REGULATION OF ADENINE NUCLEOTIDE TRANSLOCATION BY LONG CHAIN FATTY ACYL CoA ESTERS

Publisher Summary This chapter discusses the regulation of adenine nucleotide translocation by long chain fatty acyl CoA esters. The adenine nucleotide translocase is recognized to be one of the most important enzymes in cell bioenergetics. A model for the mechanism of adenine nucleotide translocation had to take into consideration the asymmetry of the binding of the inhibitors. Long chain fatty acyl CoA esters are the natural effectors of the adenine nucleotide translocator. The receptors on the ADP/ATP carrier for the acyl CoA esters are asymmetric or in different conformational states in that when the acyl CoA is bound to the cytosolic side of the inner membrane, it inhibits like atractylate, whereas when it is bound to the matrix side of the inner membrane, the acyl CoA inhibits like bongkrekic acid. Long chain acyl CoA esters can be physiologically translocated across the inner mitochondrial membrane by the acylcarnitine transferase enzymes and the carnitine-acylcarnitine translocase system.