| Official Name |
|---|
| Cholate--CoA ligase.
|
| Alternative Name(s) |
|---|
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate--CoA ligase. |
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate:CoA ligase (AMP-
forming). |
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA ligase. |
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA synthetase. |
| 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl coenzyme A
synthetase. |
| BAL. |
| Bile acid CoA ligase. |
| Bile acid coenzyme A ligase. |
| Cholate thiokinase. |
| Cholic acid:CoA ligase. |
| Cholic thiokinase. |
| Choloyl coenzyme A synthetase. |
| Choloyl-CoA synthetase. |
| Cholyl-CoA synthetase. |
| THCA-CoA ligase. |
| Trihydroxycoprostanoyl-CoA synthetase. |
| Reaction catalysed |
|---|
- ATP + cholate + CoA <=> AMP + diphosphate + choloyl-CoA
- ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + CoA <=> AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA
|
| Cofactor(s) |
|---|
| Magnesium.
|
| 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.
|
| Cross-references |
|---|
| Biochemical Pathways; map number(s) | K10 |
| BRENDA | 6.2.1.7 |
| PUMA2 | 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 |
| UniProtKB/Swiss-Prot |
|
ExPASy Home page