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- W1491689768 abstract "Adenosine diphosphate-glucose pyrophosphorylase from Arthrobacter viscosus NRRL B1973 was found to be activated by fructose-6-P, pyruvate, deoxyribose-5-P and ribose-5-P. Fructose-6-P was the most effective activator. Fructose-6-P increased the Vmax of pyrophosphorolysis of ADP-glucose 2.5-fold, and the Vmax of synthesis of ADP-glucose from ATP and glucose-1-P, 7-fold. The apparent Km's for ATP, pyrophosphate, and ADP-glucose were decreased in the presence of fructose-6-P. Pyruvate increased the Vmax of pyrophosphorolysis 2-fold and of synthesis 6-fold. However, pyruvate only decreased the Km for pyrophosphate. The Km for glucose-1-P was not effected by either pyruvate or fructose-6-P. The enzyme was found to be inhibited by phosphate, sulfate, AMP, ADP, phosphoenolpyruvate, GMP, and GDP. However, fructose-6-P completely overcame (reversed) these inhibitions. The relationship of these findings to the control of bacterial glycogen synthesis is discussed." @default.
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- W1491689768 date "1966-01-01" @default.
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- W1491689768 title "Biosynthesis of bacterial glycogen" @default.
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- W1491689768 doi "https://doi.org/10.1016/0003-9861(66)90044-0" @default.
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