Oxidation of L-glucose by a Pseudomonad

Biochim Biophys Acta. 1979 Nov 9;571(1):120-6. doi: 10.1016/0005-2744(79)90232-8.

Abstract

A new enzyme, D-threo-aldolse dehydrogenase (2S,3R-aldose dehydrogenase), found in Pseudomonas caryophylli, was capable of oxidizing L-glucose L-xylose, D-arabinose, and L-fucose in the presence of NAD+. The enzyme was synthesized constitutively and purified about 120-fold from D-glucose-grown cells. The Km values for L-glucose, L-xylose, D-arabinose, and L-fucose were 1.5 . 10(-2), 4.5 . 10(-3), 2.8 . 10(-3), and 2.1 . 10(-3), respectively. D-glucose and other aldoses inhibited the enzyme reaction; this inhibition was competitive with L-glucose as substrate and D-glucose as inhibitor. The optimum pH for the enzyme reaction was 10; the molecular weight of the enzyme was determined by gel filtration to be 7 . 10(4).

MeSH terms

  • Aldehyde Reductase / biosynthesis*
  • Arabinose / metabolism
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Fucose / metabolism
  • Glucose / metabolism*
  • Glucose Dehydrogenases / antagonists & inhibitors
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Pseudomonas / enzymology*
  • Substrate Specificity
  • Sugar Alcohol Dehydrogenases / biosynthesis*
  • Xylose / metabolism

Substances

  • Fucose
  • Xylose
  • Arabinose
  • Sugar Alcohol Dehydrogenases
  • Glucose Dehydrogenases
  • Aldehyde Reductase
  • Glucose