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Regulation of glucose 6-phosphate dehydrogenase in Zymomonas mobilis CP4
Authors:A.J. Anderson  E.A. Dawes
Affiliation:Department of Biochemistry, University of Hull, Hull, HU6 7RX, U.K.
Abstract:Abstract 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.
Keywords:Phosphoenolpyruvate inhibition    ATP inhibition    co-factor specificity
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