| 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 |
|