Search Results - "Matyuta, Ilya O"

Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from Blastococcus saxobsidens by Shilova, Sofia A., Matyuta, Ilya O., Petrova, Elizaveta S., Nikolaeva, Alena Y., Rakitina, Tatiana V., Minyaev, Mikhail E., Boyko, Konstantin M., Popov, Vladimir O., Bezsudnova, Ekaterina Yu

“…Enzymes with expanded substrate specificity are good starting points for the design of biocatalysts for target reactions. However, the structural basis of the…”
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To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme from Aminobacterium colombiense by Shilova, Sofia A, Khrenova, Maria G, Matyuta, Ilya O, Nikolaeva, Alena Y, Rakitina, Tatiana V, Klyachko, Natalia L, Minyaev, Mikhail E, Boyko, Konstantin M, Popov, Vladimir O, Bezsudnova, Ekaterina Yu

“…Pyridoxal-5'-phosphate (PLP)-dependent transaminases are highly efficient biocatalysts for stereoselective amination. D-amino acid transaminases can catalyze…”
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Friunavirus Phage-Encoded Depolymerases Specific to Different Capsular Types of Acinetobacter baumannii by Timoshina, Olga Y, Kasimova, Anastasia A, Shneider, Mikhail M, Matyuta, Ilya O, Nikolaeva, Alena Y, Evseev, Peter V, Arbatsky, Nikolay P, Shashkov, Alexander S, Chizhov, Alexander O, Shelenkov, Andrey A, Mikhaylova, Yulia V, Slukin, Pavel V, Volozhantsev, Nikolay V, Boyko, Konstantin M, Knirel, Yuriy A, Miroshnikov, Konstantin A, Popova, Anastasia V

“…is a critical priority nosocomial pathogen that produces a variety of capsular polysaccharides (CPSs), the primary receptors for specific depolymerase-carrying…”
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Structure-Functional Examination of Novel Ribonucleoside Hydrolase C (RihC) from Limosilactobacillus reuteri LR1 by Shaposhnikov, Leonid A, Chikurova, Natalia Yu, Atroshenko, Denis L, Savin, Svyatoslav S, Kleymenov, Sergei Yu, Chernobrovkina, Alla V, Pometun, Evgenii V, Minyaev, Mikhail E, Matyuta, Ilya O, Hushpulian, Dmitry M, Boyko, Konstantin M, Tishkov, Vladimir I, Pometun, Anastasia A

“…Ribonucleoside hydrolase C (RihC, EC 3.2.2.1, 3.2.2.2, 3.2.2.3, 3.2.2.7, 3.2.2.8) belongs to the family of ribonucleoside hydrolases Rih and catalyzes the…”
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A Puzzling Protein from Variovorax paradoxus Has a PLP Fold Type IV Transaminase Structure and Binds PLP without Catalytic Lysine by Boyko, Konstantin M., Matyuta, Ilya O., Nikolaeva, Alena Y., Rakitina, Tatiana V., Popov, Vladimir O., Bezsudnova, Ekaterina Yu, Khrenova, Maria G.

“…Effective biocatalysts for the synthesis of optically pure amines from keto precursors are highly required in organic synthesis. Transaminases are a large…”
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Incorporation of pyridoxal-5′-phosphate into the apoenzyme: A structural study of D-amino acid transaminase from Haliscomenobacter hydrossis by Bakunova, Alina K., Matyuta, Ilya O., Minyaev, Mikhail E., Boyko, Konstantin M., Popov, Vladimir O., Bezsudnova, Ekaterina Yu

“…Pyridoxal-5′-phosphate (PLP)-dependent transaminases are key enzymes of amino acid metabolism in cells and remarkable biocatalysts of stereoselective amination…”
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Multifunctionality of arginine residues in the active sites of non-canonical d-amino acid transaminases by Bakunova, Alina K., Matyuta, Ilya O., Minyaev, Mikhail E., Isaikina, Tatiana Y., Boyko, Konstantin M., Popov, Vladimir O., Bezsudnova, Ekaterina Yu

