Carnitine and carnitine acyltransferases were thought to be merely a mechanism for the rapid transfer of activated long-chain fatty acids into the mitochondrion for beta-oxidation, until enzymologists came along. By kinetic, physical and localization studies, eight different mammalian carnitine acyltransferases have been characterized. Of these, five have been cloned and sequenced. The carnitine :acylcarnitine exchange carrier, first characterized in mitochondria, has now been demonstrated immunologically in peroxisomal membranes too. This cell-wide carnitine system consisting of at least six proteins linking at least four intracellular pools of acyl-CoA that supply a multitude of lipid metabolic pathways is clearly more complex than was first thought. In this article, I describe the location and properties of the components to show how they can modulate acyl-CoA-dependent reactions in the cell.
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Rona Ruth Ramsay (2000) studied this question.
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