Succinyl phosphonate inhibits α‐ketoglutarate oxidative decarboxylation, catalyzed by α‐ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle

FEBS Letters

Zhukov, Yu.N.²  Khurs, E.N.²  Biryukov, A.I.²  Bunik, V.I.¹  Khomutov, R.M.² 

[1] Chair of Biochemistry, Biological Department of M.V. Lomonosov, Moscow State University, Moscow, Russia;V.A. Engelhardt Institute of Molecular Biology, RAS, Vavilov st. 32, 117984 Moscow, Russia

关键词: α-Ketoglutarate dehydrogenase;    α-Ketoglutarate phosphoanalogue;    Glutamate phosphoanalogue;    E. coli extract;    Transamination;    Pyr;    pyruvate;    α-Kglu;    α-ketoglutarate;    Oxa;    oxaloacetate;    Suc-P;    succinyl phosphonate;    Suc-P II;    succinyl phosphinate;    Ac-P;    acetyl phosphonate;    Ac-PH;    acetyl phosphinate;    Glu-P;    glutamyl phosphonate;    Glu-PH;    glutamyl phosphinate;    α-KGDC;    α-ketoglutarate dehydrogenase complex;    α-KGD;    α-ketoglutarate dehydrogenase;   

DOI  :  10.1016/0014-5793(96)00166-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown