||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 188.8.131.52, cholate—CoA ligase.
||Czuba, B. and Vessey, D.A. Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver. J. Biol. Chem. 255 (1980) 5296–5299. [PMID: 7372637]
||Jordan, T.W., Lee, R. and Lim, W.C. Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver. Biochem. Int. 1 (1980) 325–330.
||Vessey, D.A. The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver. J. Biol. Chem. 254 (1979) 2059–2063. [PMID: 422567]
||Johnson, M.R., Barnes, S., Kwakye, J.B. and Diasio, R.B. Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J. Biol. Chem. 266 (1991) 10227–10233. [PMID: 2037576]
||Falany, C.N., Xie, X., Wheeler, J.B., Wang, J., Smith, M., He, D. and Barnes, S. Molecular cloning and expression of rat liver bile acid CoA ligase. J. Lipid Res. 43 (2002) 2062–2071. [PMID: 12454267]
||He, D., Barnes, S. and Falany, C.N. Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization. J. Lipid Res. 44 (2003) 2242–2249. [PMID: 12951368]
||O'Byrne, J., Hunt, M.C., Rai, D.K., Saeki, M. and Alexson, S.E. The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J. Biol. Chem. 278 (2003) 34237–34244. [PMID: 12810727]