1 regulation, overview
metabolism
bile acids such as chenodeoxycholic acid (CDCA) activate farnesoid X receptor FXR to increase transcription of small heterodimer partner SHP, an atypical nuclear receptor that lacks a DNA binding domain and represses CYP7A1 activation by suppression of transcription factors, liver receptor homolog-1 (NR5A2) and hepatocyte nuclear factor 4a (NR2A1), which are essential for CYP7A1 expression. A second negative feedback mechanism on CYP7A1 is found in the intestine, where activation of FXR induces fibroblast growth factor 15/19, a hormonal signaling molecule that represses CYP7A1 through interaction with the liver fibroblast growth factor receptor 4 via the c-Jun signaling pathway. Role for the vitamin D receptor on CYP7A1 regulation, overview
metabolism
Cyp7a1 is a bile acid-synthetic enzyme suppressed by FXR signaling in both liver and intestine in mice, bile acid profiling in untreated and bile acid-treated liver and intestine, overview
metabolism
hepatic conversion to bile acids is a major elimination route for cholesterol in mammals. CYP7A1 catalyzes the first and rate-limiting step in classic bile acid biosynthesis, converting cholesterol to 7alpha-hydroxycholesterol. Hydroxylation of the ring system of cholesterol in a regio- and stereospecific manner with further oxidation and shortening of the side chain produces water-soluble bile acids with powerful detergent properties to emulsify dietary lipids. Bile acids also serve as signaling molecules that bind to G-protein-coupled receptors and nuclear hormone receptors that regulate lipid, glucose, and energy metabolism
metabolism
HSF-1 deletion reduces atherosclerosis and enhances dietary cholesterol metabolism, by not only inducing hepatic MDR1/Pgp but also by enhancing CYP7A1 gene expression in the liver. HSF-1 is a metabolic regulator of dietary cholesterol
metabolism
-
Cyp7a1 is a bile acid-synthetic enzyme suppressed by FXR signaling in both liver and intestine in mice, bile acid profiling in untreated and bile acid-treated liver and intestine, overview
-
metabolism
-
bile acids such as chenodeoxycholic acid (CDCA) activate farnesoid X receptor FXR to increase transcription of small heterodimer partner SHP, an atypical nuclear receptor that lacks a DNA binding domain and represses CYP7A1 activation by suppression of transcription factors, liver receptor homolog-1 (NR5A2) and hepatocyte nuclear factor 4a (NR2A1), which are essential for CYP7A1 expression. A second negative feedback mechanism on CYP7A1 is found in the intestine, where activation of FXR induces fibroblast growth factor 15/19, a hormonal signaling molecule that represses CYP7A1 through interaction with the liver fibroblast growth factor receptor 4 via the c-Jun signaling pathway. Role for the vitamin D receptor on CYP7A1 regulation, overview
-
physiological function
-
cholesterol 7 alpha-hydroxylase plays a critical role in regulation of bile acid synthesis in the liver
physiological function
-
cholesterol 7alpha-hydroxylase is the rate-limiting enzyme in the bile acid biosynthetic pathway that converts cholesterol into bile acids in the liver. Bile acids play an important role in maintaining lipid, glucose, and energy homeostasis
physiological function
-
regulation of Cyp7a1 expression is critical for maintenance of cholesterol and bile acid homeostasis
physiological function
CYP7A1 overexpression in transgenic mice leads to marked activation of the steroid response element-binding protein 2-regulated cholesterol metabolic network and absence of bile acid repression of lipogenic gene expression in livers. Cyp7a1-tg mice show significantly elevated hepatic cholesterol synthesis rates, but reduced hepatic fatty acid synthesis rates, which is accompanied by increased 14C-glucose-derived acetyl-coenzyme A incorporation into sterols for fecal excret
physiological function
