A5010590439- ATP Synthase and ATPases Research
- Biochemical and Molecular Research
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Drug Transport and Resistance Mechanisms
- Russia and Soviet political economy
- Mitochondrial Function and Pathology
- Photosynthetic Processes and Mechanisms
- Ion Transport and Channel Regulation
- Lipid Membrane Structure and Behavior
- Particle physics theoretical and experimental studies
- Quantum Chromodynamics and Particle Interactions
- High-Energy Particle Collisions Research
- Enzyme function and inhibition
- Metalloenzymes and iron-sulfur proteins
- Molecular Sensors and Ion Detection
- Bacterial Genetics and Biotechnology
- Polyamine Metabolism and Applications
- Electrochemical Analysis and Applications
- Alkaline Phosphatase Research Studies
- Microbial Community Ecology and Physiology
- Electrochemical sensors and biosensors
- Neonatal Health and Biochemistry
- Plant nutrient uptake and metabolism
- Membrane-based Ion Separation Techniques
Lomonosov Moscow State University
2015-2024
Moscow State University
1989-2024
Novosibirsk State University
2020-2022
Budker Institute of Nuclear Physics
2020-2022
Siberian Branch of the Russian Academy of Sciences
2020-2022
Novosibirsk State Technical University
2021
University of Turku
1998-2013
Constructor University
2009
Tecnologie Avanzate (Italy)
2008
Ruhr University Bochum
2008
The DHH superfamily human protein h-prune, a binding partner of the metastasis suppressor nm23-H1, is frequently overexpressed in metastatic cancers. From an evolutionary perspective, h-prune very close to eukaryotic exopolyphosphatases. Here, we show for first time that efficiently hydrolyzes short-chain polyphosphates (kcat 3−40 s−1), including inorganic tripoly- and tetrapolyphosphates nucleoside 5′-tetraphosphates. Long-chain (≥25 phosphate residues) are converted more slowly, whereas...
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr-229 Escherichia coli cells requires the presence co-expressed apbE gene. The genes cluster with for Na+-NQR other FMN-binding flavoproteins bacterial genomes encode proteins previously unknown function. Experiments isolated...
Soluble inorganic pyrophosphatase (PPase), an essential enzyme central to phosphorus metabolism, catalyzes the hydrolysis of phosphoanhydride bond in pyrophosphate. Catalysis requires divalent metal ions which affect apparent pKas general acid and base on enzyme, pKa substrate. Three five are required for maximal activity, depending pH source. A detailed understanding catalysis would aid both nature biological mechanisms phosphoryl transfer, role cations. Without a high-resolution complex...
One of the strategies used by organisms to adapt life under conditions short energy supply is use by-product pyrophosphate support cation gradients in membranes. Transport reactions are catalyzed membrane-integral pyrophosphatases (PPases), which classified into two homologous subfamilies: H + -transporting (found prokaryotes, protists, and plants) Na prokaryotes). activities have been believed require specific machinery for each ion, accordance with prevailing paradigm membrane transport....
A bstract The cross section of the process e + − → π has been measured in Spherical Neutral Detector (SND) experiment at VEPP-2000 collider energy region 525 < $$ \sqrt{s} <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"> <mml:msqrt> <mml:mi>s</mml:mi> </mml:msqrt> </mml:math> 883 MeV. measurement is based on data with an integrated luminosity about 4.6 pb 1 . systematic uncertainty determination 0.8% > 0 600 GeV. ρ meson parameters are obtained as m = 775 3 ± 5 6 MeV, Γ 145 8...
The wealth of kinetic and structural information makes inorganic pyrophosphatases (PPases) a good model system to study the details enzymatic phosphoryl transfer. enzyme accelerates metal-complexed transfer 10 -fold: but how? Our structures yeast PPase product complex at 1.15 Å fluoride-inhibited 1.9 visualize active site in three different states: substrate-bound, immediate bound, relaxed bound. These span steps around chemical catalysis provide strong evidence that water molecule (O nu )...
An open reading frame located in the COTF-TETB intergenic region of Bacillus subtilis was cloned and expressed Escherichia coli shown to encode inorganic pyrophosphatase (PPase). The isolated enzyme is Mn2+-activated, like authentic PPase from B. subtilis. Although 13 functionally important active site residues are conserved all 31 soluble sequences so far identified, only two them PPase. This suggests that represents a new family PPases (a Bs family), putative members which were found...
