Premium
Inactivation of α‐ketoglutarate dehydrogenase during oxidative decarboxylation of α‐ketoadipic acid
Author(s) -
Bunik V.I.,
Pavlova O.G.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81472-c
Subject(s) - decarboxylation , oxidative decarboxylation , oxidative phosphorylation , chemistry , biochemistry , dehydrogenase , enzyme , catalysis
α‐Ketoglutarate dehydrogenase was inactivated irreversibly and completely during oxidation of α‐ketoadipic acid. The inactivation was revealed both in the model system with ferricyanide and in the overall reaction catalyzed by the α‐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 α‐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.