transgenic mice overexpressing rat enzyme have 2fold higher isoform Cyp7a1 activity and bile acid pool than wild type mice. Gallbladder bile acid composition changes from predominantly cholic acid in wild type to chenodeoxycholic acid in trangenic mice. Transgenic mice have higher biliary and fecal cholesterol and bile acid secretion rates than wild type mice. Hepatic de novo cholesterol synthesis is markedly induced in trangenic mice but intestine fractional cholesterol absorption remains the same as wild type mice despite increased intestine bile acids. Hepatic but not intestinal expression of cholesterol transporters such as ABCG5/G8, SRB1 and bile acid transporters such as ABCB11 are significantly induced in transgenic mice
physiological function
-
CYP7A1 overexpression leads to marked activation of the steroid response elementbinding protein 2-regulated cholesterol metabolic network and absence of bile acid repression of lipogenic gene expression in livers
physiological function
heat shock factor-1 knockout enhances cholesterol 7alpha hydroxylase (CYP7A1) and multidrug transporter (MDR1) gene expressions to attenuate atherosclerosis
physiological function
hepatic conversion to bile acids is a major elimination route for cholesterol in mammals. CYP7A1 catalyzes the first and rate-limiting step in classic bile acid biosynthesis, converting cholesterol to 7alpha-hydroxycholesterol
physiological function
thyroid hormone modulates serum cholesterol by acting on thyroid hormone receptor beta1 in liver to regulate metabolic gene sets. One important thyroid hormone regulated step involves induction of Cyp7a1, an enzyme in the cytochrome P450 family, which enhances cholesterol to bile acid conversion and plays a crucial role in regulation of serum cholesterol levels
physiological function
-
utilization of cholesterol is initiated by three cholesterol hydroxylases, CYP125A3, CYP142A2, and CYP125A4. A CYP125A3/CYP142A2 double knockout mutant of Mycobacterium smegmatis is still able to grow on cholesterol as sole carbom source, albeit at a slower rate than the wild-type
physiological function
-
cholesterol 7alpha-hydroxylase is the rate-limiting enzyme in the bile acid biosynthetic pathway that converts cholesterol into bile acids in the liver. Bile acids play an important role in maintaining lipid, glucose, and energy homeostasis
-
additional information
-
high glucose stimulates bile acid synthesis and induces mRNA expression of cholesterol 7 alpha-hydroxylase, the key regulatory gene in bile acid synthesis. Glucose decreases H3K9 methylation in CYP7A1 chromatin. Knockdown of ATP-citrate lyase, which converts citrate to acetyl-CoA, decreases histone acetylation, and attenuates glucose induction of CYP7A1 mRNA expression
additional information
-
lipid responses of 67 subjects of different promoter variants -204A > C, 31 AA and 36 AC+ CC, to plant sterols, overview. Compared to AA-subjects, C-carriers show significantly higher adjusted mean reductions in total cholesterol and increases in lathosterol-to-cholesterol ratios
additional information
-
transgenic mice overexpressing Cyp7a1 in the liver are resistant to high-fat diet-induced obesity, fatty liver, and insulin resistance. Cyp7a1-tg mice show increased hepatic cholesterol catabolism and an increased bile acid pool, they have increased secretion of hepatic very low density lipoprotein but maintained plasma triglyceride homeostasis, phenotype, overview
additional information
activation of the vitamin D receptor represses hepatic SHP to increase levels of human CYP7A1 and reduce cholesterol
additional information
-
activation of the vitamin D receptor represses hepatic SHP to increase levels of human CYP7A1 and reduce cholesterol
additional information
identification of a motif of residues that promote cholest-4-en-3-one binding parallel to the heme, thus positioning the C7 atom for hydroxylation. Orientation of cholesterol in the different leaflets of the lipid bilayer can be recognized for further binding by CYP7A1 alone or in complex with protein partners
additional information
-
identification of a motif of residues that promote cholest-4-en-3-one binding parallel to the heme, thus positioning the C7 atom for hydroxylation. Orientation of cholesterol in the different leaflets of the lipid bilayer can be recognized for further binding by CYP7A1 alone or in complex with protein partners
additional information
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. Activation of the vitamin D receptor represses hepatic SHP to increase levels of mouse CYP7A1 and reduce cholesterol
