Vytas K. Švedas

Lomonosov Moscow State University

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Dmitry Suplatov

Lomonosov Moscow State University

Dmitry K. Nilov

Lomonosov Moscow State University

ДТ

Д. Т. Гуранда

Moscow State University

Luuk M. van Langen

Delft University of Technology

Yana Sharapova

University Medical Centre Mannheim

Maxim I. Youshko

Lomonosov Moscow State University

Fred van Rantwijk

Delft University of Technology

Roger A. Sheldon

Delft University of Technology

Evgeny Kirilin

Lomonosov Moscow State University

Tatyana A. Shcherbakova

Lomonosov Moscow State University

Cooperative Institutions

Lomonosov Moscow State University

195

Russian Academy of Sciences

104

Moscow State University

Siberian Branch of the Russian Academy of Sciences

A N Bach Institute of Biochemistry

Institute of Bioorganic Chemistry

Ministry of Health of the Russian Federation

Novosibirsk State University

Federal Center Research Fundamentals of Biotechnology

Russian Cancer Research Center NN Blokhin

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Professor Dr Roger A. Sheldon—65 years on

Green Chemistry (2008)

И. И. Моисеев Shun‐Ichi Murahashi Martyn Poliakoff Kenneth R. Seddon Vytas K. Švedas

Ilya I. Moiseev, Shun-Ichi Murahashi, Martyn Poliakoff, Ken Seddon and Vytas K. Švedas reflect on a recent symposium held in honour of Roger Sheldon, a founding father of green chemistry and of this journal.

Ilya

Honour

Vedas

10.1039/b719347p

Cite

Citations (0)

Penicillin acylase‐catalyzed ampicillin synthesis using a pH gradient: A new approach to optimization

Biotechnology and Bioengineering (2002)

Maxim I. Youshko Luuk M. van Langen Erik de Vroom Fred van Rantwijk Roger A. Sheldon

10.1002/bit.10234.abs

Cite

Citations (1)

A New Approach for Studying Poly(ADP-Ribose) Polymerase Inhibitors Using Permeabilized Adherent Cells

Biochemistry (Moscow) (2024)

С. И. Шрам Tatyana A. Shcherbakova Tatyana V. Abramova Maria S. Smirnovskaya Anastasia I Balandina

Ribose

10.1134/s0006297924090086

Cite

Citations (0)

Quantitative characteristic of the catalytic properties and microstructure of cross-linked enzyme aggregates of penicillin acylase

Journal of Molecular Catalysis B Enzymatic (2008)

N.A. Pchelintsev Maxim I. Youshko Vytas K. Švedas

Penicillin amidase

10.1016/j.molcatb.2008.05.006

Cite

Citations (52)

Penicillin Acylase: A Retrospective Study of the Kinetics and Thermodynamics of Practically Significant Reactions

Moscow University Chemistry Bulletin (2023)

N. V. Panin Д. Т. Гуранда И. В. Шаповалова Vytas K. Švedas

Penicillin amidase

Enzyme Kinetics

Enzyme Catalysis

10.3103/s0027131423040041

Cite

Citations (0)

Preparative Biocatalytic Synthesis of α-Ketoglutaramate

International Journal of Molecular Sciences (2021)

Maksim Nikulin Viktor Drobot Vytas K. Švedas Boris F. Krasnikov

α-Ketoglutaramate (KGM) is an underexamined metabolite of L-glutamine in the metabolic pathway of glutaminase II of α-ketoglutarate formation. Presumably, KGM may be a biomarker of hepatic encephalopathy and other hyperammonemic diseases. This metabolite is a substrate for the ω-amidase enzyme and is used to determine its activity in the study of the biochemistry of various types of cancer. However, the commercial unavailability of KGM hinders its widespread use. Methods for the preparative synthesis of KGM are known, but they either do not provide the proper yield or proper purity of the target product. In this work, a detailed description of the procedures is given that allows the production of KGM with a purity above 97% and a yield of the target product above 75% using L-amino acid oxidase from C. adamanteus as a catalyst of L-glutamine conversion. KGM can be obtained both in the form of a highly concentrated aqueous solution and in the form of crystals of sodium salt. The developed methods can be used both for scaling up the synthesis of KGM and for creating economical biocatalytic technologies for the production of other highly purified preparations.

