Vladimir K. Antonov


PeriodCountry, cityEducation institutionAdditional info
1944–1949 Russia, Moscow D.I. Mendeleev's Moscow Institute of Chemical Technology MS in chemichal technology
1955 Russia, Moscow D.I. Mendeleev's Moscow Institute of Chemical Technology Ph.D. in chemistry
1960 Russia, Moscow Institute of chemistry of the Natural Products AS USSR (ICNP) Senior research fellow awarded
1967 Russia, Moscow Institute of chemistry of the Natural Products AS USSR (ICNP) D.Sc. in chemistry

Selected publications

  1. Антонов В.К., Воротынцева Т.И., Замолодчикова Т.С. (1992). Дуоденаза – новая сериновая протеиназа с необычной специфичностью. Доклады РАН 324 (6), 1318–1322 ID:117
  2. Amerik AYu , Antonov V.K., Gorbalenya A.E., Kotova S.A., Rotanova T.V., Shimbarevich E.V. (1991). Site-directed mutagenesis of La protease. A catalytically active serine residue. FEBS Lett. 287 (1-2), 211–4 [+]

    Comparative sequence analysis of Escherichia coli ATP-dependent La protease led to the suggestion that Ser679 is the catalytically active enzyme residue. Site-directed mutagenesis Ser679----Ala, investigation of the cells containing the mutant plasmid, and study of the partially purified mutant protein produced results in favour of this suggestion.

  3. Антонов В.К., Гинодман Л.М., Румш Л.Д. (1984). Механизмы протеолиза. Биоорг. хим. 10 (8), 1044–1058 ID:118
  4. Antonov V.K., Ginodman L.M., Rumsh L.D., Kapitannikov Y.V., Barshevskaya T.N., Yavashev L.P., Gurova A.G., Volkova L.I. (1981). Studies on the mechanisms of action of proteolytic enzymes using heavy oxygen exchange. Eur. J. Biochem. 117 (1), 195–200 [+]

    Transpeptidation reactions catalyzed by chymotrypsin, pepsin, leucine aminopeptidase and thermolysin have been studied in heavy oxygen water (H2 18O). The 18O incorporation into the peptide bond of transpeptidation products and into the non-hydrolyzed substrate has been measured. The rates of 18O exchange in the carboxylic groups of N-acetylphenylalanine and leucine, catalyzed by pepsin and leucine aminopeptidase, respectively, have also been determined. These rates have been compared with that of the exchange in the presence of amino compounds which reversibly form amide bonds with the above carboxyl-containing substances. The data obtained show that, in contrast to chymotrypsin, other enzymes studied do not form 'acyl-enzymes' but function by the mechanism of general-base catalysis. In other words, their catalytically active groups promote the abstraction of a proton from the water molecule, which attacks the susceptible bond of the substrate. The structure of intermediate compounds in this type of catalysis and the mechanism of the transpeptidation reaction are discussed.

  5. Антонов В.К., Зинченко А.А., Румш Л.Д. (1976). Статистический анализ специфичности пепсина в отношении гидролиза белков. Биоорг. хим. 2 (6), 803–810 ID:253
  6. Antonov V.K., Ivanina T.V., Berezin I.V., Martinek K. (1970). n-Alkylboronic acids as bifunctional reversible inhibitors of alpha-chymotrypsin. FEBS Lett. 7 (1), 23–25 ID:252
  7. Ovchinnikov Yu.A., Shemyakin M.M., Ivanov V.T., Antonov V.K., Vinogradova E.I., Shkrob A.M., Malenkov G.G., Evstratov A.V., Laine I.A., Melnik E.I., Ryabova I.D. (1969). Cyclodepsipeptides as chemical tool for studying ionic transport through membranes. J. Membr. Biol. 1, 402–403 [+]

    This paper reports a study of the chemistry of valinomycin, enniatins and related membrane-active depsipeptides that increase alkali metal ion permeability of model and biological membranes. The antimicrobial activity of these compounds and thir effect on membranes has been correlated with their cation-complexing ability. the complexing reaction has been studied by spectropolarimetric studies have revealed coexistence of conformers of the cyclopeptides and conductometric methods.  Nuclear magnetic resonance, optical rotatory dispersion, and infrared spectrophotometric studies have revealed the coexistence ofconformers of the cyclodepsipeptides in solution and have led to elucidation of the spatial structure of valinomycin, enniatin B and their K+ complexes. The effect of the conformational properties of the cyclodepsipeptides on their complexation efficiency and selectivity, surface-active properties and behavior towards phospholipid monolayers, bimolecular phospholipid membranes and a number of biological membrane systems has been ascertained. The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies. It is suggested that the principle of conformation-dependent cation binding through ion-dipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.

  8. Антонов В.К., Иванина (Ротанова) Т.В., Березин И.В., Мартинек К. (1968). Бифункциональные обратимые ингибиторы протеолитических ферментов. Взаимодействие с α-химотрипсина с гексилборной кислотой. Доклады АН СССР 183 (6), 1435–1438 ID:116