additional information
-
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. Activation of the vitamin D receptor represses hepatic SHP to increase levels of mouse CYP7A1 and reduce cholesterol
additional information
-
the ability of CYP125A4 to oxidize 7alpha-hydroxycholesterol is due, at least in part, to the presence of a smaller amino acid side chain facing C-7 of the sterol substrate than in CYP125A3
additional information
thyroid hormones regulate cholesterol to bile acid conversion in similar ways in humans and rodent experimental models
additional information
-
thyroid hormones regulate cholesterol to bile acid conversion in similar ways in humans and rodent experimental models
additional information
-
transgenic mice overexpressing Cyp7a1 in the liver are resistant to high-fat diet-induced obesity, fatty liver, and insulin resistance. Cyp7a1-tg mice show increased hepatic cholesterol catabolism and an increased bile acid pool, they have increased secretion of hepatic very low density lipoprotein but maintained plasma triglyceride homeostasis, phenotype, overview
-
additional information
-
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. Activation of the vitamin D receptor represses hepatic SHP to increase levels of mouse CYP7A1 and reduce cholesterol
-
Show AA Sequence and Transmembrane Helices (808 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
58000
additional information
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the enzyme is phosphorylated at multiple amino acids, overview
side-chain modification
side-chain modification
-
enzyme activity decreases after dephosphorylation with alkaline phosphatase and increases after phosphorylation with cAMP-dependent protein kinase
side-chain modification
-
enzyme activity decreases after dephosphorylation with alkaline phosphatase and increases after phosphorylation with cAMP-dependent protein kinase
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
additional information
additional information
genotyping and frequency of polymorphisms in human populations, overview
additional information
-
naturally occuring polymorphisms of gene CYP7AI are C203A and T469C in the promoter region, and IVS6 + G363A in the 3'-end of the gene, the genetic variants are of no physiologic importance
additional information
-
naturally occuring promoter variant -204A > C (rs3808607) of the CYP7A1 gene, genotyping, functionality of the -204A > C variant, electrophoretic mobility gel shift assays, overview. The C-construct causes a 78% promoter activity increase and gel-shift assays howed lower affinity for nuclear transcription factors, while in silico experiments predict a binding site for inhibitory nuclear factors RXR-CAR
additional information
-
construction of Cyp7a1-tg mice overexpressing rat Cyp7a1, phenotype, overview
additional information
generation of a mutant CYP7A1 promoter luciferase construct with deletion of putative HSE binding site for HSF-1, in the CYP7A1 promoter region (-922 to -901) and determination of luciferase activity in the hepatocytes
additional information
-
construction of Cyp7a1-tg mice overexpressing rat Cyp7a1, phenotype, overview
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation upon incubating microsomes with NADPH, half-life: 1 h, addition of dithiothreitol partially protects against inactivation
rapid inactivation upon incubating microsomes with NADPH, half-life: 1 h, addition of dithiothreitol partially protects against inactivation
-
rapid inactivation upon incubating microsomes with NADPH, half-life: 1 h, addition of dithiothreitol partially protects against inactivation
-
rapid inactivation upon incubating microsomes with NADPH, half-life: 1 h, addition of dithiothreitol partially protects against inactivation
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cyp7a1-tg mice overexpressing rat Cyp7a1 complementary DNA under an ApoE3 hepatic control region
expression in Escherichia coli
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, DNA sequence determination and analysis, phylogenetic tree, expression analysis and regulation, overview
