Regulation of glucose 6-phosphate dehydrogenase in Zymomonas mobilis CP4

Glucose 6‐phosphate dehydrogenase was purified 29‐fold from Zymomonas mobilis. The enzyme was active with both NAD and NADP. Phosphoenolpyruvate was found to be a negative allosteric effector and ATP inhibited the enzyme non‐allosterically, at physiological concentrations.

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Bibliographic Details
Published in:FEMS microbiology letters 1985-01, Vol.27 (1), p.23-27
Main Authors: Anderson, A.J, Dawes, E.A
Format: Article
Language:English
Subjects:
adenosine triphosphate
ATP inhibition
Bacteriology
Biological and medical sciences
co‐factor specificity
ethanol
fermentation
Fundamental and applied biological sciences. Psychology
glucose-6-phosphate 1-dehydrogenase
glucose-6-phosphate dehydrogenase
Metabolism. Enzymes
Microbiology
Phosphoenolpyruvate inhibition
production
regulation
yeasts
Zymomonas mobilis
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Description
Summary:Glucose 6‐phosphate dehydrogenase was purified 29‐fold from Zymomonas mobilis. The enzyme was active with both NAD and NADP. Phosphoenolpyruvate was found to be a negative allosteric effector and ATP inhibited the enzyme non‐allosterically, at physiological concentrations.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1985.tb01631.x