Search Results - "Polyakov, K. M"

Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutant by Mitkevich, V. A., Schulga, A. A., Trofimov, A. A., Dorovatovskii, P. V., Goncharuk, D. A., Tkach, E. N., Makarov, A. A., Polyakov, K. M.

“…Ribonuclease from Bacillus intermedius (binase) is a small basic protein with antitumour activity. The three‐dimensional structure of the binase mutant form…”
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Structural study of the X‐ray‐induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism by Polyakov, K. M., Gavryushov, S., Ivanova, S., Fedorova, T. V., Glazunova, O. A., Popov, A. N., Koroleva, O. V.

“…The laccase from Steccherinum murashkinskyi is a member of the large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and…”
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RNA-dependent RNA polymerase of hepatitis C virus: Study on inhibition by α,γ-diketo acid derivatives by Kozlov, M. V, Polyakov, K. M, Filippova, S. E, Evstifeev, V. V, Lyudva, G. S, Kochetkov, S. N

“…It is supposed that α,γ-diketo acids (DKAs) inhibit the activity of hepatitis C virus RNA-dependent RNA poly-merase (RdRP HCV) via chelation of catalytic…”
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ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain by Petrova, T., Bezsudnova, E. Y., Boyko, K. M., Mardanov, A. V., Polyakov, K. M., Volkov, V. V., Kozin, M., Ravin, N. V., Shabalin, I. G., Skryabin, K. G., Stekhanova, T. N., Kovalchuk, M. V., Popov, V. O.

“…DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl…”
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The Thermostability of Nucleoside Phosphorylases from Prokaryotes. I. The Role of the Primary Structure of the N-terminal fragment of the Protein in the Thermostability of Uridine Phosphorylases by Veiko, V. P., Antipov, A. N., Mordkovich, N. N., Okorokova, N. A., Safonova, T. N., Polyakov, K. M.

“…Mutant uridine phosphorylase genes from Shewanella oneidensis MR-1 ( S. oneidensis ) were constructed by site-directed mutagenesis and strains-producers of the…”
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Improvement of the Diffraction Properties of Thiocyanate Dehydrogenase Crystals by Varfolomeeva, L. A., Polyakov, K. M., Komolov, A. S., Rakitina, T. V., Dergousova, N. I., Dorovatovskii, P. V., Boyko, K. M., Tikhonova, T. V., Popov, V. O.

“…During determination of the thiocyanate dehydrogenase (TcDH) structure difficulties have occurred, related to the fact that enzyme crystals have been either…”
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Preliminary X-ray Diffraction Analysis of Purine Nucleoside Phosphorylase from the Haloalkaliphilic Bacterium Halomonas chromatireducens by Safonova, T. N., Antipov, A. N., Veiko, V. P., Mordkovich, N. N., Okorokova, N. A., Dorovatovskii, P. V., Polyakov, K. M.

“…Crystals of the enzyme purine nucleoside phosphorylase from the extremophilic bacterium Halomonas Chromatireducens AGD 8-3, suitable for X-ray diffraction,…”
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Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus by Trofimov, A. A., Slutskaya, E. A., Polyakov, K. M., Dorovatovskii, P. V., Gumerov, V. M., Popov, V. O.

“…Prolidases are peptidases that are specific for dipeptides with proline as the second residue. The structure of recombinant prolidase from the…”
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Substrate specificity of Escherichia coli thymidine phosphorylase by Panova, N G, Alexeev, C S, Kuzmichov, A S, Shcheveleva, E V, Gavryushov, S A, Polyakov, K M, Kritzyn, A M, Mikhailov, S N, Esipov, R S, Miroshnikov, A I

“…Substrate specificity of Escherichia coli thymidine phosphorylase to thymidine derivatives modified at 5' -, 3' -, and 2' ,3' - positions of the sugar moiety…”
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Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding by Polyakov, K. M., Mordkovich, N. N., Safonova, T. N., Antipov, A. N., Okorokova, N. A., Dorovatovskii, P. V., Veiko, V. P.

