Major
Chemistry
Anticipated Graduation Year
2023
Access Type
Open Access
Abstract
The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) is responsible for the production of ADP-glucose, the fundamental molecule in the production of starch in plants and glycogen in bacteria. This enzyme is regulated allosterically by various sugar phosphates specific to each model organism. Past studies have sought to better understand this enzyme by exploring different amino acid residues within the enzyme and how they affect its activity. Therefore, in our study we investigate the homologous residues Thr79 in E. coli and Ser65 in Melainabacteria to determine if they are critical for allosteric activation as we suspect them to be.
Faculty Mentors & Instructors
Miguel Ballicora, Professor/Department Chair, Department of Chemistry and Biochemistry
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Insight into the regulation of ADP-glucose pyrophosphorylase: Importance of homologous serine/threonines in the allosteric site
The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) is responsible for the production of ADP-glucose, the fundamental molecule in the production of starch in plants and glycogen in bacteria. This enzyme is regulated allosterically by various sugar phosphates specific to each model organism. Past studies have sought to better understand this enzyme by exploring different amino acid residues within the enzyme and how they affect its activity. Therefore, in our study we investigate the homologous residues Thr79 in E. coli and Ser65 in Melainabacteria to determine if they are critical for allosteric activation as we suspect them to be.