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, genotyping, overview. Expression of promoter constructs in HepG2 cells
-
mutant Cyp7A1 promoter fragment cloned luciferase construct is generated using wild-type CYP7A1 promoter cloned luciferase, the gene contains a HSF-1 binding site in the CYP7A1 promoter region, oligonucleotides corresponding to -922 to -901 bases
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activation of an AMP-activated protein kinase decreases CYP7A1 mRNA, hepatocyte nuclear factor 4alpha protein, and binding to CYP7A1 chromatin
-
apobec-1 knock-out mice show a decrease in cholesterol 7alpha-hydroxylase mRNA
atorvastatin induces enzyme Cyp7a1 by suppressing FXR signaling in both liver and intestine. Atorvastatin suppresses the expression of bile acid nuclear receptor farnesoid X receptor (FXR) target genes, namely small heterodimer partner (liver) and fibroblast growth factor 15 (ileum). Atorvastatin increases the mRNAs of the organic cation uptake transporter 1 and cholesterol efflux transporters Abcg5 and Abcg8 in the liver
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 is a direct thyroid hormone target gene that responds to physiologic thyroid hormone levels through a set of distinct response elements in its promoter
CYP7A1 mRNAs have very short half-lives, and bile acids destabilize CYP7A1 mRNA via the 3'-untranslated region
-
CYP7A1 protein expression in chronic hypothyroid rats is significantly decreased
-
expression is strongly repressed after 70% partial hepatectomy (during liver regeneration)
-
fibroblast growth factor 19 inhibits cholesterol 7alpha-hydroxylase mRNA expression
-
Forkhead box transcription factor O1 inhibits cholesterol 7alpha-hydroxylase mRNA expression
-
Forkhead box transcription factor O1 inhibits cholesterol 7alpha-hydroxylase mRNA expression in livers of high fat diet-fed mice
-
heat shock factor-1 knockout enhances cholesterol 7alpha hydroxylase (CYP7A1) and multidrug transporter (MDR1) gene expressions to attenuate atherosclerosis
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
-
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
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
increase in cholesterol 7alpha-hydroxylase mRNA expression at 16 h (10 h of light) demonstrates a shift in the diurnal rhythm at day 10 postpartum
-
lithocholic acid-acetate and 1alpha,25-dihydroxy-vitamin D3 inhibit cholesterol 7alpha-hydroxylase mRNA expression
-
postpartum: increase in mRNA and protein levels of cholesterol 7alpha-hydroxylase
-
rodent Cyp7a1 expression increases in response to cholesterol-enriched diets, resulting in increased bile acid synthesis
-
several negative feedback loops within the liver and small intestine down-regulate Cyp7a1 transcription to prevent accumulation of bile acids to toxic levels. The the JNK/c-Jun pathway is involved in downregulation of Cyp7a1, overview
-
several nutritive peptides inhibit luciferase expression (cyp7alpha-reporter gene (promoter fragment fused to firefly luciferase))
-
significant increase in Cyp7a1 levels in neonatal hamsters is due to mechanisms independent of the FXR and SHP pathway and cortisol. Precocious expression of Cyp7a1 can not be induced in neonatal hamsters with dexamethasone
-
the amount of methionine and cystine in a diet affects cholesterol 7 alpha-hydroxylase activity
-
upregulation of CYP7A1 mRNA in hypercholesterolemic rats treated with extracts from steamed and dried roots of Panax ginseng C.A. Meyer, and upregulation of CYP7A1 mRNA and protein levels by the addition of ginsenosides Ro, Rg3, Re, Rg1, and Rg2 to rat primary hepatocytes
-
atorvastatin induces enzyme Cyp7a1 by suppressing FXR signaling in both liver and intestine. Atorvastatin suppresses the expression of bile acid nuclear receptor farnesoid X receptor (FXR) target genes, namely small heterodimer partner (liver) and fibroblast growth factor 15 (ileum). Atorvastatin increases the mRNAs of the organic cation uptake transporter 1 and cholesterol efflux transporters Abcg5 and Abcg8 in the liver
