N-Acetylation of Glucosamine-6-Phosphate in Leuconostoc mesenteroides
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منابع مشابه
N-Acetylation of glucosamine-6-phosphate in Leuconostoc mesenteroides.
A partially purified enzyme (120-fold) from Leuconostoc mesenteroides catalyzed the reversible N-acetylation of d-glucosamine-6-phosphate. Coenzyme A was not required and inhibited the reaction rate. Neither d-glucosamine nor N-acetyl-d-glucosamine served as a substrate for the reversible reaction. The enzyme preparation retained 50% of its original activity after 5 min at 100 C. The K(m) for a...
متن کاملGlucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Glucose 6-phosphate dehydrogenase from Zeuconostoc mesenteroides, previously isolated in crystalline form (Olive, C., and Levy, H. R., Biochemistry, 6, 730 (1967)), is shown to be essentially homogeneous by disc gel electrophoresis and sedimentation velocity analysis. The weight average molecular weight is 103,700, determined by both high speed and low speed sedimentation equilibrium techniques...
متن کاملA glucose-6-phosphate dehydrogenase in Leuconostoc mesenteroides.
Glucose fermentation by Leuconostoc me8enteroides has been shown to proceed via a mechanism which differs from the classical Embden-Meyerhof glycolytic scheme. DeMoss, Bard, and Gunsalus (1951) found no evidence in cell-free extracts of this organism for the key enzyme aldolae but showed that cellular suspensions ferment glucose to equimolar quantities of ethanol, C02, and lactate as obligatory...
متن کامل6-Phosphogluconate dehydrogenase from leuconostoc mesenteroides.
The pathways for degradation of 6-phosphogluconate have been rather clearly defined for several organisms, the most notable of which are yeast (Horecker, 1953), Escherichia coli (Cohen, 1951), Pseudomonas saccharophila (Entner and Doudoroff, 1952; MacGee and Doudoroff, 1954), and Pseudomonas fluorescens (Kovachevich and Wood, 1954). The enzymes from yeast and E. coli appear to be similar, if no...
متن کاملIron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Structural and functional changes.
As a variety of eukaryotic cells age, the specific activity of glucose-6-phosphate dehydrogenase (Glu-6-PDH) declines as much as 50%. Because of the central role of this enzyme in metabolism, it is important to define factors responsible for this loss in enzyme activity. We report that Glu-6-PDH from Leuconostoc mesenteroides is rapidly inactivated by micromolar concentrations of Fe2+ and H2O2....
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1969
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.98.1.190-197.1969