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Your query returned 15 entries. Printable version
EC | 1.1.1.52 | ||||||||||||||
Accepted name: | 3α-hydroxycholanate dehydrogenase (NAD+) | ||||||||||||||
Reaction: | lithocholate + NAD+ = 3-oxo-5β-cholan-24-oate + NADH + H+ | ||||||||||||||
For diagram of cholesterol catabolism (rings A, B and C), click here | |||||||||||||||
Glossary: | lithocholate = 3α-hydroxy-5β-cholan-24-oate | ||||||||||||||
Other name(s): | α-hydroxy-cholanate dehydrogenase; lithocholate:NAD+ oxidoreductase; 3α-hydroxycholanate dehydrogenase | ||||||||||||||
Systematic name: | lithocholate:NAD+ 3-oxidoreductase | ||||||||||||||
Comments: | Also acts on other 3α-hydroxysteroids with an acidic side-chain. cf. EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-57-3 | ||||||||||||||
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EC | 1.1.1.391 | ||||||||||||||
Accepted name: | 3β-hydroxycholanate 3-dehydrogenase (NAD+) | ||||||||||||||
Reaction: | isolithocholate + NAD+ = 3-oxo-5β-cholan-24-oate + NADH + H+ | ||||||||||||||
Glossary: | isolithocholate = 3β-hydroxy-5β-cholan-24-oate | ||||||||||||||
Other name(s): | 3β-hydroxysteroid dehydrogenase | ||||||||||||||
Systematic name: | isolithocholate:NAD+ 3-oxidoreductase | ||||||||||||||
Comments: | This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.393, 3β-hydroxycholanate 3-dehydrogenase (NADP+). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 1.1.1.392 | ||||||||||||||
Accepted name: | 3α-hydroxycholanate dehydrogenase (NADP+) | ||||||||||||||
Reaction: | lithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+ | ||||||||||||||
Glossary: | lithocholate = 3α-hydroxy-5β-cholan-24-oate | ||||||||||||||
Other name(s): | α-hydroxy-cholanate dehydrogenase (ambiguous) | ||||||||||||||
Systematic name: | lithocholate:NADP+ 3-oxidoreductase | ||||||||||||||
Comments: | This bacterial enzyme is involved in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids) via a 3-oxo intermediate. The enzyme catalyses a reversible reaction in vitro. Also acts on related bile acids. cf. EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9028-57-3 | ||||||||||||||
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EC | 1.1.1.393 | ||||||||||||||
Accepted name: | 3β-hydroxycholanate 3-dehydrogenase (NADP+) | ||||||||||||||
Reaction: | isolithocholate + NADP+ = 3-oxo-5β-cholan-24-oate + NADPH + H+ | ||||||||||||||
Glossary: | isolithocholate = 3β-hydroxy-5β-cholan-24-oate | ||||||||||||||
Other name(s): | 3β-hydroxysteroid dehydrogenase (ambiguous) | ||||||||||||||
Systematic name: | isolithocholate:NADP+ 3-oxidoreductase | ||||||||||||||
Comments: | This bacterial enzyme is involved, along with EC 1.1.1.52, 3α-hydroxycholanate dehydrogenase (NAD+), or EC 1.1.1.392, 3α-hydroxycholanate dehydrogenase (NADP+), in the modification of secondary bile acids to form 3β-bile acids (also known as iso-bile acids). The enzyme catalyses the reaction in the reduction direction in vivo. Also acts on related 3-oxo bile acids. cf. EC 1.1.1.391, 3β-hydroxycholanate 3-dehydrogenase (NAD+). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 1.14.13.94 | ||||||||||||||
Transferred entry: | lithocholate 6β-hydroxylase. Now EC 1.14.14.138, lithocholate 6β-hydroxylase | ||||||||||||||
EC | 1.14.13.97 | ||||||||||||||
Transferred entry: | taurochenodeoxycholate 6α-hydroxylase. Now EC 1.14.14.57, taurochenodeoxycholate 6α-hydroxylase | ||||||||||||||
EC | 1.14.14.57 | ||||||||||||||
Accepted name: | taurochenodeoxycholate 6α-hydroxylase | ||||||||||||||
Reaction: | (1) taurochenodeoxycholate + [reduced NADPH—hemoprotein reductase] + O2 = taurohyocholate + [oxidized NADPH—hemoprotein reductase] + H2O (2) lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = hyodeoxycholate + [oxidized NADPH—hemoprotein reductase] + H2O |
