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Succinyl phosphonate inhibits α‐ketoglutarate oxidative decarboxylation, catalyzed by α‐ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle
Author(s) -
Biryukov A.I.,
Bunik V.I.,
Zhukov Yu.N.,
Khurs E.N.,
Khomutov R.M.
Publication year - 1996
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(96)00166-4
Subject(s) - decarboxylation , oxidative decarboxylation , alpha ketoglutarate , dehydrogenase , biochemistry , oxidative phosphorylation , chemistry , phosphonate , enzyme , catalysis
Effects of a set of α‐ketoglutarate phosphoanalogues on the activity of α‐ketoglutarate dehydrogenase (EC 1.2.4.2) complexes from E. coli and pigeon breast muscle, as well as on α‐ketoglutarate dehydrogenase isolated from the pigeon breast muscle, have been studied. α‐Ketoglutarate phosphoanalogues (succinyl phosphonate and its monomethyl ester) were found to be effective inhibitors of α‐ketoglutarate oxidative decarboxylation, catalyzed by both muscle and bacterial α‐ketoglutarate dehydrogenase complexes, as well as muscle α‐ketoglutarate dehydrogenase. The ability of glutamate phosphoanalogues to inhibit α‐ketoglutarate oxidative decarboxylation has been shown in E. coli extract and a model system.