The phospholipid environment of the mitochondrial inner membrane, which contains large amounts of cardiolipin, could play a key role in transport of the long chain fatty acids. In the present study, the pre-incubation of cardiolipin with the wild type carnitine palmitoyltransferase (CPT) II led to a more than 1.5-fold increase of enzyme activity at physiological temperatures. At higher temperatures, however, there was a pronounced loss of activity. The most frequent variant S113L showed even at 37 °C a great activity loss. Pre-incubation of the wild type with both malonyl-CoA and cardiolipin counteracted the positive effect of cardiolipin. Malonyl-CoA, however, showed no inhibition effect on the variant in presence of cardiolipin. The activity loss in presence of cardiolipin at fever simulating situations was more pronounced for the variant comparing to the wild type. The reason might be a disturbed membrane association or a blockage of the active center of the mutated enzyme.
Keywords: CPT II deficiency; Cardiolipin; Enzyme activity; Membrane association.