The mitochondrial carnitine palmitoyltransferase system—from concept to molecular analysis

JD McGarry, NF Brown - European journal of biochemistry, 1997 - Wiley Online Library
JD McGarry, NF Brown
European journal of biochemistry, 1997Wiley Online Library
First conceptualized as a mechanism for the mitochondrial transport of long‐chain fatty acids
in the early 1960s, the carnitine palmitoyltransferase (CPT) system has since come to be
recognized as a pivotal component of fuel homeostasis. This is by virtue of the unique
sensitivity of the outer membrane CPT I to the simple molecule, malonyl‐CoA. In addition,
both CPT I and the inner membrane enzyme, CPT II, have proved to be loci of inherited
defects, some with disastrous consequences. Early efforts using classical approaches to …
First conceptualized as a mechanism for the mitochondrial transport of long‐chain fatty acids in the early 1960s, the carnitine palmitoyltransferase (CPT) system has since come to be recognized as a pivotal component of fuel homeostasis. This is by virtue of the unique sensitivity of the outer membrane CPT I to the simple molecule, malonyl‐CoA. In addition, both CPT I and the inner membrane enzyme, CPT II, have proved to be loci of inherited defects, some with disastrous consequences. Early efforts using classical approaches to characterize the CPT proteins in terms of structure/function/regulatory relationships gave rise to confusion and protracted debate. By contrast, recent application of molecular biological tools has brought major enlightenment at an exponential pace. Here we review some key developments of the last 20 years that have led to our current understanding of the physiology of the CPT system, the structure of the CPT isoforms, the chromosomal localization of their respective genes, and the identification of mutations in the human population.
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