atorvastatin induces enzyme Cyp7a1 by suppressing FXR signaling in both liver and intestine. Atorvastatin suppresses the expression of bile acid nuclear receptor farnesoid X receptor (FXR) target genes, namely small heterodimer partner (liver) and fibroblast growth factor 15 (ileum). Atorvastatin increases the mRNAs of the organic cation uptake transporter 1 and cholesterol efflux transporters Abcg5 and Abcg8 in the liver
-
-
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
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
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
medicine
-
association of CYP7A1 gene polymorphisms with the risk of gallbladder cancer. This polymorphism plays a significant role in the pathogenesis of gallbladder cancer which is causatively related to depressed bile acid production. The proposed tumorigenic mechanism for gallbladder cancer is independent of gallstone pathway and appears to be mediated by increase in concentration and accumulation of toxic substances in gallbladder, generated in liver as a consequence of lipid peroxidation and other catabolic reactions
medicine
-
polymorphisms/mutations described so far at the CYP7A1 promoter do not impair enzyme activity and most likely do not contribute directly to hypercholesterolemia and/or increased cardiovascular risk
medicine
-
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
medicine
CYP7A1 overexpression in transgenic mice leads to marked activation of the steroid response element-binding protein 2-regulated cholesterol metabolic network and absence of bile acid repression of lipogenic gene expression in livers. Cyp7a1-tg mice show significantly elevated hepatic cholesterol synthesis rates, but reduced hepatic fatty acid synthesis rates, which is accompanied by increased 14C-glucose-derived acetyl-coenzyme A incorporation into sterols for fecal excret
medicine
-
in inborn error of metabolism known as Smith-Lemli-Opitz syndrome, 7-oxocholesterol levels may also be elevated in tissue and fluids as a result of CYP7A1 oxidation of 7-dehydrocholesterol
medicine
-
upregulation of CYP7A1 mRNA in hypercholesterolemic rats treated with extracts from steamed and dried roots of Panax ginseng C.A. Meyer. Treatment leads to decreased ratios of low-density lipoprotein-cholesterol to high-density lipoprotein-cholesterol. In-vitro studies also show the upregulation of CYP7A1 mRNA and protein levels by the addition of ginsenosides Ro, Rg3, Re, Rg1, and Rg2 to rat primary hepatocytes
medicine
manipulation of hormone signaling pathways can provide a strategy to enhance Cyp7a1 activity in human patients
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mitton, J.R.; Scholan, N.A.; Boyd, G.S.
The oxidation of cholesterol in rat liver sub-cellular particles. The cholesterol-7-alpha-hydroxylase enzyme system
Eur. J. Biochem.
20
569-579
1971
Rattus norvegicus
brenda
Boyd, G.S.; Grimwade, A.M.; Lawson, M.E.
Studies on rat-liver microsomal cholesterol 7alpha-hydroxylase
Eur. J. Biochem.
37
334-340
1973
Rattus norvegicus
brenda
Rush, W.R.; Gibson, G.G.; Parke, D.V.
The purification and reconstitution of cytochrome P-450-dependent cholesterol 7alpha-hydroxylase activity from rat liver microsomal fractions
Biochem. Soc. Trans.
8
102-103
1980
Rattus norvegicus
brenda
Van Cantfort, J.; Gielen, J.
Cholesterol 7alpha-hydroxylase. 2. Biochemical properties and participation of endogenous cholesterol in the assay in vitro
Eur. J. Biochem.
55
33-40
1975
Rattus norvegicus
brenda
Andersson, S.; Bostrm, H.; Danielsson, H.; Wikvall, K.
Purification from rabbit and rat liver of cytochromes P-450 involved in bile acid biosynthesis
Methods Enzymol.
111
364-377
1985
Rattus norvegicus
brenda
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
brenda
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
brenda
Kalles, I.; Wikvall, K.
Role of sulfhydryl groups in catalytic activity of purified cholesterol 7alpha-hydroxylase system from rabbit and rat liver microsomes
Biochem. Biophys. Res. Commun.
100
1361-1369
1981
Oryctolagus cuniculus, Rattus norvegicus
brenda
Waxman, D.J.
Rat hepatic cholesterol 7alpha-hydroxylase: biochemical properties and comparison to constitutive and xenobiotic-inducible cytochrome P-450 enzymes
Arch. Biochem. Biophys.
247
335-345
1986
Rattus norvegicus
brenda
Chiang, J.Y.L.; Miller, W.F.; Lin, G.M.