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For diagram of the biosynthesis of cholic-acid conjugates, click here | |||||||||||||||
Glossary: | taurochenodeoxycholic acid = N-(3α,7α-dihydroxy-5β-cholan-24-oyl)taurine taurohyocholic acid = N-(3α,6α,7α-trihydroxy-5β-cholan-24-oyl)taurine hyodeoxycholate = 3α,6α-dihydroxy-5β-cholan-24-oate lithocholate = 3α-hydroxy-5β-cholan-24-oate |
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Other name(s): | CYP3A4; CYP4A21; taurochenodeoxycholate 6α-monooxygenase | ||||||||||||||
Systematic name: | taurochenodeoxycholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6α-hydroxylating) | ||||||||||||||
Comments: | A cytochrome P-450 (heme-thiolate) protein. Requires cytochrome b5 for maximal activity. Acts on taurochenodeoxycholate, taurodeoxycholate and less readily on lithocholate and chenodeoxycholate. In adult pig (Sus scrofa), hyocholic acid replaces cholic acid as a primary bile acid [5]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 105669-85-0 | ||||||||||||||
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EC | 1.14.14.138 | ||||||||||||||
Accepted name: | lithocholate 6β-hydroxylase | ||||||||||||||
Reaction: | lithocholate + [reduced NADPH—hemoprotein reductase] + O2 = 6β-hydroxylithocholate + [oxidized NADPH—hemoprotein reductase] + H2O | ||||||||||||||
For diagram of the reaction of deoxycholate and related bile acids, click here | |||||||||||||||
Glossary: | lithocholate = 3α-hydroxy-5β-cholan-24-oate 6β-hydroxylithocholate = murideoxycholate = 3α,6β-dihydroxy-5β-cholan-24-oate |
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Other name(s): | lithocholate 6β-monooxygenase; CYP3A10; 6β-hydroxylase; cytochrome P450 3A10; lithocholic acid 6β-hydroxylase | ||||||||||||||
Systematic name: | lithocholate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (6β-hydroxylating) | ||||||||||||||
Comments: | A cytochrome P-450 (heme-thiolate) protein from Mesocricetus auratus (golden hamster). Expression of the gene for this enzyme is 50-fold higher in male compared to female hamsters [1]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-83-6 | ||||||||||||||
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EC | 1.17.1.6 | ||||||||||||||
Transferred entry: | bile-acid 7α-dehydroxylase. Now EC 1.17.99.5, bile-acid 7α-dehydroxylase. It is now known that FAD is the acceptor and not NAD+ as was thought previously | ||||||||||||||
EC | 1.17.98.1 | ||||||||||||||
Deleted entry: | bile-acid 7α-dehydroxylase. Now known to be catalyzed by multiple enzymes. | ||||||||||||||
EC | 1.17.99.5 | ||||||||||||||
Transferred entry: | bile-acid 7α-dehydroxylase. Now classified as EC 1.17.98.1, bile-acid 7α-dehydroxylase. | ||||||||||||||
EC | 2.8.2.14 | ||||||||||||||
Accepted name: | bile-salt sulfotransferase | ||||||||||||||
Reaction: | (1) 3′-phosphoadenylyl sulfate + glycolithocholate = adenosine 3′,5′-bisphosphate + glycolithocholate 3-sulfate (2) 3′-phosphoadenylyl sulfate + taurolithocholate = adenosine 3′,5′-bisphosphate + taurolithocholate sulfate |
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For diagram of reaction, click here and for diagram of cholic acid conjugates biosynthesis, click here | |||||||||||||||
Glossary: | glycolithocholate 3-sulfate = N-(3α-sulfooxy-5β-cholan-24-oyl)glycine | ||||||||||||||
Other name(s): | BAST I; bile acid:3′-phosphoadenosine-5′-phosphosulfate sulfotransferase; bile salt:3′phosphoadenosine-5′-phosphosulfate:sulfotransferase; bile acid sulfotransferase I; glycolithocholate sulfotransferase; 3′-phosphoadenylyl-sulfate:glycolithocholate sulfotransferase | ||||||||||||||
Systematic name: | 3′-phosphoadenylyl-sulfate:glycolithocholate sulfonotransferase | ||||||||||||||
