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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
-
?
additional information
?
-
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.
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
-
?
additional information
?
-
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
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
the enzyme belongs to the cytochrome P450 family
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
-
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
-
CYP7A1 is an enzyme involved in bile acid synthesis
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
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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
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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
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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
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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
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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
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Homo sapiens
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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