Date of Award
Doctor of Philosophy (PhD)
The synthesis of glycogen in bacteria and starch in plants is allosterically controlled by the production of ADP-glucose by ADP-glucose pyrophosphorylase. Using computational studies, site directed mutagenesis, and kinetic characterization, and protein crystallography we found a critical region for transmitting the allosteric signal in the Escherichia coli and A. tumefaciens ADP-glucose pyrophosphorylase. Molecular dynamics simulations and structural comparisons with other ADP-glucose pyrophosphorylases provided information to hypothesize communication pathways that link allosteric and active sites, and this was tested by site-directed mutagenesis and kinetic characterization of the mutant enzymes. In addition, the application of x-ray crystallography enabled the pinpointing of the allosteric binding site in the A. tumefaciens enzyme. These findings may be important for understanding allosteric regulation of ADP-glucose pyrophosphorylases, which is a critical enzyme for the production of glycogen and starch, which are some of the most abundant polysaccharides on earth.
Hill, Benjamin Luke, "Studies Into the Allosteric Regulation of ADP-Glucose Pyrophosphorylases" (2016). Dissertations. 1947.
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Copyright © 2016 Benjamin Luke Hill