Malonyl-CoA inhibits proteolysis of carnitine palmitoyltransferase

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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.