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Rat liver microsomal glucose 6-phosphatase previously has been shown to catalyze an inorganic pyrophosphate-glucose phosphotransferase reaction. Citrate, which has been employed as a buffer in some earlier studies of this enzyme, recently has been found to inhibit both of these activities. Detailed investigations of the inhibition of both phosphohydrolase(More)
The multifunctional nature of classical microsomal glucose-6-phosphatase (D-glucose-6-P phosphohydrolase, EC 3.1.3.9) is now well documented (see, for example, refs. 1-8). Inherent in the reaction mechanism proposed by Arion and Nordlie2 to describe the variety of phosphohydrolase and phosphotransferase reactions catalyzed by the enzyme is the mutual(More)
Inhibition of rat liver microsomal glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9) by orthophosphate and organophosphate esters was examined at pH 6.0 and 7.5 with and without enzyme pretreatment with 0.2% (w/v) deoxycholate. Inhibition by orthophosphate and monoethyl phosphate was competitive with respect to glucose-6-P while(More)
  • D G Lygre
  • Canadian journal of biochemistry
  • 1976
Inhibition by saccharin of rat liver glucose-6-phosphatase (EC 3.1.3.9) generally decreased as the pH increased in the range pH 4-8. This pattern was exhibited by homogenates from control and alloxan-treated animals assayed each in the absence and presence of 0.2% (w/v) deoxycholate. Saccharin inhibited in competitive fashion with respect to(More)
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