• Title of article

    8-(4-Bromo-2,3-dioxobutylthio)NAD: A New Affinity Label for NAD-Specific Isocitrate Dehydrogenase

  • Author/Authors

    Kumar، نويسنده , , A. and Colman، نويسنده , , R.F.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 1994
  • Pages
    10
  • From page
    357
  • To page
    366
  • Abstract
    8-(4-Bromo-2,3-dioxobutylthio)nicotinamide adenine dinucleotide (8-BDB-TNAD), a new reactive NAD analog, was synthesized by coupling 8-thio-AMP with NMN, followed by condensation with 1,4-dibromobutanedione. Incubation of 160 μM 8-BDB-TNAD with the allosteric pig heart NAD-dependent isocitrate dehydrogenase causes time-dependent inactivation to a limit of 25% residual activity concomitant with incorporation of ∼ 1 mol reagent/mol average subunit. In addition to binding sites for NAD and NADH, this enzyme has been shown to have regulatory sites for NADPH and for ADP (R. S. Ehrlich and R. F. Colman 1982, J. Biol. Chem. 257, 4769-4774). Marked protection against enzyme inactivation by 8-BDB-TNAD and incorporation is provided by the regulatory nucleotides NADPH or ADP, while NAD and NADH are less effective. The rate constant for inactivation shows a nonlinear dependence on 8-BDB-TNAD concentration which can be ascribed to reversible formation of an enzyme-reagent complex (KI = 83 μM) prior to an irreversible reaction (kmax = 0.0625 min−1). Analysis of the kinetic properties and binding characteristics of modified enzyme indicates that this enzyme retains the ability to bind ADP, but does not bind NADPH. Thus, 8-BDB-TNAD reacts at or near the allosteric NADPH site of pig heart NAD-dependent isocitrate dehydrogenase.
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    1994
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1451512