Binding of thiamin thiazolone pyrophosphate to mammalian pyruvate dehydrogenase and its effects of kinase and phosphatase activities.
Binding of thiamin thiazolone pyrophosphate to mammalian pyruvate dehydrogenase and its effects of kinase and phosphatase activities.
复制标题
硫胺素噻唑酮焦磷酸与哺乳动物丙酮酸脱氢酶的结合及其对激酶和磷酸酶活性的影响。
DOI：
10.1016/0006-291x(77)90636-2
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发表时间：
1977
影响因子：
3.1
通讯作者：
Lester J. Reed
中科院分区：
文献类型：
--
作者：
James R. Butler;F. Pettit;P. Davis;Lester J. Reed
The pyruvate dehydrogenase component of the bovine kidney pyruvate dehydrogenase complex has two thiamin-PP binding sites perα2β2tetramer. Titration of these binding sites with the transition state analog, thiamin thiazolone pyrophosphate, strongly inhibits phosphorylation of pyruvate dehydrogenase by pyruvate dehydrogenase kinase and ATP. The analog has little effect, if any, on dephosphorylation of phosphorylated pyruvate dehydrogenase by pyruvate dehydrogenase phosphatase. Phosphorylation of pyruvate dehydrogenase inactivates the enzyme, but does not significantly affect the thiamin-PP binding sites. It appears that phosphorylation produces a conformational change in pyruvate dehydrogenase that displaces a catalytic group (or groups) at the active center.
