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

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 transferas...

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Bibliographic Details
Published in:The Journal of biological chemistry 1976-06, Vol.251 (11), p.3352-3358
Main Authors: Webster, L T, Siddiqui, U A, Lucas, S V, Strong, J M, Mieyal, J J
Format: Article
Language:English
Subjects:
Acyltransferases - isolation & purification
Acyltransferases - metabolism
Animals
Coenzyme A
Glutamine
Glycine
Humans
Kinetics
Macaca mulatta
Mass Spectrometry
Mice
Mitochondria, Liver - enzymology
Molecular Weight
Species Specificity
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(17)33444-0