EC 18.104.22.168 - Bile acid-CoA:amino acid N-acyltransferase
IntEnz Enzyme Nomenclature
amino acid N-choloyltransferase
cholyl-CoA glycine-taurine N-acyltransferase
- choloyl-CoA + glycine = CoA + glycocholate
Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-β-alanine can act as substrates, but more slowly . The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase . Bile-acid—amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol . This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 22.214.171.124, cholate—CoA ligase.
Links to other databases
Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver.J. Biol. Chem. 255 : 5296-5299 (1980). [PMID: 7372637]
Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver.Biochem. Int. 1 : 325-330 (1980).
The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver.J. Biol. Chem. 254 : 2059-2063 (1979). [PMID: 422567]
Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver.J. Biol. Chem. 266 : 10227-10233 (1991). [PMID: 2037576]
Molecular cloning and expression of rat liver bile acid CoA ligase.J. Lipid Res. 43 : 2062-2071 (2002). [PMID: 12454267]
Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.J. Lipid Res. 44 : 2242-2249 (2003). [PMID: 12951368]
The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine.J. Biol. Chem. 278 : 34237-34244 (2003). [PMID: 12810727]
[EC 126.96.36.199 created 1983, modified 2005]