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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Formate dehydrogenase from Staphylococcus aureus: preparation, crystallization and pre-liminary structure analysisтезисы доклада
- Авторы: Kargov I.S., Alekseeva A.A., Boyko K.M., Popov V.O., Savin S.S., Tishkov V.I.
- Сборник: Program and Abstract Book of International Conference "Biocatalysis-2015: Fundamentals and Applications", Moscow region, Avantel Club Istra
- Тезисы
- Год издания: 2015
- Место издания: Innovations and High Technologies MSU Ltd Moscow
- Первая страница: 108
- Последняя страница: 108
- Аннотация: NAD+-dependent formate dehydrogenase (EC 1.2.1.2., FDH) is found in a wide range of living organisms, from bacteria and yeast to plants and fungi. FDH plays a significant role in the cell life main-tainance, as it is a stress enzyme, thus its expression rises at stress conditions. Many pathogenic microorganisms can form biofilms to survive in and to adapt themselves to different strict conditions. The expression level of FDH in Staphylococcus aureus, a widespread patho-genic bacterium, increases, when the bacterium is in the form of a biofilm. Irreversible inhibition of this enzyme can be a way to combat such a pathogen. Thus thorough analysis of this enzyme is of great sci-entific and practical interest. Our laboratory carries out systematic studies of formate dehydrogenases from different natural sources, and now we are focused on the bacterial FDH from S. aureus (SauFDH). Examination of a significant number of amino acid sequences of different FDHs revealed, that this enzyme shows very poor homology with FDHs from other sources. The gene, coding SauFDH was cloned and expressed in E. coli. We also carried out a major cultivation of the enzyme (yielding more than 500 mg per liter of nutrient solution) and developed a high-efficient purification system. Analysis of the SauFDH properties showed both advantages and disadvantages of the enzyme. On the one hand, it possesses high thermal stability in comparison with FDHs from other sources and an outstanding catalytic constant. On the other hand, values of Michaelis constants both for NAD+ and formate are extraordinary high, compared to ones for FDHs from bacteria, yeast and plants. This study was supported by Russian Foundation for Basic Research (grants 14-04-32042-mol_a).
- Добавил в систему: Тишков Владимир Иванович