“…Crystals of mutants of uridine phosphorylase from Shewanella oneidensis MR-1 at the active-site threonine residue were obtained, and the three-dimensional…”
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X-ray diffraction and biochemical studies of W34F mutant ribonuclease binase by Polyakov, K. M, Goncharuk, D. A, Trofimov, A. A, Safonova, T. N, Mitkevich, V. A, Tkach, E. N, Makarov, A. A, Shulga, A. A

“…The structures of two crystal modifications of the W34F mutant ribonuclease from the bacterium Bacillus intermedius (binase) were solved and refined at 1.7 and…”
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Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens by Tikhonova, T. V, Slutskaya, E. S, Filimonenkov, A. A, Boyko, K. M, Kleimenov, S. Yu, Konarev, P. V, Polyakov, K. M, Svergun, D. I, Trofimov, A. A, Khomenkov, V. G, Zvyagilskaya, R. A, Popov, V. O

“…A new procedure for isolation of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens increasing significantly…”
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Concerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme by Safonova, T. N., Mordkovich, N. N., Veiko, V. P., Okorokova, N. A., Manuvera, V. A., Dorovatovskii, P. V., Popov, V. O., Polyakov, K. M.

“…Uridine phosphorylase (UP; EC 2.4.2.3), a key enzyme in the pyrimidine‐salvage pathway, catalyzes the reversible phosphorolysis of uridine to uracil and ribose…”
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Structural study of the X-ray-induced enzymatic reaction of octahaem cytochrome c nitrite reductase by Trofimov, A. A., Polyakov, K. M., Lazarenko, V. A., Popov, A. N., Tikhonova, T. V., Tikhonov, A. V., Popov, V. O.

“…Octahaem cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens catalyzes the reduction of nitrite to ammonium and of sulfite to…”
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Study of Structural-Functional Organization of Nucleoside Phosphorylases of Gammaproteobacteria. Special Aspects of Functioning of Uridine Phosphorylase Phosphate-Binding Site by Mordkovich, N. N., Safonova, T. N., Antipov, A. N., Manuvera, V. A., Polyakov, K. M., Okorokova, N. A., Veiko, V. P.

“…Series of mutant genes of prokaryotic uridine phosphorylases ( Shewanella oneidensis MR-1, Escherichia coli ) were constructed, and the resulting…”
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Incorporation of copper ions into crystals of T2 copper-depleted laccase from Botrytis aclada by Osipov, E. M., Polyakov, K. M., Tikhonova, T. V., Kittl, R., Dorovatovskii, P.V., Shleev, S. V., Popov, V. O., Ludwig, R.

“…Laccases belong to the class of multicopper oxidases catalyzing the oxidation of phenols accompanied by the reduction of molecular oxygen to water without the…”
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Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleft by Shabalin, I. G., Filippova, E. V., Polyakov, K. M., Sadykhov, E. G., Safonova, T. N., Tikhonova, T. V., Tishkov, V. I., Popov, V. O.

“…NAD+‐dependent formate dehydrogenase (FDH) catalyzes the oxidation of formate ion to carbon dioxide coupled with the reduction of NAD+ to NADH. The crystal…”
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Purification, biochemical characterization, and structure of recombinant endo-1,4-β-xylanase XylE by Fedorova, T. V., Chulkin, A. M., Vavilova, E. A., Maisuradze, I. G., Trofimov, A. A., Zorov, I. N., Khotchenkov, V. P., Polyakov, K. M., Benevolensky, S. V., Koroleva, O. V., Lamzin, V. S.

“…The gene xylE encoding endo-1,4-β-xylanase from the 10th family of glycosyl hydrolases produced by the mycelial fungus Penicillium canescens has been expressed…”
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Structures of β-glycosidase from Acidilobus saccharovorans in complexes with tris and glycerol by Trofimov, A. A., Polyakov, K. M., Tikhonov, A. V., Bezsudnova, E. Y., Dorovatovskii, P. V., Gumerov, V. M., Ravin, N. V., Skryabin, K. G., Popov, V. O.

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Physicochemical characterization of uridine phosphorylase from Shewanella oneidensis MR-1 by Mordkovich, N. N., Safonova, T. N., Manuvera, V. A., Veiko, V. P., Polyakov, K. M., Alekseev, K. S., Mikhailov, S. N., Popov, V. O.

“…Uridine phosphorylase (UP) belongs to nucleoside phosphorylases that play an important role in nucleoside metabolism. These enzymes exhibit an elevated level…”
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