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 β-oxidation [1], until enzymologists came along. By kinetic, physical and localization studies, eight different mammalian carnitine acyltransferases have been characterized (reviewed in [2,3]). Of these, five have been cloned and sequenced. The carnitine: acylcarnitine exchange carrier, first characterized in mitochondria [4,5], has now been demonstrated immunologically in peroxisomal membranes too [6]. 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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Conference Article|
February 01 2000
The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions
R. R. Ramsay
R. R. Ramsay
1Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews, Fife KYI6 9ST, U.K.
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Publisher: Portland Press Ltd
Received:
August 09 1999
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2000 Biochemical Society
2000
Biochem Soc Trans (2000) 28 (2): 182–186.
Article history
Received:
August 09 1999
Citation
R. R. Ramsay; The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions. Biochem Soc Trans 1 February 2000; 28 (2): 182–186. doi: https://doi.org/10.1042/bst0280182
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