Use of ramachandran plot for increasing thermal stability of bacterial formate dehydrogenase

Serov, A.E.; Odintzeva, E.R.; Uporov, I.V.; Tishkov, V.I.

Информация о цитировании статьи получена из Web of Science, Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.

Авторы: Serov A.E., Odintzeva E.R., Uporov I.V., Tishkov V.I.
Журнал: Biochemistry (Moscow)
Том: 70
Номер: 7
Год издания: 2005
Издательство: Pleiades Publishing, Ltd
Местоположение издательства: Road Town, United Kingdom
Первая страница: 804
Последняя страница: 808
DOI: 10.1007/s10541-005-0187-z
Аннотация: From analysis of Ramachandran plot for NAD(+)-dependent formate dehydrogenase from the methylotrophic bacterium Pseudomonas sp. 101 (FDH, EC 1.2.1.2), five amino acid residues with non-optimal values phi and gamma have been located in beta- and pi-turns of the FDH polypeptide chain, e.g., Asn 136, Ala191, Tyr144, Asn234, and His263. To clarify their role in the enzyme stability, the residues were replaced with Gly by means of site-directed mutagenesis. The His263Gly mutation caused FDH destabilization and a 1.3-fold increase in the monomolecular inactivation rate constant. The replacements Ala191Gly and Asn234Gly had no significant effect on the stability The mutations Asn136Gly and Tyr144Gly resulted in higher thermal stability and decreased the inactivation rate by 1.2- and 1.4-fold, respectively. The stabilizing effect of the Tyr144Gly mutation was shown to be additive when introduced into the previously obtained mutant FDH with enhanced thermal stability.
Добавил в систему: Упоров Игорь Владимирович

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Use of ramachandran plot for increasing thermal stability of bacterial formate dehydrogenaseстатья

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