Major
Chemistry
Anticipated Graduation Year
2023
Access Type
Open Access
Abstract
ADP-glucose pyrophosphorylase is the enzyme responsible for the production of ADP-glucose, which is used for the synthesis of starch in plants and glycogen in bacteria. This enzyme within our model organism Agrobacterium tumefaciens is allosterically regulated through various activators and inhibitors. Previously single mutation residues at predetermined sites of interest within the wild type of A. tumefaciens have been studied. Two of these sites Tyr 39 and Arg 75, are residues located on the allosteric binding site of the activator Fru6P. Therefore, we targeted this site with a double mutation of both residues to an alanine and observed the results.
Community Partners
NA
Faculty Mentors & Instructors
Miguel Ballicora, Professor/Department Chair, Department of Chemistry and Biochemistry
Supported By
NA
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Effect of the double mutation Y39A/R75A on the allosteric regulation of ADP-glucose pyrophosphorylase from agrobacterium tumefaciens
ADP-glucose pyrophosphorylase is the enzyme responsible for the production of ADP-glucose, which is used for the synthesis of starch in plants and glycogen in bacteria. This enzyme within our model organism Agrobacterium tumefaciens is allosterically regulated through various activators and inhibitors. Previously single mutation residues at predetermined sites of interest within the wild type of A. tumefaciens have been studied. Two of these sites Tyr 39 and Arg 75, are residues located on the allosteric binding site of the activator Fru6P. Therefore, we targeted this site with a double mutation of both residues to an alanine and observed the results.