Comments: | The formation of sulfate esters of bile acids is an essential step in the prevention of toxicity by monohydroxy bile acids in many species [3]. This enzyme is both a bile salt and a 3-hydroxysteroid sulfotransferase. In addition to the 5β-bile acid glycolithocholate, deoxycholate, 3β-hydroxy-5-cholenoate and dehydroepiandrosterone (3β-hydroxyandrost-5-en-17-one) also act as substrates [see also EC 2.8.2.2 (alcohol sulfotransferase) and EC 2.8.2.34 (glycochenodeoxycholate sulfotransferase)]. May be identical to EC 2.8.2.2 [3]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65802-92-8 | ||||||||||||||
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EC | 2.8.2.34 | ||||||||||||||
Accepted name: | glycochenodeoxycholate sulfotransferase | ||||||||||||||
Reaction: | 3′-phosphoadenylyl sulfate + glycochenodeoxycholate = adenosine 3′,5′-bisphosphate + glycochenodeoxycholate 7-sulfate | ||||||||||||||
For diagram of reaction, click here | |||||||||||||||
Glossary: | 3′-phosphoadenylyl sulfate = PAPS glycochenodeoxycholate 7-sulfate = N-(3α-hydroxy-7α-sulfooxy-5β-cholan-24-oyl)glycine |
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Other name(s): | bile acid:3′-phosphoadenosine-5′-phosphosulfate sulfotransferase; bile acid:PAPS:sulfotransferase; BAST; 3′-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfotransferase | ||||||||||||||
Systematic name: | 3′-phosphoadenylyl-sulfate:glycochenodeoxycholate 7-sulfonotransferase | ||||||||||||||
Comments: | The enzyme specifically sulfates glycochenodeoxycholate at the 7α-position (see also EC 2.8.2.14 bile-salt sulfotransferase). The monohydroxy bile acids glycolithocholate, chenodeoxycholate and ursodeoxycholate act as inhibitors. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72668-90-7 | ||||||||||||||
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EC | 2.8.3.25 | ||||||||||||||
Accepted name: | bile acid CoA-transferase | ||||||||||||||
Reaction: | (1) lithocholoyl-CoA + cholate = lithocholate + choloyl-CoA (2) deoxycholoyl-CoA + cholate = deoxycholate + choloyl-CoA |
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Other name(s): | baiF (gene name); baiK (gene name); bile acid coenzyme A transferase | ||||||||||||||
Systematic name: | lithocholoyl-CoA:cholate CoA-transferase | ||||||||||||||
Comments: | The enzyme, characterized from the gut bacterium Clostridium scindens, catalyses the last step in bile acid 7α-dehydroxylation, the removal of the CoA moiety from the products. By using a transferase rather than hydrolase, the bacteria conserve the thioester bond energy, saving ATP molecules. Clostridium scindens possesses two forms of the enzyme, encoded by the baiF and baiK genes. While the enzymes have a broad acceptor specificity and can use allocholate, ursodeoxycholate, and β-muricholate, the donor specificity is more strict. BaiF acts on lithocholoyl-CoA and deoxycholoyl-CoA, and BaiK acts only on the latter. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 6.2.1.7 | ||||||||||||||
Accepted name: | cholate—CoA ligase | ||||||||||||||
Reaction: | (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA (2) ATP + (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA |
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For diagram of cholic acid conjugates biosynthesis, click here and for diagram of cholic acid biosynthesis (sidechain), click here | |||||||||||||||
Glossary: | cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate trihydroxycoprostanoate = 3α,7α,12α-trihydroxy-5β-cholestan-26-oate |
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Other name(s): | BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate—CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase | ||||||||||||||
Systematic name: | cholate:CoA ligase (AMP-forming) | ||||||||||||||
Comments: | Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates [7]. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway [5]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-90-1 | ||||||||||||||
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