| Entry |
|
| Name |
cholate---CoA ligase;
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;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase;
THCA-CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate---CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-forming);
cholyl-CoA synthetase;
trihydroxycoprostanoyl-CoA synthetase
|
| Class |
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
 |
| Sysname |
cholate:CoA ligase (AMP-forming)
|
| Reaction(IUBMB) |
(1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN: R02794];
(2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN: R04580]
|
| Reaction(KEGG) |
|
| Substrate |
ATP [CPD: C00002];
cholate [CPD: C00695];
CoA [CPD: C00010];
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
|
| Product |
AMP [CPD: C00020];
diphosphate [CPD: C00013];
choloyl-CoA [CPD: C01794];
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
|
| Comment |
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 alpha-dehydroxylation pathway [5].
|
| Pathway |
| Primary bile acid biosynthesis | | Metabolic pathways |
|
| Orthology |
| solute carrier family 27 (fatty acid transporter), member 5 |
|
| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | SHR: | | OAA: | | » show all
 |
| Reference |
|
| Authors |
ELLIOTT WH. |
| Title |
The enzymic activation of cholic acid by guinea-pig-liver microsomes. |
| Journal |
Biochem. J. 62 (1956) 427-33. |
| Organism |
Cavia porcellus |
| Reference |
|
| Authors |
ELLIOTT WH. |
| Title |
The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes. |
| Journal |
Biochem. J. 65 (1957) 315-21. |
| Organism |
Cavia porcellus |
| Reference |
|
| Authors |
Prydz K, Kase BF, Bjorkhem I, Pedersen JI. |
| Title |
Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver. |
| Journal |
J. Lipid. Res. 29 (1988) 997-1004. |
| Organism |
Rattus norvegicus [GN: rno] |
| Reference |
|
| Authors |
Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S, Eyssen HJ, Mannaerts GP. |
| Title |
Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver. |
| Journal |
Biochem. J. 257 (1989) 221-9. |
| Organism |
Rattus norvegicus [GN: rno] |
| Reference |
|
| Authors |
Mallonee DH, Adams JL, Hylemon PB |
| Title |
The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase. |
| Journal |
J. Bacteriol. 174 (1992) 2065-71. |
| Reference |
|
| Authors |
Wheeler JB, Shaw DR, Barnes S. |
| Title |
Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes. |
| Journal |
Arch. Biochem. Biophys. 348 (1997) 15-24. |
| Organism |
Rattus norvegicus [GN: rno] |
| Sequence |
|
| Reference |
|
| Authors |
Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S. |
| Title |
Molecular cloning and expression of rat liver bile acid CoA ligase. |
| Journal |
J. Lipid. Res. 43 (2002) 2062-71. |
| Organism |
Rattus norvegicus [GN: rno] |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 9027-90-1 |