Essential role of coenzyme A in pyruvate dehydrogenase kinase activity

FEBS Letters

Siess, E.A.¹  Weiland, O.H.¹ 

[1] Forschergruppe Diabetes and Institut für Klinische Chemie, Städtisches Krankenhaus München-Schwabing, Kölner Platz 1, D-8000 München 40, FRG

关键词: Pyruvate dehydrogenase kinase;    Phosphorylation;    Coenzyme A;    Heart muscle;   

DOI  :  10.1016/0014-5793(82)80808-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The rate of phosphorylation and concomitant inactivation of purified pig heart muscle pyruvate dehydrogenase complex by intrinsic kinase (EC 2.7.1.99) is markedly accelerated by the addition of coenzyme A to the incubation medium, showing a half-maximum effect at 1.8 μM. The pantetheine moiety is the effective part of the coenzyme A molecule. The free thiol group is prerequisite for the stimulatory action, acetyl-CoA, benzoyl-CoA or CoAS-SCoA being ineffectual. The thiol's specificity is evidenced by showing that dithiothreitol, 2-mercaptoethanol or glutathione up to 5 mM failed to replace coenzyme A. The possibility is considered that coenzyme A might act as a physiological modifier of pyruvate dehydrogenase kinase activity.

【 授权许可】

Unknown