NAD+-dependent format dehydrogenase from the thermotolerant yeast ogataea parapolymorpha: properties and protein engineering of the n-terminal sequence
- Авторлар: Pometun A.1,2, Shaposhnikov L.1,2, Zubanova S.2, Kovalevskii R.2, Atroshenko D.1,2, Pometun E.3, Savin S.1,2, Tishkov V.1,2
-
Мекемелер:
- Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences
- Faculty of Chemistry, Lomonosov Moscow State University
- Sechenov First Moscow State Medical University
- Шығарылым: Том 88, № 9 (2023)
- Беттер: 1667-1680
- Бөлім: Articles
- URL: https://journals.rcsi.science/0320-9725/article/view/141496
- DOI: https://doi.org/10.31857/S0320972523090178
- EDN: https://elibrary.ru/WVQLMP
- ID: 141496
Дәйексөз келтіру
Аннотация
Авторлар туралы
A. Pometun
Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences;Faculty of Chemistry, Lomonosov Moscow State University
Email: aapometun@gmail.com
119071 Moscow, Russia;119991 Moscow, Russia
L. Shaposhnikov
Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences;Faculty of Chemistry, Lomonosov Moscow State University119071 Moscow, Russia;119991 Moscow, Russia
S. Zubanova
Faculty of Chemistry, Lomonosov Moscow State University119991 Moscow, Russia
R. Kovalevskii
Faculty of Chemistry, Lomonosov Moscow State University119991 Moscow, Russia
D. Atroshenko
Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences;Faculty of Chemistry, Lomonosov Moscow State University119071 Moscow, Russia;119991 Moscow, Russia
E. Pometun
Sechenov First Moscow State Medical University119991 Moscow, Russia
S. Savin
Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences;Faculty of Chemistry, Lomonosov Moscow State University119071 Moscow, Russia;119991 Moscow, Russia
V. Tishkov
Bach Institute of Biochemistry, Federal Research Centre “Fundamentals of Biotechnology” of the Russian Academy of Sciences;Faculty of Chemistry, Lomonosov Moscow State University
Email: vitishkov@gmail.com
119071 Moscow, Russia;119991 Moscow, Russia
Әдебиет тізімі
- Tishkov, V. I., and Popov, V. O. (2004) Catalytic mechanism and application of formate dehydrogenase, Biochemistry (Moscow), 69, 1252-1267, doi: 10.1007/s105410050071x.
- Tishkov, V. I., and Popov, V. O. (2006) Protein engineering of formate dehydrogenase, Biomol. Eng., 23, 89-110, doi: 10.1016/j.bioeng.2006.02.003.
- Alekseeva, A. A., Savin, S. S., and Tishkov, V. I (2011) NAD+-dependent formate dehydrogenase from plants, Acta Naturae, 3, 38-54, doi: 10.32607/20758251-2011-3-4-38-54.
- Tishkov, V. I., Pometun, A. A., and Savin, S. S. (2023) Formate dehydrogenase: from NAD(P)H regeneration to targeting pathogen biofilms, composing highly efficient hybrid biocatalysts and atmospheric CO2 fixation, Moscow Univ. Chem. Bull., 78, 151-169, doi: 10.3103/S0027131423040077.
- Kragl, U., Kruse, W., Hummel, W., and Wandrey, C. (1996) Enzyme engineering aspects of biocatalysis: cofactor regeneration as example, Biotechnol. Bioeng., 52, 309-319, doi: 10.1002/(SICI)1097-0290.
- Tishkov, V. I., Galkin, A. G., Marchenko, G. N., Tsygankov, Y. D., and Egorov, A. M. (1993) Formate dehydrogenase from methylotrophic bacterium Pseudomonas sp. 101: gene cloning and expression in Escherichia coli, Biotechnol. Appl. Biochem., 18, 201-207.
- Yu, S., Zhu, L., Zhou, C., An, T., Zhang, T., Jiang, B., and Mu, W. (2014) Promising properties of a formate dehydrogenase from a methanol-assimilating yeast Ogataea parapolymorpha DL-1 in His-tagged form, Appl. Microbiol. Biotechnol., 98, 1621-1630, doi: 10.1007/s00253-013-4996-5.
- Tishkov, V. I., Pometun, A. A., Stepashkina, A. V., Fedorchuk, V. V., Zarubina, S. A., Kargov, I. S., Atroshenko, D. L., Parshin, P. D., Kovalevski, R. P., Boiko, K. M., Eldarov, M. A., D'Oronzo, E., Facheris, S., Secundo, F., and Savin, S. S. (2018) Rational design of practically important enzymes, Moscow Univ. Chem. Bull., 73, 1-6, doi: 10.3103/S0027131418020153.
