EC |
2.3.1.65 |
Accepted name: |
bile acid-CoA:amino acid N-acyltransferase |
Reaction: |
choloyl-CoA + glycine = CoA + glycocholate |
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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] |
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[EC 2.3.1.65 created 1983, modified 2005] |
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EC |
3.5.1.24 |
Accepted name: |
choloylglycine hydrolase |
Reaction: |
glycocholate + H2O = cholate + glycine |
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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] |
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[EC 3.5.1.24 created 1972] |
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