Regulation of mitochondrial carnitine palmitoyl transferases from liver and extrahepatic tissues.
Developments in our understanding of the complex CPT enzyme system over the past ten years have been reviewed. Liver CPT1, which is probably distinct from that in several extrahepatic tissues, is subject to up- or down-regulation of its activity and kinetic properties with changing physiological state. Evidence is now accumulating to support the notion that the catalytic and malonyl-CoA-binding entities of CPT1 are separate polypeptides.
Saggerson
D
D
Department of Biochemistry and Molecular Biology, University College, London, U.K.
Ghadiminejad
I
I
Awan
M
M
D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000187:drug effects / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology; D008099:Liver / Q000502:physiology*; D008316:Malonyl Coenzyme A / Q000378:metabolism / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects / Q000201:enzymology / Q000648:ultrastructure; D008929:Mitochondria, Heart / Q000187:drug effects / Q000378:metabolism; D008930:Mitochondria, Liver / Q000187:drug effects / Q000201:enzymology* / Q000648:ultrastructure; D009206:Myocardium / Q000378:metabolism; D051381:Rats; D014018:Tissue Distribution
D005227:Fatty Acids; D008316:Malonyl Coenzyme A; D002334:Carnitine O-Palmitoyltransferase