Rational design of practically important enzymes

Tishkov, V.I.; Pometun, A.A.; Stepashkina, A.V.; Fedorchuk, V.V.; Zarubina, S.A.; Kargov, I.S.; Atroshenko, D.L.; Parshin, P.D.; Shelomov, M.D.; Kovalevski, R.P.; Boiko, K.M.; Eldarov, M.A.; D'Oronzo, E.; Facheris, S.; Secundo, F.; Savin, S.S.

Авторы: Tishkov V.I., Pometun A.A., Stepashkina A.V., Fedorchuk V.V., Zarubina S.A., Kargov I.S., Atroshenko D.L., Parshin P.D., Shelomov M.D., Kovalevski R.P., Boiko K.M., Eldarov M.A., D'Oronzo E., Facheris S., Secundo F., Savin S.S.
Журнал: Moscow University Chemistry Bulletin
Том: 73
Номер: 1
Год издания: 2018
Издательство: Allerton Press Inc.
Местоположение издательства: United States
Первая страница: 1
Последняя страница: 6
DOI: 10.3103/S0027131418020153
Аннотация: Majority of native enzymes are poorly applicable for practical usage: that is why different methods of enzyme modification are used to obtain the biocatalysts with appropriate characteristics. Development of genome sequencing and various modern approaches in protein engineering allow one to identify protein of interest and to improve the enzyme properties for a particular process. This review describes the results on development of novel biocatalysts based on bioinformatics and rational design. New genes encoding formate dehydrogenase (FDH) from bacteria Staphylococcus aureus, yeasts Ogataea parapolymorpha and Saccharomyces cerevisiae and moss Physcomitrella patens (SauFDH, OpaFDH, SceFDH and PpaFDH, respectively), have been cloned. New FDHs were produced in the active form and characterized. SauFDH was shown to have at least 2-fold higher catalytic constant than other known FDHs. OpaFDH has catalytic parameters as good as those for soy FDH mutant forms, and in addition, is more thermostable. Apo- and holo-forms of SauFDH have been crystallized. Mutation of two Cys residues in Pseudomonas sp.101 enzyme (PseFDH) yields enzyme preparations with improved kinetic parameters and enhanced thermal and chemical stability. New generation of PseFDH preparations with the coenzyme specificity changed from NAD+ to NADP+ have been obtained. The effect of ionic liquids on the catalytic properties and thermal stability of six wild-type recombinant FDHs, and a number of their mutants, have been studied.
Добавил в систему: Тишков Владимир Иванович

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