SUCCINYL PHOSPHONATE INHIBITS ALPHA-KETOGLUTARATE OXIDATIVE DECARBOXYLATION, CATALYZED BY ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEXES FROM ESCHERICHIA-COLI AND PIGEON BREAST MUSCLE

Effects of a set of a-ketoglutarate phosphoanalogues on the activity o f alpha-ketoglutarate dehydrogenase (EC 1.2.4.2) complexes from E. col i and pigeon breast muscle, as well as on alpha-ketoglutarate dehydrog enase isolated from the pigeon breast muscle, have been studied, alpha -Ketoglutarate phosphoanalogues (succinyl phosphonate and its monometh yl ester) were found to be effective inhibitors of alpha-ketoglutarate oxidative decarboxylation, catalyzed by both muscle and bacterial alp ha-ketoglutarate dehydrogenase complexes, as well as muscle alpha-keto glutarate dehydrogenase, The ability of glutamate phosphoanalogues to inhibit alpha-ketoglutarate oxidative decarboxylation has been shown i n E. coli extract and a model system.