Title | Oxidation of L-glucose by a Pseudomonad. |
Publication Type | Journal Article |
Year of Publication | 1979 |
Authors | Sasajima, KI, Sinskey, AJ |
Journal | Biochim Biophys Acta |
Volume | 571 |
Issue | 1 |
Pagination | 120-6 |
Date Published | 1979 Nov 09 |
ISSN | 0006-3002 |
Keywords | Aldehyde Reductase, Arabinose, Chromatography, Gel, Chromatography, Ion Exchange, Fucose, Glucose, Glucose Dehydrogenases, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Pseudomonas, Substrate Specificity, Sugar Alcohol Dehydrogenases, Xylose |
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). |
DOI | 10.1016/0005-2744(79)90232-8 |
Alternate Journal | Biochim Biophys Acta |
Citation Key | 267 |
PubMed ID | 40609 |