PMID: 40609Nov 9, 1979

Oxidation of L-glucose by a Pseudomonad

Biochimica Et Biophysica Acta
K I Sasajima, A J Sinskey

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).

References

Aug 1, 1965·Proceedings of the National Academy of Sciences of the United States of America·R P MortlockW A Wood
Nov 1, 1962·Journal of Neurochemistry·F F FOLDESE G ERDOS
Sep 24, 2004·Infection and Immunity·Clemens WalterMatthias Krüll
Apr 27, 2011·Chemistry : a European Journal·Zhijun NingHans Ågren

Citations

Oct 6, 2012·The Journal of Biological Chemistry·Tetsu ShimizuAkira Nakamura
Mar 3, 2018·Chirality·Raluca-Ioana Stefan-van Staden, Grigorina Mitrofan
Apr 5, 2020·Cancers·Koki OnoKatsuya Yamada

Related Concepts

Xylose Reductase
Arabinose
Molecular Sieve Chromatography
Ion-Exchange Chromatography Procedure
Fucose
Anhydrous Dextrose
Glucose Dehydrogenases
Hydrogen-Ion Concentration
Pseudomonas
Substrate Specificity

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