Date of Award
2016
Degree Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
Department
Chemistry
Abstract
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.
Recommended Citation
Hill, Benjamin Luke, "Studies Into the Allosteric Regulation of ADP-Glucose Pyrophosphorylases" (2016). Dissertations. 1947.
https://ecommons.luc.edu/luc_diss/1947
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Copyright Statement
Copyright © 2016 Benjamin Luke Hill
