EC 2.3.1.65 - Bile acid-CoA:amino acid N-acyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.65

Names

Accepted name:
bile acid-CoA:amino acid N-acyltransferase
Other names:
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

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047963
CAS Registry Number: 74506-32-4
UniProtKB/Swiss-Prot:

References

  1. Czuba, B. and Vessey, D.A.
    Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver.
    J. Biol. Chem. 255: 5296-5299 (1980). [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: 325-330 (1980).
  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: 2059-2063 (1979). [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: 10227-10233 (1991). [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: 2062-2071 (2002). [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: 2242-2249 (2003). [PMID: 12951368]
  7. O'Byrne, J., Hunt, M.C., Rai, D.K., Saeki, M. and Alexson, S.E.H.
    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 2.3.1.65 created 1983, modified 2005]