Benzimidazoles as competitive inhibitors of FAD-monooxygenase

Zakhariants, A.A.; Poloznikov, A.A.; Hushpulian, D.M.; Osipova, T.A.; Tishkov, V.I.; Gazaryan, I.G.

Информация о цитировании статьи получена из Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 6 апреля 2016 г.

Авторы: Zakhariants A.A., Poloznikov A.A., Hushpulian D.M., Osipova T.A., Tishkov V.I., Gazaryan I.G.
Журнал: Moscow University Chemistry Bulletin
Том: 70
Номер: 6
Год издания: 2015
Издательство: Allerton Press Inc.
Местоположение издательства: United States
Первая страница: 261
Последняя страница: 267
DOI: 10.3103/S0027131415060073
Аннотация: Benzimidazoles represent the drugs targeting tubulin and widely used to treat intestinal parasites. Four benzimidazoles were tested with the well-characterized and commercially available bacterial para-hydroxybenzoate hydroxylase (PHBH), which belongs to the group of FAD-dependent monooxygenases class A including such enzymes as FAD-containing monooxygenase domain of MICAL. PHBH was shown to be competitively inhibited by all four benzimidazoles (mebendazole, albendazole, fenbendazole, oxibendazole) in the micromolar range in the hydroxylase reaction, but not in the non-physiological NADPH-dehydrogenase reaction of ferricyanide reduction. Inhibition pattern is consistent with benzimidazoles competing with para-hydroxybenzoate for the resting state of the enzyme, indirectly indicating the ordered mechanism of substrate binding. Modeling studies support the conclusions derived from steady-state kinetics.
Добавил в систему: Тишков Владимир Иванович

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Benzimidazoles as competitive inhibitors of FAD-monooxygenaseстатья

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