Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man

J Biol Chem. 1976 Jun 10;251(11):3352-8.


The conjugation of glycine to benzoates and the conjugation of L-glutamine to certain arylacetates are catalyzed by two different acyl-CoA:amino acid N-acyltransferases which can be purified separately from liver mitochondrial fractions of either rhesus monkey or man. In both species, one transferase is specific for glycine and the other for L-glutamine. The glycine enzyme utilizes either butyryl-CoA or benzoyl-CoA as acyl donors while the glutamine enzyme uses either phenylacetyl-CoA or indoleacetyl-CoA. Acyl-CoA substrates for one transferase do not serve as substrates for the other. Additional studies with the monkey liver enzymes revealed that acyl-CoA substrates for one transferase inhibit the other, that the apparent Km value is low (10(-6) to 10(-5) M range) for the preferred acyl-CoA substrate as compared to the amino acid acceptor (greater than 10(-2) M) and that both transferases have a molecular weight of approximately 24,000. Hippuric acid and either phenylacetylglutamine or indoleacetylglutamine were characterized as the products formed by the separate enzymes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyltransferases / isolation & purification
  • Acyltransferases / metabolism*
  • Animals
  • Coenzyme A
  • Glutamine
  • Glycine
  • Humans
  • Kinetics
  • Macaca mulatta
  • Mass Spectrometry
  • Mice
  • Mitochondria, Liver / enzymology*
  • Molecular Weight
  • Species Specificity


  • Glutamine
  • Acyltransferases
  • Coenzyme A
  • Glycine