Oxidation of L-glucose by a Pseudomonad.
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).
D000449:Aldehyde Reductase / Q000096:biosynthesis*; D001089:Arabinose / Q000378:metabolism; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005643:Fucose / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D005948:Glucose Dehydrogenases / Q000037:antagonists & inhibitors; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D013401:Sugar Alcohol Dehydrogenases / Q000096:biosynthesis*; D014994:Xylose / Q000378:metabolism
D005643:Fucose; D014994:Xylose; D001089:Arabinose; D013401:Sugar Alcohol Dehydrogenases; D005948:Glucose Dehydrogenases; D000449:Aldehyde Reductase; D005947:Glucose