The substrate specificity of carnitine acetyltransferase
Open accessAbstract
1. A study of the acyl group specificity of the carnitine acetyltransferase reaction [acyl-(-)carnitine+CoASH right harpoon over left harpoon (-)-carnitine+acyl-CoA] has been made with the enzyme from pigeon breast muscle. Acyl groups containing up to 10 carbon atoms are transferred and detailed kinetic investigations with a range of acyl-CoA and acylcarnitine substrates are reported. 2. Acyl-CoA derivatives with 12 or more carbon atoms in the acyl group are potent reversible inhibitors of carnitine acetyltransferase, competing with acetyl-CoA. Lauroyl- and myristoyl-CoA show a mixed inhibition with respect to (-)-carnitine, but palmitoyl-CoA competes strictly with this substrate also. Palmitoyl-dl-carnitine shows none of these effects. 3. Ammonium palmitate inhibits the enzyme competitively with respect to (-)-carnitine and non-competitively with respect to acetyl-CoA. 4. It is suggested that a hydrophobic site exists on the carnitine acetyltransferase molecule. The hydrocarbon chain of an acyl-CoA derivative containing eight or more carbon atoms in the acyl group may interact with this, which results in enhanced acyl-CoA binding. Competition occurs between ligands bound to this hydrophobic site and the carnitine binding site. 5. The possible physiological significance of long-chain acyl-CoA inhibition of this enzyme is discussed.
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CrAT activity is principally regulated by substrate availability.
“These results are consistent with in vitro kinetic assays showing that CrAT activity is principally regulated by substrate availability (21,22).”
From Carnitine insufficiency caused by aging and overnutrition compromises mitochondrial performance and metabolic control (2009) · cites this paper as [22]
Earlier in vitro work found that long chain acyl-CoAs inhibit CrAT specific activity.
“and earlier studies reported that CrAT specific activity measured in vitro is inhibited by long chain acyl-CoAs (Chase, 1967).”
From Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility (2012) · cites this paper as Chase, 1967
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Cites
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- Authors
- Chase, J.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1967-08-01
- Volume
- 104
- Issue
- 2
- Pages
- 510-518
- ISSN
- 0006-2936 (ISSN-L)
- PMC
- PMC1270613
- OpenAlex
- W1865315855
- Cited by
- 86
- References
- 18
- Citations by year
- 2026: 1 · 2023: 1 · 2017: 1 · 2014: 1 · 2013: 2 · 2012: 1
- FWCI
- 5.83
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- carnitine acetyltransferase, substrate specificity, acyl-CoA, acylcarnitines, competitive inhibition, mixed-type inhibition, non-competitive inhibition, palmitoyl-CoA, myristoyl-CoA, hydrophobic binding site, enzyme kinetics, pigeon breast muscle
- MeSH terms
- Acyltransferases, Quaternary Ammonium Compounds, Animals, Binding Sites, Carnitine, Coenzyme A, Kinetics, Muscles, Palmitic Acids, Columbidae
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