- Pometun, A. A., Kleymenov, S. Y., Zarubina, S. A., Kargov, I. S., Parshin, P. D., Sadykhov, E. G., Savin, S. S., and Tishkov, V. I. (2018) Comparison of thermal Stability of new formate dehydrogenases by differential scanning calorimetry, Moscow Univ. Chem. Bull., 73, 80-84, doi: 10.3103/S002713141802013X.
- Pometun, A. A., Boyko, K. M., Zubanova, S. A., Nikolaeva, A. Yu., Atroshenko, D. L., Savin, S. S., and Tishkov, V. I. (2021) Preparation of recombinant formate dehydrogenase from thermotolerant yeast Ogataea parapolymorpha and crystallization of its apo- and holo-forms, Moscow Univ. Chem. Bull., 76, 49-55, doi: 10.3103/S0027131421010120.
- Rojkova, A. M., Galkin, A. G., Kulakova, L. B., Serov, A. E., Savitsky, P. A., Fedorchuk, V. V., and Tishkov, V. I. (1999) Bacterial formate dehydrogenase. Increasing the enzyme thermal stability by hydrophobization of alpha-helices, FEBS Lett., 445, 183-188, doi: 10.1016/S0014-5793(99)00127-1.
- Досон Р., Эллиот Д., Эллиот У., Джонс К. (1991) Справочник биохимика, Мир, Москва, ISBN 5-03-001032-7.
- Varshavsky, A. (2011) The N-end rule pathway and regulation by proteolysis, Protein Sci., 20, 1298-1345, doi: 10.1002/pro.666.
- Klyushnichenko, V., Tishkov, V., and Kula, M.-R. (1997) Rapid SDS-gel capillary electrophoresis for the analysis of recombinant NADP+-dependent formate dehydrogenase during expression in E. coli cells and purification, J. Biotechnol., 58, 187-195, doi: 10.1016/S0168-1656(97)00149-1.
- Pometun, A. A., Parshin, P. D., Galanicheva, N. P., Uporov, I. V., Atroshenko, D. L., Savin, S. S., and Tishkov, V. I. (2020) Influence of His6 sequence on the properties of formate dehydrogenase from bacterium Pseudomonas sp. 101, Moscow Univ. Chem. Bull., 75, 250-257, doi: 10.3103/S0027131420040057.
- Shaposhnikov, L. A., Savin, S. S., Atroshenko, D. L., Chubar, T. A., Pometun, E. V., Tishkov, V. I., and Pometun, A. A. (2023) Engineering the N-terminal sequence of Glycine max soybean formate dehydrogenase, Moscow Univ. Chem. Bull., 78, 220-230, doi: 10.3103/S0027131423040053.
- Hatrongjit, R., and Packdibamrung, K. (2010) A novel NADP-dependent formate dehydrogenase from Burkholderia stabilis 15516: Screening, purification and characterization, Enzyme Microb. Technol., 46, 557-561, doi: 10.1016/j.enzmictec.2010.03.002.
- Ding, H. T., Liu, D. F., Li, Z. L., Du, Y. Q., Xu, X. H., and Zhao, Y. H. (2011) Characterization of a thermally stable and organic solvent-adaptative NAD+-dependent formate dehydrogenase from Bacillus sp. F1, J. Appl. Microbiol., 111, 1075-1085, doi: 10.1111/j.1365-2672.2011.05124.x.
- Andreadeli, A., Flemetakis, E., Axarli, I., Dimou, M., Udvardi, M. K., Katinakis, P., and Labrou, N. E. (2009) Cloning and characterization of Lotus japonicus formate dehydrogenase: a possible correlation with hypoxia, Biochim. Biophys. Acta, 1794, 976-984, doi: 10.1016/j.bbapap.2009.02.009.
- Pometun, A. A., Voinova, N. S., Pometun, E. V., Savin, S. S., and Tishkov, V. I. (2018) Effect of medium pH and ion strength on the thermal stability of plant formate dehydrogenases, Moscow Univ. Chem. Bull., 73, 199-203, doi: 10.3103/S0027131418040077.
- Cornish-Bowden, A. (2012) in Fundamentals of Enzyme Kinetic 4th Ed., Wiley-Blackwell, Singapore, p. 18-20.
- Tishkov, V. I., Goncharenko, K. V., Alekseeva, A. A., Kleymenov, S. Yu, and Savin, S. S. (2015) Role of a structurally equivalent phenylalanine residue in catalysis and thermal stability of formate dehydrogenases from different sources, Biochemistry (Moscow), 80, 1690-1700, doi: 10.1134/S0006297915130052.
![](/img/style/loading.gif)