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Acido biliare-CoA:amminoacido N-aciltransferasi

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acido biliare-CoA:amminoacido N-aciltransferasi
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Numero EC2.3.1.65
ClasseTransferasi
Nome sistematico
coloil-CoA:glicina N-coloiltransferasi
Altri nomi
glicina-taurina N-aciltransferasi; amminoacido N-coloiltransferasi; BAT; glicina N-coloiltransferasi; BACAT; colil-CoA glicina-taurina N-aciltransferasi; colil-CoA:taurina N-aciltransferasi
Banche datiBRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum)
Fonte: IUBMB
Modifica dati su Wikidata · Manuale

L'acido biliare-CoA:amminoacido N-aciltransferasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione:

coloil-CoA + glicina ⇄ CoA + glicocolato

L'enzima catalizza l'unione di un acido grasso con la glicina e può agire come tioesterasi degli acil-CoA a catena molto lunga. I coniugati acido biliare-amminoacido sono utilizzati dall'organismo come detergenti nel tratto gastrointestinale, in grado di solubilizzare gli acidi grassi a lunga catena (mono- e digliceridi), le vitamine liposolubili ed il colesterolo.

Questo è il secondo enzima di un pathway a due fasi che porta alla coniugazione degli acidi biliari agli amminoacidi; la prima fase è la conversione degli acidi biliari nei loro acil-CoA tioesteri, che è che è catalizzata dalla colato-CoA ligasi (numero EC 6.2.1.7[1]).

L'enzima agisce anche sui derivati del CoA di altri acidi biliari. La taurina e la 2-fluoro-β-alanina possono agire come substrati, ma più lentamente.

Note

  1. ^ (EN) 6.2.1.7, in ExplorEnz — The Enzyme Database, IUBMB.

Bibliografia

  • 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, in J. Biol. Chem., vol. 278, 2003, pp. 34237–34244, Entrez PubMed 12810727.
  • He, D., Barnes, S. and Falany, C.N., Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization, in J. Lipid Res., vol. 44, 2003, pp. 2242–2249, Entrez PubMed 12951368.
  • 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, in J. Lipid Res., vol. 43, 2002, pp. 2062–2071, Entrez PubMed 12454267.
  • Vessey, D.A., The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver, in J. Biol. Chem., vol. 254, 1979, pp. 2059–2063, Entrez PubMed 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, in J. Biol. Chem., vol. 266, 1991, pp. 10227–10233, Entrez PubMed 2037576.
  • 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, in Biochem. Int., vol. 1, 1980, pp. 325–330.
  • Czuba, B. and Vessey, D.A., Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver, in J. Biol. Chem., vol. 255, 1980, pp. 5296–5299, Entrez PubMed 7372637.
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