Purification of two forms of the associated 3-dehydroquinate hydro-lyase and shikimate:NADP+ oxidoreductase in Phaseolus mungo seedlings

Biochim Biophys Acta. 1978 Jan 12;522(1):10-8. doi: 10.1016/0005-2744(78)90317-0.

Abstract

Two associated enzymes, 3-dehydroquinate hydro-lyase (EC 4.2.1.10) and shikimate:NADP+ oxidoreductase (EC 1.1.1.25), have been purified from Phaseolus mungo seedlings. These enzymes were purified 6900- and 9700-fold, respectively, but they were not separable. Moreover, two activity bands of the shikimate:NADP+ oxidoreductase were detected after polyacrylamide gel electrophoresis and the two peaks also have 3-dehydroquinate hydro-lyase activity. The two forms of the associated enzymes showed only small differences in molecular weight, Km value, pH optimum and the responses to some inhibitors.

MeSH terms

  • Alcohol Oxidoreductases / isolation & purification*
  • Alcohol Oxidoreductases / metabolism
  • Hydro-Lyases / isolation & purification*
  • Hydro-Lyases / metabolism
  • Isoenzymes / isolation & purification
  • Kinetics
  • Molecular Weight
  • Plants / enzymology*
  • Quinic Acid / analogs & derivatives
  • Shikimic Acid

Substances

  • Isoenzymes
  • Quinic Acid
  • Shikimic Acid
  • Alcohol Oxidoreductases
  • Hydro-Lyases