| 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) |
R02794 R04580;
(other) R04507 R08733 R08738 R08743
 |
|---|
| 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. This membrane-bound enzyme catalyses the
first step in the conjugation of bile acids with amino acids,
converting bile acids into their acyl-CoA thioesters. The second
step involves EC 2.3.1.65, bile acid-CoA:amino acid
N-acyltransferase and converts the acyl-CoA thioester into the
corresponding N-acyl amidate by conjugation with glycine or taurine
[5]. Chenodeoxycholate, deoxycholate, lithocholate and
trihydroxycoprostanoate can also act as substrates [6]. |
|---|
| Pathway |
PATH: ec00120 Primary bile acid biosynthesis
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K08748 solute carrier family 27 (fatty acid transporter),
member 5 |
|---|
| Genes |
HSA: 10998(SLC27A5)
PTR: 456351(SLC27A5)
MCC: 713713
MMU: 26459(Slc27a5)
RNO: 79111(Slc27a5)
CFA: 484223 608675(SLC27A5)
BTA: 533016(SLC27A5)
ECB: 100051678(SLC27A5)
 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:13303991]
ELLIOTT WH.
The enzymic activation of cholic acid by guinea-pig-liver
microsomes.
Biochem. J. 62 (1956) 427-33.
Cavia porcellus |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:13403911]
ELLIOTT WH.
The breakdown of adenosine triphosphate accompanying cholic acid
activation by guinea-pig liver microsomes.
Biochem. J. 65 (1957) 315-21.
Cavia porcellus |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:3183523]
Prydz K, Kase BF, Bjorkhem I, Pedersen JI.
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.
J. Lipid. Res. 29 (1988) 997-1004.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:2521999]
Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S,
Eyssen HJ, Mannaerts GP.
Subcellular distribution and characteristics of
trihydroxycoprostanoyl-CoA synthetase in rat liver.
Biochem. J. 257 (1989) 221-9.
Rattus norvegicus [GN:rno] |
|---|
Reference
Authors
Title
Journal
Organism
Sequence
|
5 [PMID:9390170]
Wheeler JB, Shaw DR, Barnes S.
Purification and characterization of a rat liver bile acid coenzyme
A ligase from rat liver microsomes.
Arch. Biochem. Biophys. 348 (1997) 15-24.
Rattus norvegicus [GN:rno]
RNO: 79111 |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:12454267]
Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S.
Molecular cloning and expression of rat liver bile acid CoA ligase.
J. Lipid. Res. 43 (2002) 2062-71.
Rattus norvegicus [GN:rno] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 6.2.1.7
IUBMB Enzyme Nomenclature: 6.2.1.7
ExPASy - ENZYME nomenclature database: 6.2.1.7
BRENDA, the Enzyme Database: 6.2.1.7
CAS: 9027-90-1 |
|---|
