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• W1649546940 endingPage "644" @default.
• W1649546940 startingPage "627" @default.
• W1649546940 abstract "This chapter focuses on carnitine acyltransferases. The carnitine enzyme with a large acyl transfer capacity for acetyl residues is called “carnitine acetyltransferase” (CAT), whereas the enzyme, which has a high transfer capacity for palmityl residues, is named “carnitine palmityltransferase” (CPT). The broad acyl specificity of the carnitine acyltransferases in mammalian systems does not occur in all living systems. In some yeasts, plants, and even insects, the acyl specificity may be more restricted and appears to depend on the fuel source and metabolism involved. The functions of short-chain carnitine acyltransferases require elucidation, especially in non-fatty acid-oxidizing systems such as trypanosomes and certain yeasts, and also in mammals. The number and nature of the transferases depend on the tissue and animal source. Trypanosomes and yeast contain a short-chain carnitine acyltransferase of very narrow acyl specificity. In contrast, mammalian systems contain more than one enzyme and the short-chain acyl-specific activity often greatly exceeds that of the long-chain. Even for mammals, the number and nature of transferases vary and are tissue specific. Although carnitine palmityltransferase (CPT) is associated with mitochondria, it's distribution with respect to the intramitochondrial membrane has not been unequivocally established. The amount of catalytically active outer CPT becomes quite critical when one considers its potential effect on the flux of fatty acids through mitochondrial β oxidation and its regulation by malonyl-CoA. Carnitine acetyltransferase is the predominant acyltransferase in most tissues. In tissues such as liver, CAT is associated with at least three different subcellular structures, while in tissues such as heart and skeletal muscle the distribution of CAT appears to be more limited." @default.
• W1649546940 created "2016-06-24" @default.
• W1649546940 creator A5024707559 @default.
• W1649546940 creator A5056819586 @default.
• W1649546940 date "1983-01-01" @default.
• W1649546940 modified "2023-09-27" @default.
• W1649546940 title "18 Carnitine Acyltransferases" @default.
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• W1649546940 doi "https://doi.org/10.1016/s1874-6047(08)60316-9" @default.
• W1649546940 hasPublicationYear "1983" @default.
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