“…Structure-function relationships are key to understanding enzyme mechanisms, controlling enzyme activities, and designing biocatalysts. Here, we investigate…”
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The crystal structure of yeast mitochondrial type pyrophosphatase provides a model to study pathological mutations in its human ortholog by Bezpalaya, Ekaterina Y., Matyuta, Ilya O., Vorobyeva, Natalia N., Kurilova, Svetlana A., Oreshkov, Sergey D., Minyaev, Mikhail E., Boyko, Konstantin M., Rodina, Elena V.

“…Mutations in human ppa2 gene encoding mitochondrial inorganic pyrophosphatase (PPA2) result in the mitochondria malfunction in heart and brain and lead to…”
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Mechanism of D-Cycloserine Inhibition of D-Amino Acid Transaminase from Haliscomenobacter hydrossis by Bakunova, Alina K., Matyuta, Ilya O., Nikolaeva, Alena Yu, Boyko, Konstantin M., Popov, Vladimir O., Yu. Bezsudnova, Ekaterina

“…D-cycloserine inhibits pyridoxal-5′-phosphate (PLP)-dependent enzymes. Inhibition effect depend on organization of the active site and mechanism of the…”
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Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase from IBlastococcus saxobsidens/I by Shilova, Sofia A, Matyuta, Ilya O, Petrova, Elizaveta S, Nikolaeva, Alena Y, Rakitina, Tatiana V, Minyaev, Mikhail E, Boyko, Konstantin M, Popov, Vladimir O, Bezsudnova, Ekaterina Yu

“…Enzymes with expanded substrate specificity are good starting points for the design of biocatalysts for target reactions. However, the structural basis of the…”
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Structure–Functional Examination of Novel Ribonucleoside Hydrolase C from ILimosilactobacillus reuteri/I LR1 by Shaposhnikov, Leonid A, Chikurova, Natalia Yu, Atroshenko, Denis L, Savin, Svyatoslav S, Kleymenov, Sergei Yu, Chernobrovkina, Alla V, Pometun, Evgenii V, Minyaev, Mikhail E, Matyuta, Ilya O, Hushpulian, Dmitry M, Boyko, Konstantin M, Tishkov, Vladimir I, Pometun, Anastasia A

“…Ribonucleoside hydrolase C (RihC, EC 3.2.2.1, 3.2.2.2, 3.2.2.3, 3.2.2.7, 3.2.2.8) belongs to the family of ribonucleoside hydrolases Rih and catalyzes the…”
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To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme from IAminobacterium colombiense/I by Shilova, Sofia A, Khrenova, Maria G, Matyuta, Ilya O, Nikolaeva, Alena Y, Rakitina, Tatiana V, Klyachko, Natalia L, Minyaev, Mikhail E, Boyko, Konstantin M, Popov, Vladimir O, Bezsudnova, Ekaterina Yu

“…Pyridoxal-5′-phosphate (PLP)-dependent transaminases are highly efficient biocatalysts for stereoselective amination. D-amino acid transaminases can catalyze…”
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IFriunavirus/I Phage-Encoded Depolymerases Specific to Different Capsular Types of IAcinetobacter baumannii/I by Timoshina, Olga Y, Kasimova, Anastasia A, Shneider, Mikhail M, Matyuta, Ilya O, Nikolaeva, Alena Y, Evseev, Peter V, Arbatsky, Nikolay P, Shashkov, Alexander S, Chizhov, Alexander O, Shelenkov, Andrey A, Mikhaylova, Yulia V, Slukin, Pavel V, Volozhantsev, Nikolay V, Boyko, Konstantin M, Knirel, Yuriy A, Miroshnikov, Konstantin A, Popova, Anastasia V

“…Acinetobacter baumannii is a critical priority nosocomial pathogen that produces a variety of capsular polysaccharides (CPSs), the primary receptors for…”
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