Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Irina V. Shapovalova"'
Autor:
Sergey V. Pushkarev, Valeriia A. Vinnik, Irina V. Shapovalova, Vytas K. Švedas, Dmitry K. Nilov
Publikováno v:
Biochemistry. Biokhimiia. 87(5)
Abstract tRNA-guanine transglycosylase, an enzyme catalyzing replacement of guanine with queuine in human tRNA and participating in the translation mechanism, is involved in the development of cancer. However, information on the small-molecule inhibi
Autor:
Nikolay V. Panin, Irina V. Shapovalova, Tatyana A. Shcherbakova, Vytas K. Švedas, Dmitry A. Suplatov
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 112:66-68
The computationally designed βD484N mutant of penicillin acylase from Escherichia coli was shown to be more stable at alkaline conditions, resistant to inactivation by high substrate concentrations and able to catalyze preparative peptide synthesis
Autor:
Irina V. Shapovalova, Dick B. Janssen, D.B. Švedas, E. de Vries, Wynand Alkema, O.V. Jamskova, D.T. Guranda
Publikováno v:
Acta naturae, 1(3), 94-98
Acta Naturae
Acta Naturae
Residue phenylalanine 71 of the beta-chain of penicillin acylase from E. coil is involved in substrate binding and chiral discrimination of its enantiomers. Different amino acid residues have been introduced at position beta F71, and the mutants were
Autor:
Oleg V. Stroganov, Ilyas G. Khaliullin, Ghermes G. Chilov, Irina V. Shapovalova, Vytas K. Švedas, Nikolay V. Panin, Fedor N. Novikov
Publikováno v:
The FEBS journal. 280(1)
Molecular modeling was addressed to understand different substrate-binding modes and clarify the role of two positively charged residues of the penicillin G acylase active site - βR263 and αR145 - in binding of negatively charged substrates. Althou
Publikováno v:
Acta Naturae
ResearcherID
ResearcherID
A full-atomic molecular model of human apurinic/apyrimidinic endonuclease APE1, an important enzyme in the DNA repair system, has been constructed. The research consisted of hybrid quantum mechanics/ molecular mechanics modeling of the enzyme-substra