Inactivation of alpha-ketoglutarate dehydrogenase during oxidative decarboxylation of alpha-ketoadipic acid.
alpha-Ketoglutarate dehydrogenase was inactivated irreversibly and completely during oxidation of alpha-ketoadipic acid. The inactivation was revealed both in the model system with ferricyanide and in the overall reaction catalyzed by the alpha-ketoglutarate dehydrogenase complex. Neither substrate depletion nor product accumulation induced the inactivation. The results obtained were compared with recent data on the enzyme inactivation during oxidation of alpha-ketoglutaric acid. The differences in the inactivation kinetics observed with the two substrates of the enzyme were analyzed. They seem not to reflect the different mechanisms of the inactivation, but, rather, depend on the changes in the rates of the individual stages of the process.
Bunik
V I
VI
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
Pavlova
O G
OG
D000272:Adipates / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D010856:Columbidae; D003653:Decarboxylation; D007655:Ketoglutarate Dehydrogenase Complex / Q000037:antagonists & inhibitors*; D007700:Kinetics; D010084:Oxidation-Reduction
D000272:Adipates; C001918:alpha-ketoadipic acid; D007655:Ketoglutarate Dehydrogenase Complex