Abstract
Carnitine acyltransferases in mitochondria, peroxisomes and the endoplasmic reticulum are different gene products and serve different metabolic functions in the cell. Here we summarize briefly evidence that carnitine octanoyltransferase (COT) from the peroxisomes and carnitine palmitoyltransferase II (CPT-II) from the mitochondria (both matrix facing enzymes) differ kinetically and demonstrate that they differ in their sensitivity to conformationally constrained inhibitors that mimic the reaction intermediate. Medium chain inhibitors are 15 times more effective on COT than on CPT-II and long chain inhibitors, such as hemipalmitoylcarnitinium, 80 times more effective on the mitochondrial enzyme. Thus, it may be possible to develop inhibitors to inhibit mitochondrial β-oxidation with minimal effects on peroxisomal β-oxidation and otheracyl-CoA dependent reactions.
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© 2002 Kluwer Academic Publishers
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Ramsay, R.R., Gandour, R.D. (2002). Selective Modulation of Carnitine Long-chain Acyltransferase Activities. In: Quant, P.A., Eaton, S. (eds) Current Views of Fatty Acid Oxidation and Ketogenesis. Advances in Experimental Medicine and Biology, vol 466. Springer, Boston, MA. https://doi.org/10.1007/0-306-46818-2_11
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DOI: https://doi.org/10.1007/0-306-46818-2_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46200-9
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