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The effect of phosphorylation on catalytic function of muscle pyruvate dehydrogenase complexстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 28 декабря 2015 г.
- Авторы: Korochkina LG, Khailova LS, Severin SE
- Журнал: Biochemistry (Moscow)
- Том: 58
- Номер: 10
- Год издания: 1993
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1503
- Последняя страница: 1512
- Аннотация: It has been shown that phosphorylation of the pyruvate dehydrogenase complex from pigeon breast muscle by endogenous ATP-dependent protein kinase suppresses the substrate conversion in the pyruvate: acceptor oxidoreductase reactions and nonoxidative reactions monitored by pyruvate decline in the absence of CoA and NAD. To identify the catalytic step blocked by phosphorylation, CD spectroscopy was used which revealed the appearance and decay of the charge transfer complex between component E1 and thiamine pyrophosphate during the enzymatic reaction. Phosphorylation of the pyruvate dehydrogenase complex while lowering the affinity for thiamine pyrophosphate does not preclude the formation of holo-E1 but inhibits its interaction with pyruvate. Phosphorylated pyruvate dehydrogenase, like the dephosphorylated enzyme, reacts with 2-hydroxyethyl thiamine pyrophosphate in half of the active sites. In the presence of deacylating agents (CoA or dithiothreitol) all the sites are reactive. A conclusion is drawn that the alternating functioning of the active centers is preserved in reductive acetylation of the acceptor substrates by phospho-E1.
- Добавил в систему: Хайлова Людмила Самуиловна