ABSTRACT
A long chain carnitine acytransferase, carnitine palmitoyltransferase (CPT), is located in the mitochondrion only. Mitochondrial CPT activities can be demonstrated both on the cytosolic and the matrix faces of the mitochondrion. Several forms of regulation of catalytic activity of CPT have been reported. Competitive inhibition by malonyl CoA of CPT was the first reported mechanism of control of this enzyme. Other events, such as phosphorylation and membrane fluidity, have been suggested to exert some level of control. Although other factors such as phosphorylation or changes in the lipid environment have a limited effect, the major mechanism of control of the 68-kDa CPT must be protein synthesis. If the 68-kDa CPT proves to be the only mitochondrial CPT protein, then malonyl CoA may share an equal role in the overall regulation of this enzyme. The purification of the protein has allowed the generation of antibody, which has allowed quantification of CPT protein.