10.3390/ijms222312748

Cite

Citations (7)

Resolution of (RS)-phenylglycinonitrile by penicillin acylase-catalyzed acylation in aqueous medium

Tetrahedron Asymmetry (2003)

Ghermes G. Chilov Harold M. Moody Wilhelmus H. J. Boesten Vytas K. Švedas

Penicillin amidase

Kinetic resolution

Phenylacetic acid

Amidase

Aqueous medium

Enzyme Catalysis

10.1016/s0957-4166(03)00523-8

Cite

Citations (23)

Molecular modeling of formate dehydrogenase: the formation of the Michaelis complex

Journal of Biomolecular Structure and Dynamics (2012)

Dmitry K. Nilov I.G. Shabalin Vladimir O. Popov Vytas K. Švedas

Abstract The formation of the reactive enzyme–substrate complex of formate dehydrogenase has been investigated by molecular dynamics techniques accounting for different conformational states of the enzyme. Simulations revealed that the transport of substrate to the active site through the substrate channel proceeds in the open conformation of enzyme due to the crucial role of the Arg284 residue acting as a vehicle. However, formate binding in the active site of the open conformation leads to the formation of a nonproductive enzyme–substrate complex. The productive Michaelis complex is formed only in the closed enzyme conformation after the substrate and coenzyme have bound, when required rigidity of the binding site and reactive formate orientation due to interactions with Arg284, Asn146, Ile122, and His332 residues is attained. Then, the high occupancy (up to 75%) of the reactive substrate–coenzyme conformation is reached, which was demonstrated by hybrid quantum mechanics/molecular mechanics simulations using various semiempirical Hamiltonians. Keywords: formate dehydrogenaseMichaelis complexmolecular modelingmolecular dynamicsmolecular mechanicsquantum mechanicsopen conformationclosed conformationreactive conformationsubstrate channel Acknowledgments We are grateful to Sergey Zhumatiy and Vladimir Voevodin for their assistance in parallel computations and to David R. Cooper, Tatiana Safonova, and Matt Demas for their help in correcting English text. This work was supported by the Russian Foundation for Basic Research (Joint project RFBR-DFG RECESS, Grant 09-04-92,744).

Formate dehydrogenase

Molecular mechanics

10.1080/07391102.2012.677768

Cite

Citations (18)

Penicillin Acylase-Catalyzed Solid-State Ampicillin Synthesis

Advanced Synthesis & Catalysis (2002)

Maxim I. Youshko Vytas K. Švedas

The ability of immobilized penicillin acylase from E. coli to retain a remarkable catalytic activity in solid-state systems has been demonstrated. Stabilization of immobilized penicillin acylase by inorganic salt hydrates allowed us to exploit nearly the whole catalytic activity of the enzyme at a very low water content. Using this technique, enzymatic synthesis of ampicillin in solid-state systems was performed with high yields (up to 70% starting from equimolar mixture of reagents) and rates comparable to the corresponding values in homogeneous solutions and heterogeneous systems, “aqueous solution-precipitate”. Peculiarities of the enzymatic solid-state acyl transfer process, such as absence of the clear-cut maximum on the ampicillin accumulation curves and dependence of the synthetic efficiency on the enzyme loading, have been observed. The space-time yield of solid-state enzymatic ampicillin synthesis was shown to be up to ten times higher compared to the homogeneous solutions and heterogeneous “aqueous solution-precipitate” systems.

Penicillin amidase

Enzyme Catalysis

10.1002/1615-4169(200209)344:8<894::aid-adsc894>3.0.co;2-q

Cite

Citations (19)

Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis

Journal of Molecular Catalysis B Enzymatic (2004)

Tatyana A. Shcherbakova Alexei Korennykh Luuk M. van Langen Roger A. Sheldon Vytas K. Švedas

Course (navigation)

10.1016/j.molcatb.2004.07.006

Cite

Citations (3)