IntEnz

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

IntEnz Enzyme Nomenclature
EC 2.3.1.65

Names

Reaction

• 14001 [IUBMB]
  choloyl-CoA

  choloyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57373

  Formula: C45H70N7O20P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  glycine

  glycine

  Name origin: UniProt - CHECKED (C)

  CHEBI:57305

  Formula: C2H5NO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  CoA

  CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57287

  Formula: C21H32N7O16P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  glycocholate

  glycocholate

  Name origin: UniProt - CHECKED (C)

  CHEBI:29746

  Formula: C26H42NO6
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

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

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]