Vladimir Leskovac

Summary

Affiliation: University of Novi Sad
Country: Serbia and Montenegro

Publications

  1. ncbi request reprint The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae
    Vladimir Leskovac
    Faculty of Technology, The University of Novi Sad, Bulevar Cara Lazara 1, 21000 Novi Sad, Yugoslavia
    FEMS Yeast Res 2:481-94. 2002
  2. ncbi request reprint Deriving the rate equations for product inhibition patterns in bisubstrate enzyme reactions
    Vladimir Leskovac
    Faculty of Technology, University of Novi Sad, Yugoslavia
    J Enzyme Inhib Med Chem 21:617-34. 2006
  3. ncbi request reprint A general method for the analysis of random bisubstrate enzyme mechanisms
    Vladimir Leskovac
    Faculty of Technology, Bulevar Cara Lazara 1, 21000, Novi Sad, Yugoslavia
    J Ind Microbiol Biotechnol 31:155-60. 2004
  4. ncbi request reprint Bioorganic mechanisms of the formation of free radicals catalyzed by glucose oxidase
    Svetlana Trivic
    Faculty of Science Novi Sad, Yugoslavia
    Bioorg Chem 30:95-106. 2002
  5. ncbi request reprint The chemical mechanism of action of glucose oxidase from Aspergillus niger
    Gerd Wohlfahrt
    Orion Corporation, Orion Pharma, Espoo, Finland
    Mol Cell Biochem 260:69-83. 2004
  6. ncbi request reprint Inactivation of cytochrome-c with glucose oxidase
    Vladimir Leskovac
    Faculty of Technology Novi Sad, Bulevar Cara Lazara 1, YU 21000 Novi Sad
    J Enzyme Inhib Med Chem 19:169-74. 2004

Collaborators

  • Svetlana Trivic
  • Gerd Wohlfahrt
  • Jasmina Zeremski
  • Draginja Pericin
  • Gary W Winston
  • Miroslav Vrvić

Detail Information

Publications6

  1. ncbi request reprint The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae
    Vladimir Leskovac
    Faculty of Technology, The University of Novi Sad, Bulevar Cara Lazara 1, 21000 Novi Sad, Yugoslavia
    FEMS Yeast Res 2:481-94. 2002
    ..Finally, the bio-organic chemistry of the hydride-transfer reactions catalyzed by the enzyme is covered: this chemistry explains the narrow substrate specificity and the enantioselectivity of the yeast enzyme...
  2. ncbi request reprint Deriving the rate equations for product inhibition patterns in bisubstrate enzyme reactions
    Vladimir Leskovac
    Faculty of Technology, University of Novi Sad, Yugoslavia
    J Enzyme Inhib Med Chem 21:617-34. 2006
    ..The practical application of above product inhibition analysis was illustrated with three examples of yeast alcohol dehydrogenase-catalyzed reactions...
  3. ncbi request reprint A general method for the analysis of random bisubstrate enzyme mechanisms
    Vladimir Leskovac
    Faculty of Technology, Bulevar Cara Lazara 1, 21000, Novi Sad, Yugoslavia
    J Ind Microbiol Biotechnol 31:155-60. 2004
    ..0, 25 degrees C. It was found that this fully reversible reaction proceeds by a steady-state random Bi-Bi mechanism, whereby both dead-end complexes are formed...
  4. ncbi request reprint Bioorganic mechanisms of the formation of free radicals catalyzed by glucose oxidase
    Svetlana Trivic
    Faculty of Science Novi Sad, Yugoslavia
    Bioorg Chem 30:95-106. 2002
    ..Under optimal conditions, free radicals are stable for several minutes in aqueous solutions under physiological conditions...
  5. ncbi request reprint The chemical mechanism of action of glucose oxidase from Aspergillus niger
    Gerd Wohlfahrt
    Orion Corporation, Orion Pharma, Espoo, Finland
    Mol Cell Biochem 260:69-83. 2004
    ..It was estimated that the pKa of Glu412 (bound to His559) in the free reduced enzyme is 3.4, and the pKa of His516 in the free reduced enzyme is 6.9...
  6. ncbi request reprint Inactivation of cytochrome-c with glucose oxidase
    Vladimir Leskovac
    Faculty of Technology Novi Sad, Bulevar Cara Lazara 1, YU 21000 Novi Sad
    J Enzyme Inhib Med Chem 19:169-74. 2004
    ..The initial rate of reaction is almost independent of the concentration of enzyme and glucose. The striking feature of this reaction is the fact that the reaction proceeds efficiently even below a concentration of 10 nM enzyme...