ENZYME entry: EC 6.2.1.7

Accepted 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.
  • Formerly EC 6.2.1.29.
Cross-references
BRENDA6.2.1.7
EC2PDB6.2.1.7
ExplorEnz6.2.1.7
PRIAM enzyme-specific profiles6.2.1.7
KEGG Ligand Database for Enzyme Nomenclature6.2.1.7
IUBMB Enzyme Nomenclature6.2.1.7
IntEnz6.2.1.7
MEDLINEFind literature relating to 6.2.1.7
MetaCyc6.2.1.7
UniProtKB/Swiss-Prot
Q9Y2P5, S27A5_HUMAN;  Q4LDG0, S27A5_MOUSE;  Q9ES38, S27A5_RAT;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.2.1.-
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