Major
Chemistry
Anticipated Graduation Year
2021
Access Type
Restricted Access
Abstract
The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) plays an essential role in catalyzing the synthesis of glycogen in many prokaryotic and eukaryotic organisms. Regions within ADP-Glc PPase have been found to contain amino acid residues which may serve as binding sites for allosteric molecules. Previous research of other species of bacteria revealed key regulatory residues within ADP-Glc PPase. By mutating specific amino acid residues within ADP-Glc PPase in Melainabacteria, we hope to identify homologous amino acid residues that serve a regulatory function within the enzyme. Knowledge of this enzyme and the pathway it catalyzes has many applications in biotechnology and agriculture.
Faculty Mentors & Instructors
Dr. Miguel Ballicora, Department Chair, Department of Chemistry and Biochemistry; Rania Hussein, Graduate Student, Department of Chemistry and Biochemistry; Jaina Bhayani, Graduate Student, Department of Chemistry and Biochemistry
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
The Role of Arginine 27 in Melainabacteria ADP-glucose pyrophosphorylase
The enzyme ADP-glucose pyrophosphorylase (ADP-Glc PPase) plays an essential role in catalyzing the synthesis of glycogen in many prokaryotic and eukaryotic organisms. Regions within ADP-Glc PPase have been found to contain amino acid residues which may serve as binding sites for allosteric molecules. Previous research of other species of bacteria revealed key regulatory residues within ADP-Glc PPase. By mutating specific amino acid residues within ADP-Glc PPase in Melainabacteria, we hope to identify homologous amino acid residues that serve a regulatory function within the enzyme. Knowledge of this enzyme and the pathway it catalyzes has many applications in biotechnology and agriculture.
Comments
I am a biochemistry major (it was not listed in the dropdown menu)