A5066561438- Toxin Mechanisms and Immunotoxins
- Enzyme Structure and Function
- Peptidase Inhibition and Analysis
- Glycosylation and Glycoproteins Research
- RNA and protein synthesis mechanisms
- Biochemical and Molecular Research
- Protein Structure and Dynamics
- Transgenic Plants and Applications
- Carbohydrate Chemistry and Synthesis
- Synthesis and Biological Evaluation
- Organometallic Complex Synthesis and Catalysis
- Crystal structures of chemical compounds
- Galectins and Cancer Biology
- Computational Drug Discovery Methods
- Bioactive Compounds and Antitumor Agents
- Biochemical and Structural Characterization
- Analytical Chemistry and Chromatography
- Mass Spectrometry Techniques and Applications
- Organometallic Compounds Synthesis and Characterization
- Microfinance and Financial Inclusion
- Plant Virus Research Studies
- Viral Infections and Immunology Research
- Porphyrin Metabolism and Disorders
- Pharmacogenetics and Drug Metabolism
- Cassava research and cyanide
National Academy of Sciences of Belarus
2019-2024
Institute of Bioorganic Chemistry
2019-2024
Kuban State Agrarian University
2019
Oligopeptidase B (OpB) is a two-domain, trypsin-like serine peptidase belonging to the S9 prolyloligopeptidase (POP) family. Two domains are linked by hinge region that participates in transition of enzyme between two major states—closed and open—in which residues catalytic triad located close each other separated, respectively. In this study, we described, for first time, structure OpB from bacteria obtained an Serratia proteomaculans with modified (PSPmod). PSPmod was crystallized...
The crystal structure of bacterial oligopeptidase B from Serratia proteamaculans (SpOpB) in complex with a chloromethyl ketone inhibitor was determined at 2.2 Å resolution. SpOpB crystallized closed (catalytically active) conformation. A single molecule bound simultaneously to the catalytic residues S532 and H652 mimicked tetrahedral intermediate reaction. comparative analysis obtained OpB Trypanosoma brucei (TbOpB) conformation showed that both enzymes, stabilization D-loop (carrying D)...
The search of a putative physiological electron acceptor for thiocyanate dehydrogenase (TcDH) newly discovered in the thiocyanate-oxidizing bacteria Thioalkalivibrio paradoxus revealed an unusually large, single-heme cytochrome c (CytC552), which was co-purified with TcDH from periplasm. Recombinant CytC552, produced Escherichia coli as mature protein without signal peptide, has spectral properties similar to endogenous and serves vitro TcDH-catalyzed reaction. CytC552 structure determined...
It happens with ever-increasing frequency that the modern world financial system, based on theories and practices by Western economists, malfunctions results in global crises.In this regard, USA European economists themselves doubt system's universality applicability to all countries of world.Until recently, Islamic economic theory excited nothing more than just academic interest among a limited circle scientists world.Nevertheless, under conditions today, model, its structure mechanisms is...
Oligopeptidase B (OPB) is the least studied group from prolyl oligopeptidase family. OPBs are found in bacteria and parasitic protozoa represent pathogenesis factors of corresponding infections. consist two domains connected by a hinge region have characteristics conformational dynamics, which include types movements: bridging/separation α/β-hydrolase catalytic β-propeller-regulatory movement loop carrying histidine, regulates an assembly/disassembly triad. In this work, elucidation...
Structurally similar catalytic subunits A of ricin (RTA) and viscumin (MLA) exhibit cytotoxic activity through ribosome inactivation. Ricin is more than viscumin, although the molecular mechanisms behind this difference are still poorly understood. To shed light on problem, we used a combined biochemical/molecular modeling approach to assess possible relationships between toxins their structural/dynamic properties. Based bioassay measurements, it was suggested that differences in associated...
Cytochrome P450 3A4 (3A4) is highly expressed in the human liver cells and plays a decisive role metabolism of xenobiotics, including more than 50 % medical products. The activity this enzyme can be regulated at expression level genes, as well conformation structure protein itself, due to changes molecular environment, interaction with high-molecular effectors. understanding dynamics response environmental necessary predict its that considerable extent regulates body’s homeostasis. To...