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ENZYME

ENZYME entry: EC 6.2.1.7

PURL: https://purl.expasy.org/enzyme/EC/6.2.1.7
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
  • cholate + ATP + CoA = choloyl-CoA + AMP + 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
Rhea expert-curated reactions6.2.1.7
ExplorEnz6.2.1.7
IUBMB Enzyme Nomenclature6.2.1.7
UniProtKB/Swiss-Prot
P19409, BAIB_CLOSVO14975, S27A2_HUMANO35488, S27A2_MOUSE
P97524, S27A2_RATQ9Y2P5, S27A5_HUMANQ4LDG0, S27A5_MOUSE
Q9ES38, S27A5_RAT
BRENDA6.2.1.7
MetaCyc6.2.1.7
KEGG Ligand Database for Enzyme Nomenclature6.2.1.7
EC2PDB6.2.1.7
MEDLINEFind literature relating to 6.2.1.7

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