ID   6.2.1.7
DE   Cholate--CoA ligase.
AN   3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate--CoA ligase.
AN   3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate:CoA ligase (AMP-
AN   forming).
AN   3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA ligase.
AN   3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA synthetase.
AN   3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl coenzyme A
AN   synthetase.
AN   BAL.
AN   Bile acid CoA ligase.
AN   Bile acid coenzyme A ligase.
AN   Cholate thiokinase.
AN   Cholic acid:CoA ligase.
AN   Cholic thiokinase.
AN   Choloyl coenzyme A synthetase.
AN   Choloyl-CoA synthetase.
AN   Cholyl-CoA synthetase.
AN   THCA-CoA ligase.
AN   Trihydroxycoprostanoyl-CoA synthetase.
CA   (1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA.
CA   (2) ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-
CA   oate + CoA = AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha-
CA   trihydroxy-5-beta-cholestanoyl-CoA.
CF   Magnesium.
CC   -!- This membrane-bound enzyme catalyzes the first step in the
CC       conjugation of bile acids with amino acids, converting bile acids
CC       into their acyl-CoA thioesters.
CC   -!- The second step involves EC 2.3.1.65 and converts the acyl-CoA
CC       thioester into the corresponding N-acyl amidate by conjugation with
CC       glycine or taurine.
CC   -!- Chenodeoxycholate, deoxycholate, lithocholate and
CC       trihydroxycoprostanoate can also act as substrates.
CC   -!- Formerly EC 6.2.1.29.
DR   Q9Y2P5, S27A5_HUMAN;  Q4LDG0, S27A5_MOUSE;  Q9ES38, S27A5_RAT  ;
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