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Bacterial formate dehydrogenase. Substrate specificity and kinetic mechanism of S-formyl glutathione oxidationстатья
Дата последнего поиска статьи во внешних источниках: 20 апреля 2016 г.
- Авторы: Tishkov V.I., Egorov A.M., Popov V.O.
- Журнал: Biochemistry (Moscow)
- Том: 48
- Номер: 7
- Год издания: 1983
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1172
- Последняя страница: 1180
- Аннотация: The substrate specificity of NAD-dependent formate dehydrogenase from the methylotrophic bacterium Achromobacter parvulus T1 was studied. The kinetic mechanism of S-formyl glutathione oxidation was determined. The initial velocity studies and inhibition analysis were carried out. It was shown that the kinetic mechanism for the enzyme with S-formyl glutathione as a substrate is similar to that with formate and is rapid-equilibrium random. Using independent methods, it was found that formate dehydrogenase forms a binary complex with S-formyl glutathione (Kd = 2.5 mM).
- Добавил в систему: Тишков Владимир Иванович