Regulation of cholesterol 7alpha-hydroxylase in the liver. Purification of cholesterol 7alpha-hydroxylase and the immunochemical evidence for the induction of cholesterol 7alpha-hydroxylase by cholestyramine and circadian rhythm
J. Biol. Chem.
265
3889-3897
1990
Rattus norvegicus
brenda
Suckling, K.E.; Jackson, B.; Suffolk, R.A.; Houghton, J.D.; Suckling, C.J.
Effects of 6,6-difluorocholestanol and 7,7-difluorocholestanol on hepatic enzymes of cholesterol metabolism
Biochim. Biophys. Acta
1002
401-404
1989
Rattus norvegicus
brenda
Ogishima, T.; Deguchi, S.; Okuda, K.
Purification and characterization of cholesterol 7alpha-hydroxylase from rat liver microsomes
J. Biol. Chem.
262
7646-7650
1987
Rattus norvegicus
brenda
Danielsson, H.; Kalles, I.; Wikvall, K.
Regulation of hydroxylations in biosynthesis of bile acids. Isolation of a protein from rat liver cytosol stimulating reconstituted cholesterol 7alpha-hydroxylase activity
J. Biol. Chem.
259
4258-4262
1984
Rattus norvegicus
brenda
Ozasa, S.; Boyd, G.S.
Cholesterol 7alpha-hydroxylase of rat liver. Studies on the solubilisation, resolution and reconstitution of the enzyme complex
Eur. J. Biochem.
119
263-272
1981
Rattus norvegicus
brenda
Hansson, R.; Wikvall, K.
Properties of reconstituted cholesterol 7alpha-hydroxylase system from rat and rabbit liver microsomes
Eur. J. Biochem.
93
419-426
1979
Oryctolagus cuniculus, Rattus norvegicus
brenda
Miki, N.; Miura, R.; Miyake, Y.
Purification and characterization of cholesterol 7alpha-hydroxylase cytochrome P-450 of untreated rabbit liver microsomes
J. Biochem.
101
1087-1094
1987
Oryctolagus cuniculus
brenda
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
brenda
Souidi, M.; Parquet, M.; Ferezou, J.; Lutton, C.
Modulation of cholesterol 7alpha-hydroxylase and sterol 27-hydroxylase activities by steroids and physiological conditions in hamster
Life Sci.
17
1585-1593
1999
Mesocricetus auratus
brenda
Yamada, M.; Nagatomo, J.; Setoguchi, Y.; Kuroki, N.; Higashi, s.; Setoguchi, T.
Circadian Rhytms of sterol 12alpha-hydroxylase, cholesterol 7alpha-hydroxylase and DBP involved in rat cholesterol catabolism
Biol. Chem.
381
1149-1153
2000
Rattus norvegicus
brenda
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
brenda
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
brenda
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, Homo sapiens, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus
brenda
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
brenda
Shin, Y.; Vaziri, N.D.; Willekes, N.; Kim, C.H.; Joles, J.A.
Effects of gender on hepatic HMG-CoA reductase, cholesterol 7alpha-hydroxylase, and LDL receptor in hereditary analbuminemia
Am. J. Physiol. Endocrinol. Metab.
289
E993-E998
2005
Rattus norvegicus
brenda
Maeda, Y.; Nagatomo, H.; Kuroki, N.; Nagatomo, J.; Uchiyama, F.; Shimozono, K.; Kohno, Y.; Chijiiwa, K.
Bile acid biosynthesis during liver regeneration: enzyme activities of cholesterol 7alpha-hydroxylase and 3beta-hydroxy-delta5-C27-steroid dehydrogenase in rats
Ann. Clin. Lab. Sci.
35
323-328
2005
Rattus norvegicus
brenda
Handschin, C.; Gnerre, C.; Fraser, D.J.; Martinez-Jimenez, C.; Jover, R.; Meyer, U.A.
Species-specific mechanisms for cholesterol 7alpha-hydroxylase (CYP7A1) regulation by drugs and bile acids
Arch. Biochem. Biophys.
