Výsledky vyhledávání - "D L, Atroshenko"

Mechanism of the Antioxidant Activity and Structure–Activity Relationship of N-Monosubstituted Amino Acid Derivatives of Fullerene С60

Autor: D. V. Kurilov, M. V. Voronkov, L. Yu. Martirosyan, N. N. Sazhina, V. A. Volkov, D. L. Atroshenko, V. S. Romanova, Olga Yamskova, D. V. Vokhmyanina, Yu. Ts. Martirosyan

Publikováno v: Kinetics and Catalysis. 62:395-403

Abstract The kinetic characteristics, mechanisms of activity, and relationship between the antioxidant activity and the molecular and supramolecular structure of fullerene C60 and some of its N-monosubstituted amino acid derivatives have been studied

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5fb573369fc136be226a2209fa1c9e95
https://doi.org/10.1134/s0023158421030095

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Preparation of Recombinant Formate Dehydrogenase from Thermotolerant Yeast Ogataea parapolymorpha and Crystallization of Its Apo- and Holo- Forms

Autor: Konstantin M. Boyko, D. L. Atroshenko, A. Yu. Nikolaeva, Vladimir I. Tishkov, A. A. Pometun, S. S. Savin, S. A. Zubanova

Publikováno v: Moscow University Chemistry Bulletin. 76:49-55

NAD+-dependent formate dehydrogenase from thermotolerant yeast Ogataea parapolymorpha DL-1 (OpaFDH, EC 1.2.1.2) with the additional N-terminal Gly residue and its double mutant OpaFDH_AD were overexpressed in E. coli cells. The enzyme yield was, resp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e7b72095e56a4109fcc66db2deeb387b
https://doi.org/10.3103/s0027131421010120

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Influence of His6 Sequence on the Properties of Formate Dehydrogenase from Bacterium Pseudomonas sp. 101

Autor: N. P. Galanicheva, D. L. Atroshenko, Vladimir I. Tishkov, A. A. Pometun, P. D. Parshin, S. S. Savin, I. V. Uporov

Publikováno v: Moscow University Chemistry Bulletin. 75:250-257

NAD(P)+-dependent formate dehydrogenase (FDH, EC 1.2.1.2.) is actively used in processes of chiral synthesis by oxidoreductases with systems of reduced cofactor regeneration. The efficient use of FDH in such systems requires simple and fast enzyme pu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::79d2ba69d478af62d353f9e01bc70203
https://doi.org/10.3103/s0027131420040057

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Effect of His6-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fusca

Autor: P. D. Parshin, U A Martysuk, D. L. Atroshenko, A. A. Pometun, S. S. Savin, Vladimir I. Tishkov, E. V. Pometun, S. Yu. Kleymenov

Publikováno v: Biochemistry (Moscow). 85:575-582

Phenylacetone monooxygenase (EC 1.14.13.92, PAMО) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters. PAMО is a promising enzyme for biotechnological processes. In this work, we generated genetic constructs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b19c713800e2b7c1c33043c1d564bb96
https://doi.org/10.1134/s0006297920050065

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Determination of the Kinetic Parameters of a Wild-Type D-Amino Acid Oxidase from Yeast and Its Mutant Forms in a Reaction of Cephalosporin C Oxidation

Autor: S. S. Savin, Vladimir I. Tishkov, D. L. Atroshenko, A. A. Pometun

Publikováno v: Moscow University Chemistry Bulletin. 74:169-172

The oxidation of cephalosporin C (CPC) by D-amino acid oxidase is the first stage in the biocatalytic industrial process of the production of 7-aminocephalosporanic acid, the initial synthon for the production of semisynthetic cephalosporin antibioti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b6f4251948f1037d2761cd6f9ba8e0ea
https://doi.org/10.3103/s0027131419040023

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Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and Crystallization

Autor: Vladimir I. Tishkov, Vladimir Popov, A. Yu. Nikolaeva, Konstantin M. Boyko, D. L. Atroshenko, A. A. Pometun, I.S. Kargov, S. S. Savin, T.S. Yurchenko

Publikováno v: Biochemistry. Biokhimiia. 85(6)

These authors contributed equally to the work. NAD+-dependent formate dehydrogenase from Staphylococcus aureus (SauFDH) is one of the key enzymes responsible for the survival of this pathogen in the form of biofilms. 3D structure of the enzyme might

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2712a0799b178440c194d0828f130f1d
https://pubmed.ncbi.nlm.nih.gov/32586232

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