Succinyl phosphonate inhibits alpha-ketoglutarate oxidative decarboxylation, catalyzed by alpha-ketoglutarate dehydrogenase complexes from E-coli and pigeon breast muscle

被引：22

作者：

Biryukov, AI

Bunik, VI

Zhukov, YN

Khurs, EN

Khomutov, RM

机构：

[1] RUSSIAN ACAD SCI, VA ENGELHARDT MOLEC BIOL INST, MOSCOW 117984, RUSSIA

[2] MOSCOW MV LOMONOSOV STATE UNIV, DEPT BIOL, CHAIR BIOCHEM, MOSCOW, RUSSIA

来源：

FEBS LETTERS | 1996年 / 382卷 / 1-2期

关键词：

alpha-ketoglutarate dehydrogenase; alpha-ketoglutarate phosphoanalogue; glutamate phosphoanalogue; E-coli extract; transamination;

D O I：

10.1016/0014-5793(96)00166-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Effects of a set of a-ketoglutarate phosphoanalogues on the activity of alpha-ketoglutarate dehydrogenase (EC 1.2.4.2) complexes from E. coli and pigeon breast muscle, as well as on alpha-ketoglutarate dehydrogenase isolated from the pigeon breast muscle, have been studied, alpha-Ketoglutarate phosphoanalogues (succinyl phosphonate and its monomethyl ester) were found to be effective inhibitors of alpha-ketoglutarate oxidative decarboxylation, catalyzed by both muscle and bacterial alpha-ketoglutarate dehydrogenase complexes, as well as muscle alpha-ketoglutarate dehydrogenase, The ability of glutamate phosphoanalogues to inhibit alpha-ketoglutarate oxidative decarboxylation has been shown in E. coli extract and a model system.

引用

页码：167 / 170

页数：4

共 16 条

[1] SPIN-LABEL STUDY OF MOBILITY OF ENZYME-BOUND LIPOIC ACID IN PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX OF ESCHERICHIA-COLI [J].