Eduard A Sergienko

Summary

Publications

  1. ncbi New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme
    Eduard A Sergienko
    Department of Chemistry and Program in Cellular and Molecular Biodynamics, Rutgers, The State University of New Jersey, Newark, New Jersey 07102, USA
    Biochemistry 41:3952-67. 2002
  2. ncbi Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity
    Eduard A Sergienko
    Department of Chemistry and Program in Cellular and Molecular Biodynamics, Rutgers, The State University of New Jersey, Newark, New Jersey 07102, USA
    Biochemistry 41:6164-9. 2002
  3. ncbi Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase
    Elena S Polovnikova
    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA
    Biochemistry 42:1820-30. 2003

Collaborators

  • F Jordan
  • Elena S Polovnikova
  • Asim K Bera
  • George L Kenyon
  • Natalie L Anderson
  • Miriam S Hasson
  • John T Burgner
  • Michael J McLeish

Detail Information

Publications3

  1. ncbi New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: demonstration of the existence of two active forms of the enzyme
    Eduard A Sergienko
    Department of Chemistry and Program in Cellular and Molecular Biodynamics, Rutgers, The State University of New Jersey, Newark, New Jersey 07102, USA
    Biochemistry 41:3952-67. 2002
    ..Addition of pyruvamide or acetaldehyde to YPDC results in the appearance of additional conformations of the enzyme...
  2. ncbi Yeast pyruvate decarboxylase tetramers can dissociate into dimers along two interfaces. Hybrids of low-activity D28A (or D28N) and E477Q variants, with substitution of adjacent active center acidic groups from different subunits, display restored activity
    Eduard A Sergienko
    Department of Chemistry and Program in Cellular and Molecular Biodynamics, Rutgers, The State University of New Jersey, Newark, New Jersey 07102, USA
    Biochemistry 41:6164-9. 2002
    ..The significance of the results is discussed in light of a recently proposed alternating sites mechanism for YPDC. A preparative ion-exchange method is reported for the separation and purification of hybrid enzymes...
  3. ncbi Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase
    Elena S Polovnikova
    Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA
    Biochemistry 42:1820-30. 2003
    ..H281 is involved in protonation of the enamine. Surprisingly, S26 appears to be involved not only in substrate binding but also in other steps of the reaction...