The Enzyme Database

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EC 2.3.1.65     
Accepted name: bile acid-CoA:amino acid N-acyltransferase
Reaction: choloyl-CoA + glycine = CoA + glycocholate
For diagram of the biosynthesis of cholic-acid conjugates, click here
Glossary: choloyl-CoA = 3α,7α,12α-trihydroxy-5β-cholan-24-oyl-CoA
Other name(s): glycine—taurine N-acyltransferase; amino acid N-choloyltransferase; BAT; glycine N-choloyltransferase; BACAT; cholyl-CoA glycine-taurine N-acyltransferase; cholyl-CoA:taurine N-acyltransferase
Systematic name: choloyl-CoA:glycine N-choloyltransferase
Comments: Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-β-alanine can act as substrates, but more slowly [4]. The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase [7]. 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 [4]. 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 6.2.1.7, cholate—CoA ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65979-40-0
References:
1.  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]
2.  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.
3.  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]
4.  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]
5.  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]
6.  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. [DOI] [PMID: 12951368]
7.  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. [DOI] [PMID: 12810727]
[EC 2.3.1.65 created 1983, modified 2005]
 
 
EC 3.5.1.24     
Accepted name: choloylglycine hydrolase
Reaction: glycocholate + H2O = cholate + glycine
For diagram of cholic acid conjugates biosynthesis, click here
Glossary: glycocholate = N-(3α,7α,12α-trihydroxy-5β-cholan-24-oyl)glycine
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
Other name(s): glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase
Systematic name: glycocholate amidohydrolase
Comments: Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-07-9
References:
1.  Nair, P.P., Gordon, M. and Reback, J. The enzymatic cleavage of the carbon-nitrogen bond in 3α,7α,12α-trihydroxy-5-β-cholan-24-oylglycine. J. Biol. Chem. 242 (1967) 7–11. [PMID: 6016335]
2.  Stellwag, E.J. and Hylemon, P.B. Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452 (1976) 165–176. [DOI] [PMID: 10993]
[EC 3.5.1.24 created 1972]
 
 


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