Comparison of Thermal Stability of New Formate Dehydrogenases by Differential Scanning Calorimetry

被引：7

作者：

Pometun A.A. ^{[1
,2
]}

Kleymenov S.Y. ^{[1
,4
]}

Zarubina S.A. ^{[2
,3
]}

Kargov I.S. ^{[1
,2
,3
]}

Parshin P.D. ^{[2
,3
]}

Sadykhov E.G. ^{[1
]}

Savin S.S. ^{[2
,3
]}

Tishkov V.I. ^{[1
,2
,3
]}

机构：

[1] Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology,”, Russian Academy of Sciences, Moscow

[2] Innovations and High Technologies MSU Ltd., Moscow

[3] Department of Chemistry, Moscow State University, Moscow

[4] Koltzov Institute of Developmental Biology, Russian Academy of Sciences, Moscow

来源：

Moscow University Chemistry Bulletin | 2018年 / 73卷 / 2期

基金：

俄罗斯科学基金会; 俄罗斯基础研究基金会;

关键词：

differential scanning calorimetry; formate dehydrogenase; thermal stability;

D O I：

10.3103/S002713141802013X

中图分类号：

学科分类号：

摘要：

Formate dehydrogenases (FDHs) from different sources are systematically studied in our laboratory. Over the past few years, new genes of four FDHs from pathogenic bacterium Staphylococcus aureus (SauFDH), methylotrophic thermotolerant yeast Ogataea parapolymorpha (OpaFDH), yeast Saccharomyces cerevisiae (SceFDH), and moss Physcomitrella patens (PpaFDH) have been cloned and expressed in E. coli cells. By means of differential scanning calorimetry, a comparative study of thermal stability of new recombinant formate dehydrogenases and a number of FDHs from other sources has been performed. It was shown that two new enzymes, SauFDH and OpaFDH, are comparable to the FDH from Pseudomonas sp. 101 bacteria in their stability. SceFDH is the least stable FDH among the described formate dehydrogenases. © 2018, Allerton Press, Inc.

引用

页码：80 / 84

页数：4

共 12 条

[1] Tishkov V.I., Popov V.O., Biochemistry (Moscow), 69, 11, (2004)
[2] Tishkov V.I., Popov V.O., Biomol. Eng., 23, 2-3, (2006)
[3] Alekseeva A.A., Savin S.S., Tishkov V.I., Acta Naturae, 3, 11, (2011)
[4] Hummel W., Kula M.R., Eur. J. Biochem., 184, 1, (1989)
[5] Tishkov V.I., Matorin A.D., Rojkova A.M., Fedorchuk V.V., Savitsky A.P., Dementieva L.A., Lamzin V.S., Mezentzev A.V., Popov V.O., FEBS Lett., 390, 1, (1996)
[6] Fedorchuk V.V., Galkin A.G., Yasny I.E., Kulakova L.B., Rojkova A.M., Filippova A.A., Tishkov V.I., Biochemistry (Moscow), 67, 10, (2002)
[7] Alekseeva A.A., Fedorchuk V.V., Zarubina S.A., Sadykhov E.G., Matorin A.D., Savin S.S., Tishkov V.I., Acta Naturae, 7, 1, (2015)
[8] Alekseeva A.A., Serenko A.A., Kargov I.S., Savin S.S., Kleymenov S.Y., Tishkov V.I., Protein Eng., Des. Sel., 25, 11, (2012)
[9] Kargov I.S., Kleymenov S.Y., Savin S.S., Tishkov V.I., Alekseeva A.A., Protein Eng., Des. Sel., 28, 6, (2015)
[10] Tishkov V.I., Goncharenko K.V., Alekseeva A.A., Kleymenov S.Y., Savin S.S., Biochemistry (Moscow), 80, 13, (2015)

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