Accepted Name |
cholate--CoA ligase.
|
Alternative Name(s) |
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-
forming). |
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate--CoA ligase. |
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase. |
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase. |
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A
synthetase. |
BAL. |
bile acid CoA ligase. |
bile acid coenzyme A ligase. |
cholate thiokinase. |
cholic acid:CoA ligase. |
cholic thiokinase. |
choloyl-CoA synthetase. |
choloyl coenzyme A synthetase. |
cholyl-CoA synthetase. |
THCA-CoA ligase. |
trihydroxycoprostanoyl-CoA synthetase. |
Reaction catalysed |
- ATP + cholate + CoA <=> AMP + choloyl-CoA + diphosphate
- (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + ATP + CoA <=> (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate
|
Comment(s) |
- This membrane-bound enzyme catalyzes 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 and converts the acyl-CoA
thioester into the corresponding N-acyl amidate by conjugation with
glycine or taurine.
- Chenodeoxycholate, deoxycholate, lithocholate and
trihydroxycoprostanoate can also act as substrates.
- Formerly EC 6.2.1.29.
|
Cross-references |
BRENDA | 6.2.1.7 |
EC2PDB | 6.2.1.7 |
ExplorEnz | 6.2.1.7 |
PRIAM enzyme-specific profiles | 6.2.1.7 |
KEGG Ligand Database for Enzyme Nomenclature | 6.2.1.7 |
IUBMB Enzyme Nomenclature | 6.2.1.7 |
IntEnz | 6.2.1.7 |
MEDLINE | Find literature relating to 6.2.1.7 |
MetaCyc | 6.2.1.7 |
Rhea expert-curated reactions | 6.2.1.7 |
UniProtKB/Swiss-Prot |
|