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  • Title: Anomer specificity of glucose-6-phosphatase and glucokinase.
    Author: Furuya E, Hotta K, Tagawa K.
    Journal: Biochem Biophys Res Commun; 1986 Dec 30; 141(3):931-6. PubMed ID: 3028393.
    Abstract:
    The anomeric form of glucose produced by glucose-6-phosphatase was studied using an apparatus that specifically measures beta-D-glucose. The time course of beta-D-glucose formation from glucose-6-P by glucose-6-phosphatase is essentially linear. In the presence of mutarotase, this rate is reduced to 70% of that obtained in the absence of mutarotase. When detergent treated microsomes were used, the rate of beta-D-glucose formation is unaffected by mutarotase. These results suggest that only beta-anomer of glucose is produced by microsomal glucose-6-phosphatase and this specificity is determined by translocase for glucose-6-P or glucose. It was also demonstrated that alpha-D-glucose is the substrate for glucokinase.
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