434
75-85
2005
Gallus gallus (Q5ILH2), Gallus gallus
brenda
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
brenda
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
brenda
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
brenda
Wang, J.; Olin, M.; Rozell, B.; Bjoerkhem, I.; Einarsson, C.; Eggertsen, G.; Gafvels, M.
Differential hepatocellular zonation pattern of cholesterol 7alpha-hydroxylase (Cyp7a1) and sterol 12alpha-hydroxylase (Cyp8b1) in the mouse
Histochem. Cell Biol.
127
253-261
2007
Mus musculus
brenda
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
brenda
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)
brenda
Shibata, S.; Hayakawa, K.; Egashira, Y.; Sanada, H.
Hypocholesterolemic mechanism of Chlorella: Chlorella and its indigestible fraction enhance hepatic cholesterol catabolism through up-regulation of cholesterol 7alpha-hydroxylase in rats
Biosci. Biotechnol. Biochem.
71
916-925
2007
Rattus norvegicus
brenda
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
brenda
Hubacek, J.A.; Bobkova, D.; Bohuslavova, R.; Poledne, R.
Differences in expression of cholesterol 7alpha-hydroxylase between PHHC and Wistar rats
Folia Biol. (Praha)
54
18-23
2008
Rattus norvegicus
brenda
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)
brenda
Cheng, Z.; Zhou, H.; Luther, M.; Yin, J.J.; Yu, L.L.
Effects of wheat antioxidants on oxygen diffusion-concentration products in liposomes and mRNA levels of HMG-CoA reductase and cholesterol 7alpha-hydroxylase in primary rat hepatocytes
J. Agric. Food Chem.
56
5033-5042
2008
Rattus norvegicus
brenda
Noshiro, M.; Usui, E.; Kawamoto, T.; Kubo, H.; Fujimoto, K.; Furukawa, M.; Honma, S.; Makishima, M.; Honma, K.; Kato, Y.
Multiple mechanisms regulate circadian expression of the gene for cholesterol 7alpha-hydroxylase (Cyp7a), a key enzyme in hepatic bile acid biosynthesis
J. Biol. Rhythms
22
299-311
2007
Mus musculus (Q64505)
brenda
Li, T.; Ma, H.; Chiang, J.Y.
TGF{beta}1, TNF{alpha}, and insulin signaling crosstalk in regulation of the rat cholesterol 7{alpha}-hydroxylase gene expression
J. Lipid Res.
49
1981-1989
2008
Rattus norvegicus
brenda
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
brenda
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
brenda
Wooton-Kee, C.; Cohen, D.; Vore, M.
Increased cholesterol 7alpha-hydroxylase expression and size of the bile acid pool in the lactating rat
Am. J. Physiol. Gastrointest. Liver Physiol.
294
G1009-G1016
2008
Rattus norvegicus
brenda
Burke, K.T.; Horn, P.S.; Tso, P.; Heubi, J.E.; Woollett, L.A.
Hepatic bile acid metabolism in the neonatal hamster: expansion of the bile acid pool parallels increased Cyp7a1 expression levels
Am. J. Physiol. Gastrointest. Liver Physiol.
297
G144-G151
2009
Mesocricetus auratus
brenda
Kojima, M.; Ashino, T.; Yoshida, T.; Iwakura, Y.; Sekimoto, M.; Degawa, M.
IL-1 regulates the Cyp7a1 gene and serum total cholesterol level at steady state in mice
Biochem. Biophys. Res. Commun.
379
239-242
2009
Mus musculus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Xie, Y.; Blanc, V.; Kerr, T.A.; Kennedy, S.; Luo, J.; Newberry, E.P.; Davidson, N.O.
Decreased expression of cholesterol 7alpha-hydroxylase and altered bile acid metabolism in Apobec-1-/- mice lead to increased gallstone susceptibility
J. Biol. Chem.
284
16860-16871
2009
Mus musculus (Q64505), Mus musculus
brenda
Taniguchi, M.; Nagao, K.; Inoue, K.; Imaizumi, K.
