The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions

Rona Ruth Ramsay

Research output: Contribution to conferencePaper

72 Citations (Scopus)

Abstract

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 [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.

Original languageEnglish
Pages182-186
Publication statusPublished - Feb 2000

Keywords

  • acyl-CoA pools
  • carnitine analogues
  • carnitine palmitoyltransferases
  • subcellular localization
  • MALONYL-COA
  • SACCHAROMYCES-CEREVISIAE
  • HEART-MITOCHONDRIA
  • PALMITOYLTRANSFERASE
  • RAT
  • OCTANOYLTRANSFERASE
  • ACETYLTRANSFERASES
  • PEROXISOMES
  • METABOLISM
  • MECHANISM

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