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• W2068298222 abstract "Fructose-1,6-bisphosphate activates ADP-glucose pyrophosphorylase and the synthesis of glycogen in Escherichia coli. Here, we show that although pyruvate is a weak activator by itself, it synergically enhances the fructose-1,6-bisphosphate activation. They increase the enzyme affinity for each other, and the combination increases Vmax, substrate apparent affinity, and decreases AMP inhibition. Our results indicate that there are two distinct interacting allosteric sites for activation. Hence, pyruvate modulates E. coli glycogen metabolism by orchestrating a functional network of allosteric regulators. We postulate that this novel dual activator mechanism increases the evolvability of ADP-glucose pyrophosphorylase and its related metabolic control." @default.
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• W2068298222 date "2014-08-07" @default.
• W2068298222 modified "2023-10-13" @default.
• W2068298222 title "A Novel Dual Allosteric Activation Mechanism of Escherichia coli ADP-Glucose Pyrophosphorylase: The Role of Pyruvate" @default.
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• W2068298222 doi "https://doi.org/10.1371/journal.pone.0103888" @default.
• W2068298222 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4125136" @default.
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