Malonyl-CoA inhibits proteolysis of carnitine palmitoyltransferase.
Incubation of isolated mitochondria in the presence of malonyl-CoA prevented proteolysis of the outer carnitine palmitoyltransferase by Nagarse and trypsin. Malonyl-CoA had no direct action on trypsin when present in a chromogenic assay system for proteolysis or when preincubated with the proteases in the absence of mitochondria. As reported previously, Nagarse had a differential effect on carnitine palmitoyltransferase in which malonyl-CoA inhibition was diminished to a greater extent than activity was lost, but all effects were blocked by malonyl-CoA in a concentration-dependent manner. These data suggest a specific effect of binding of malonyl-CoA to carnitine palmitoyltransferase as the protective mechanism.
Kashfi
K
K
Department of Pharmacology, College of Medicine, University of Tennessee, Memphis 38163.
Cook
G A
GA
D000818:Animals; D002334:Carnitine O-Palmitoyltransferase / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008316:Malonyl Coenzyme A / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013381:Subtilisins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors; D008316:Malonyl Coenzyme A; D002334:Carnitine O-Palmitoyltransferase; D013381:Subtilisins; D014357:Trypsin