Oxidation of L-glucose by a Pseudomonad.

TitleOxidation of L-glucose by a Pseudomonad.
Publication TypeJournal Article
Year of Publication1979
AuthorsSasajima, KI, Sinskey, AJ
JournalBiochim Biophys Acta
Date Published1979 Nov 09
KeywordsAldehyde Reductase, Arabinose, Chromatography, Gel, Chromatography, Ion Exchange, Fucose, Glucose, Glucose Dehydrogenases, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Pseudomonas, Substrate Specificity, Sugar Alcohol Dehydrogenases, Xylose

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).

Alternate JournalBiochim Biophys Acta
Citation Key267
PubMed ID40609