Výsledky vyhledávání

Rational Design of Practically Important Enzymes

Autor: I. S. Kargov, Vladimir I. Tishkov, A.V. Stepashkina, V. V. Fedorchuk, M. D. Shelomov, P. D. Parshin, Francesco Secundo, E. D’Oronzo, K. M. Boiko, S. Facheris, Michael A. Eldarov, S. A. Zarubina, S. S. Savin, R. P. Kovalevski, A. A. Pometun, D. L. Atroshenko

Publikováno v: Moscow University chemistry bulletin 73 (2018): 70–77. doi:10.3103/S0027131418020153
info:cnr-pdr/source/autori: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./titolo:Rational Design of Practically Important Enzymes/doi:10.3103%2FS0027131418020153/rivista:Moscow University chemistry bulletin/anno:2018/pagina_da:70/pagina_a:77/intervallo_pagine:70–77/volume:73

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 appro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7b49225f1596434c566d90c93d6673
https://doi.org/10.3103/s0027131418020153

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Isolation, purification, crystallization, and preliminary X-ray diffraction study of the crystals of HU protein from M. gallisepticum

Autor: D. A. Korzhenevskii, A. Yu. Nikolaeva, A. V. Lipkin, Vladimir I. Timofeev, K. M. Boiko, Tatiana V. Rakitina, Pavel V. Dorovatovskii

Publikováno v: Crystallography Reports. 60:880-883

HU proteins are involved in bacterial DNA and RNA repair. Since these proteins are absent in cells of higher organisms, inhibitors of HU proteins can be used as effective and safe antibiotics. The crystallization conditions for the M. gallisepticum H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::afa2c605337e988612e41037ac6fe6a9
https://doi.org/10.1134/s1063774515060231

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A novel approach to studying the structural and functional properties of proteins with unknown functions

Autor: A. G. Yarosh, I.A. Shumilin, K. M. Boiko, M.A. Gorbacheva, A. V. Lipkin, D. A. Korzhenevskii, Vladimir Popov, Pavel V. Dorovatovskii, Tatiana V. Rakitina

Publikováno v: Russian Journal of Bioorganic Chemistry. 38:83-88

Three proteins from extremophilic bacteria—hypothetical monooxygenase from Deinococcus radiodurans, hypothetical nucleotidyl transferase from Thermotoga maritime, and hypothetical oxidoreductase from Exiguobacterium sibiricum—and the DJ-1 chapero

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f54f78ca5cb0936d9b99a2f875ecb020
https://doi.org/10.1134/s1068162012010098

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Crystal structures of complexes of NAD+-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp. 101 with formate

Autor: T.N. Stekhanova, K. M. Boiko, Vladimir I. Tishkov, I. G. Sadykhov, Tamara V. Tikhonova, Konstantin M. Polyakov, Vladimir Popov, E.V. Filippova, N. Labru

Publikováno v: Crystallography Reports. 51:627-631

Formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 catalyzes oxidation of formate to NI2 with the coupled reduction of nicotinamide adenine dinucleotide (NAD+). The three-dimensional structures of the apo form (the free

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::06cd9f98739976714dd55f0e21175cd9
https://doi.org/10.1134/s1063774506040146

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Structure of a new crystal modification of the bacterial NAD-dependent formate dehydrogenase with a resolution of 2.1 Å

Autor: Tamara V. Tikhonova, T.N. Stekhanova, K. M. Boiko, Vladimir Popov, E.V. Filippova, Konstantin M. Polyakov

Publikováno v: Crystallography Reports. 50:796-800

Formate dehydrogenase (FDG) from methylotrophic bacteria Pseudomonas sp. 101 catalyzes the reaction of oxidation of the formate ion to carbon dioxide, which is accompanied by the reduction of nicotinamid adenine dinucleotide (NAD+). The structures of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3f448612e6d14f6dd7d4123552840633
https://doi.org/10.1134/1.2049398

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