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[Phosphorylation as a method of regulating inorganic pyrophosphatase activity in E. coli. I. Phosphorylation and enzyme activation induced by ATP]статья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 28 мая 2015 г.
- Авторы: Vener A.V., Ichetovkina L.E., Nazarova T.I., Avaeva S.M.
- Журнал: Bioorganicheskaia khimiia
- Том: 12
- Номер: 2
- Год издания: 1986
- Первая страница: 195
- Последняя страница: 199
- Аннотация: A bond formed by phosphate with Pi-phosphorylated pyrophosphatase from E. coli was found to be labile in acidic and alkaline media and to be rapidly cleaved by hydroxylamine at neutral pH. N-Methylhydroxylamine modifies also activated carboxyl groups of the enzyme. Interaction of inorganic pyrophosphatase with ATP produces an alkali-resistant phosphoamide bond. A phosphorylated amino acid, identified as phosphohistidine, was isolated from the alkaline hydrolyzate of the ATP-phosphorylated pyrophosphatase.
- Добавил в систему: Назарова Татьяна Ивановна