Major
Chemistry
Access Type
Open Access
Abstract
ADP-glucose Pyrophosphorylase (ADP-GlcPPase) is a regulatory enzyme in bacteria that synthesizes glycogen. A. tumefaciens ADP-Glc PPase is activated by Fructose 6-phosphate (Fru6P) and Pyruvate (Pyr). To investigate Fru6P binding, the Tyrosine 124 and Arginine 75 residues of A. tumefaciens ADP-Glc PPase were mutated to Alanine. We found that Y124A and R75A had some activation by Fru6P and Pyr but did not reach a Vmax equivalent to Wildtype. R75A/Y124A had similar activation to the single mutants. Thermal Shift assays tested the enzyme-ligand binding of the activators. This project expanded our understanding of the allosteric binding in A. tumefaciens ADP-Glc PPase.
Faculty Mentors & Instructors
Dr. Miguel A. Ballicora, Chair of Chemistry and BioChemistry Department; Claire Kennedy, PhD student, Biochemistry department
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Examining the Efficacy of the Allosteric site in ADP Glucose Pyrophosphorylase from A. tumefaciens
ADP-glucose Pyrophosphorylase (ADP-GlcPPase) is a regulatory enzyme in bacteria that synthesizes glycogen. A. tumefaciens ADP-Glc PPase is activated by Fructose 6-phosphate (Fru6P) and Pyruvate (Pyr). To investigate Fru6P binding, the Tyrosine 124 and Arginine 75 residues of A. tumefaciens ADP-Glc PPase were mutated to Alanine. We found that Y124A and R75A had some activation by Fru6P and Pyr but did not reach a Vmax equivalent to Wildtype. R75A/Y124A had similar activation to the single mutants. Thermal Shift assays tested the enzyme-ligand binding of the activators. This project expanded our understanding of the allosteric binding in A. tumefaciens ADP-Glc PPase.