Identification of separate acyl- CoA:glycine and acyl-CoA:L-glutamine N-acyltransferase activities in mitochondrial fractions from liver of rhesus monkey and man
Open accessAbstract
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.
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PAGln can be formed by phenylacetic acid conjugation to glutamine by human and rhesus monkey liver enzymes.
“Previous studies with either liver extracts or isolated enzymes have reported PAGln can be formed by phenylacetic acid (PAA) conjugation to the amino acid glutamine (Gln) by both human and rhesus monkey liver enzymes (Webster et al., 1976)”
From A Cardiovascular Disease-Linked Gut Microbial Metabolite Acts via Adrenergic Receptors (2020) · cites this paper as Webster et al., 1976
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Cites
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Research works printed but not linked: 1
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A Cardiovascular Disease-Linked Gut Microbial Metabolite Acts via Adrenergic Receptors
Nemet, I., Saha, P. P., Gupta, N., Zhu, W., Romano, K. A., Skye, S. M., Cajka, T., Mohan, M. L., Li, L., Wu, Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.016 · Cited by 784 · see citing works
O'Sullivan, A., Gibney, M. J., & Brennan, L. (2011) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.110.000950 · Cited by 297 · see citing works
- Authors
- Webster, L. T., Siddiqui, U. A., Lucas, S. V., Strong, J. M., & Mieyal, J. J.
- Affiliations
- Northwestern University (US)
- ORCID
- Mieyal, J J
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1976-06
- Volume
- 251
- Issue
- 11
- Pages
- 3352-3358
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1515879379
- Cited by
- 129
- References
- 13
- Citations by year
- 2026: 6 · 2025: 4 · 2024: 5 · 2023: 4 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 1 · 2014: 5 · 2013: 2 · 2012: 4
- FWCI
- 2.36
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- glycine conjugation, liver mitochondria, rhesus monkeys, human liver, enzyme specificity, substrate inhibition, hippuric acid, phenylacetylglutamine, enzyme purification
- MeSH terms
- Acyltransferases, Animals, Coenzyme A, Glutamine, Glycine, Humans, Kinetics, Macaca mulatta, Mitochondria, Liver, Molecular Weight, Species Specificity, Mass Spectrometry, Mice
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