期刊论文详细信息
FEBS Letters
Succinyl phosphonate inhibits α‐ketoglutarate oxidative decarboxylation, catalyzed by α‐ketoglutarate dehydrogenase complexes from E. coli and pigeon breast muscle
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.
PDF
【 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   

【 预 览 】
附件列表
Files Size Format View
RO201912020302462ZK.pdf 428KB PDF download
  文献评价指标  
  下载次数:6次 浏览次数:5次