Cholesterol lowering effect of sulfur-containing amino acids added to a soybean protein diet in rats
J. Nutr. Sci. Vitaminol.
54
448-453
2008
Rattus norvegicus
brenda
Pond, W.G.; Mersmann, H.J.; Su, D.; McGlone, J.J.; Wheeler, M.B.; Smith, E.O.
Neonatal dietary cholesterol and alleles of cholesterol 7-alpha hydroxylase affect piglet cerebrum weight, cholesterol concentration, and behavior
J. Nutr.
138
282-286
2008
Sus scrofa
brenda
Zhang, L.; Huang, X.; Meng, Z.; Dong, B.; Shiah, S.; Moore, D.D.; Huang, W.
Significance and mechanism of CYP7a1 gene regulation during the acute phase of liver regeneration
Mol. Endocrinol.
23
137-145
2009
Mus musculus
brenda
Zhou, X.; Han, Y.; Liu, J.; Gao, L.; Zhao, J.
Decreased protein and gene expression of hepatic cholesterol 7a-hydroxylase associated with dilated endoplasmic reticulum in chronic hypothyroid rats
Pathol. Int.
59
729-734
2009
Rattus norvegicus
brenda
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
brenda
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
brenda
Wooton-Kee, C.; Coy, D.; Athippozhy, A.; Zhao, T.; Jones, B.; Vore, M.
Mechanisms for increased expression of cholesterol 7alpha-hydroxylase (Cyp7a1) in lactating rats
Hepatology
51
277-285
2010
Rattus norvegicus
brenda
Li, T.; Owsley, E.; Matozel, M.; Hsu, P.; Novak, C.M.; Chiang, J.Y.
Transgenic expression of cholesterol 7alpha-hydroxylase in the liver prevents high-fat diet-induced obesity and insulin resistance in mice
Hepatology
52
678-690
2010
Mus musculus, Mus musculus C57BL/6
brenda
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
brenda
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
brenda
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
brenda
Li, T.; Matozel, M.; Boehme, S.; Kong, B.; Nilsson, L.M.; Guo, G.; Ellis, E.; Chiang, J.Y.
Overexpression of cholesterol 7alpha-hydroxylase promotes hepatic bile acid synthesis and secretion and maintains cholesterol homeostasis
Hepatology
53
996-1006
2011
Rattus norvegicus (P18125)
brenda
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)
brenda
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
brenda
Kawase, A.; Yamada, A.; Gamou, Y.; Tahara, C.; Takeshita, F.; Murata, K.; Matsuda, H.; Samukawa, K.; Iwaki, M.
Increased effects of ginsenosides on the expression of cholesterol 7alpha-hydroxylase but not the bile salt export pump are involved in cholesterol metabolism
J. Nat. Med.
67
545-553
2013
Rattus norvegicus
brenda
Frank, D.J.; Waddling, C.A.; La, M.; Ortiz de Montellano, P.R.
Cytochrome P450 125A4, the third cholesterol C-26 hydroxylase from Mycobacterium smegmatis
Biochemistry
54
6909-6916
2015
Mycolicibacterium smegmatis
brenda
Krishnamurthy, K.; Glaser, S.; Alpini, G.; Cardounel, A.J.; Liu, Z.; Ilangovan, G.
Heat shock factor-1 knockout enhances cholesterol 7alpha hydroxylase (CYP7A1) and multidrug transporter (MDR1) gene expressions to attenuate atherosclerosis
Cardiovasc. Res.
111
74-83
2016
Mus musculus (Q64505)
brenda
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)
brenda
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
brenda
Fu, Z.D.; Cui, J.Y.; Klaassen, C.D.
Atorvastatin induces bile acid-synthetic enzyme Cyp7a1 by suppressing FXR signaling in both liver and intestine in mice
J. Lipid Res.
55
2576-2586
2014
Mus musculus (Q64505), Mus musculus C57BL/6 (Q64505)
brenda
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
brenda
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Release 2023.1 (January 2023)
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