• Title of article

    Tartrate Dehydrogenase, a New Member of the Family of Metal-Dependent Decarboxylating R-Hydroxyacid Dehydrogenases

  • Author/Authors

    Tipton، نويسنده , , P.A. and Beecher، نويسنده , , B.S.، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 1994
  • Pages
    7
  • From page
    15
  • To page
    21
  • Abstract
    The gene encoding tartrate dehydrogenase has been cloned from Pseudomonas putida and sequenced. The gene is 1098 nucleotides long and encodes a protein 365 amino acids in length with a calculated Mr of 40,636. The gene and the protein encoded by it show strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase. Thus, tartrate dehydrogenase is the third member to be identified of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases which have an evolutionarily distinct NAD+-binding domain. The poor catalytic properties of tartrate dehydrogenase suggest that it has not been under strong selective pressure to maximize its ability to turn over (+)-tartrate for very long; the homology with isopropylmalate dehydrogenase makes it an attractive candidate for a recent progenitor of tartrate dehydrogenase. β-Isopropylmalate is a substrate for tartrate dehydrogenase with a Km of 14 ± 2 μM; it is turned over with a Vmax that is 35% of Vmax in the (+)-tartrate reaction. The gene encoding tartrate dehydrogenase has been expressed in Escherichia coli and large quantities of soluble enzyme can be obtained.
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    1994
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1452260