The results of analyses the steady‐state kinetics vacuolar H + ‐translocating pyrophosphatase (V‐PPase) native tonoplast vesicles isolated from etiolated hypocotyls Vigna radiata (mung bean) and purified enzyme same source under a wide range Mg 2+ , pyrophosphate (PP i ) K concentrations are consistent with minimal reaction scheme in which dimagnesium is active substrate species catalysis mediated by preformed enzyme‐Mg complex. When account taken sensitivity V‐PPase to ionic strength,...
7,8-Dihydro-8-oxoguanine (8-oxoG) is a ubiquitous oxidative DNA lesion resulting from injury to via reactive oxygen species. 8-oxoG lesions may play role in the formation of aberrant methylation patterns during carcinogenesis. In this study, we assessed effects on and complex nine 30-mer oligodeoxynucleotide duplexes by catalytic domain murine Dnmt3a methyltransferase (Dnmt3a-CD). The rate hemimethylated varied 25-fold decrease 1.8-fold increase, depending position relative Dnmt3a-CD...
Membrane pyrophosphatases (PPases), divided into K+-dependent and K+-independent subfamilies, were believed to pump H+ across cell membranes until a recent demonstration that some PPases function as Na+ pumps. Here, we have expressed seven evolutionarily important putative in Escherichia coli estimated their hydrolytic, transport, transport activities well K+ requirements inner membrane vesicles. Four of these enzymes (from Anaerostipes caccae, Chlorobium limicola, Clostridium tetani,...
The suitability of different pyrophosphate (PPi) analogs as inhibitors the vacuolar H+-translocating inorganic pyrophosphatase (V-PPase; EC 3.6.1.1) tonoplast vesicles isolated from etiolated hypocotyls Vigna radiata was investigated. Five 1,1-diphosphonates and imidodiphosphate were tested for their effects on substrate hydrolysis by V-PPase at a concentration corresponding to Km enzyme. order inhibitory potency (apparent inhibition constants, Kiapp values, [mu]M, in parentheses) compounds...
Based on the primary structure, soluble inorganic pyrophosphatases can be divided into two families which exhibit no sequence similarity to each other. Family I, comprising most of known pyrophosphatase sequences, further prokaryotic, plant and animal/fungal pyrophosphatases. Interestingly, bear a closer prokaryotic than Only 17 residues are conserved in all 37 family I remarkably, 15 these located at active site. Subunit interface but not
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure and function analysis of Escherichia coli inorganic pyrophosphatase: is a hydroxide ion the key to catalysis?Tiina Salminen, Jarmo Kaepylae, Pirkko Heikinheimo, Jussi Kankare, Adrian Goldman, Jukka Heinonen, Alexander A. Baykov, Barry S. Cooperman, Reijo LahtiCite this: Biochemistry 1995, 34, 3, 782–791Publication Date (Print):January 1, 1995Publication History Published online1 May 2002Published inissue 1 January...
Pyrophosphatase (PPase) from Bacillus subtilis has recently been found to be the first example of a family II soluble PPase with unique requirement for Mn2+. In present work, we cloned and overexpressed in Escherichia coli putative genes two more PPases (fromStreptococcus mutans Streptococcus gordonii), isolated recombinant proteins, showed them highly specific active (catalytic constants 1700–3300 s−1 at 25 °C comparison 200–400 I). All three were dimeric manganese metalloenzymes,...
Membrane-bound pyrophosphatase (PPase) is commonly believed to couple pyrophosphate (PPi) hydrolysis H+ transport across the membrane. Here, we demonstrate that two newly isolated bacterial membrane PPases from mesophile Methanosarcina mazei (Mm-PPase) and moderate thermophile Moorella thermoacetica a previously described PPase hyperthermophilic bacterium Thermotoga maritima catalyze Na+ rather than into Escherichia coli inner vesicles (IMV). When assayed in uncoupled IMV, three exhibit an...
Combined evidence obtained from the measurements of pyrophosphate hydrolysis and synthesis, oxygen exchange between phosphate water, enzyme-bound formation Mg2+ binding enabled us to deduce overall scheme catalysis by Escherichia coli inorganic pyrophosphatase in presence Mg2+. We determined equilibrium constants for various enzyme species forward reverse rate four steps catalytic reaction, namely, binding/release PPi, hydrolysis/synthesis PPi successive two Pi molecules. Catalysis E. both...
We report the expression and initial characterization of 19 active‐site variants Saccharomyces cerevisiae inorganic pyrophosphatase (PPase), including measurements thermostability, oligomeric structure specific activity at pH 7.2. 13 conservative substitutions resulted in least a fivefold decrease activity, indicating that these residues are important for yeast PPase catalysis. The E58D, D117E, D120E D152E had no under conditions tested, suggesting Glu58, Asp117, Asp120 Asp152 may have...