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- W1493332113 abstract "The ADP-glucose pyrophosphorylases from R. capsulata and A. tumefaciens are found to be activated by fructose-6-P and to lesser extents by pyruvate, KDPG, ribose-5-P, and deoxyribose-5-P. Fructose-6-P increases the Vmax of synthesis of ADP-glucose for both enzymes about 6-fold. In addition the S0.5 values (concentrations of substrates giving 50% of maximal velocity) for ATP and glucose-1-P for both enzymes are decreased in the presence of the activator, fructose-6-P. Both enzymes are inhibited by Pi, AMP, ADP, and phosphoenolpyruvate. However the presence of fructose-6-P decreases the sensitivities of the enzymes to inhibition by the above compounds. The concentration of Pi, AMP, ADP, and PEP required for 50% inhibition in the absence of fructose-6-P are 0.26, 0.64, 0.41, and 0.047 mm, respectively. These values are increased to 5.8, 7.3, 3.8, and 1.6 mm, respectively, in the presence of 1.0 mm fructose-6-P. These findings are discussed with respect to glycogen synthesis in these microorganisms and are related to the findings that indicate that both R. capsulata and A. tumefaciens catabolize glucose mainly via the Entner-Doudoroff pathway." @default.
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- W1493332113 title "Biosynthesis of bacterial glycogen" @default.
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- W1493332113 doi "https://doi.org/10.1016/0003-9861(70)90010-x" @default.
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