Date of Award
11-7-2015
Publication Type
Master Thesis
Degree Name
M.Sc.
Department
Chemistry and Biochemistry
Keywords
Acetylation, Protein Disulfide Isomerase
Supervisor
Mutus, Bulent
Rights
info:eu-repo/semantics/openAccess
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Abstract
Protein disulfide isomerase (PDI) is crucial in the redox of disulfide bonds, where it catalyzes reductase, oxidase, and isomerase activity. The active site motif for PDI is CXXC, which is found in the a and a’ domain. PDI is mainly localized to the endoplasmic reticulum, where it plays a key role in the folding of new proteins through proper disulfide formation. With new studies about the regulation of protein activity by lysine acetylation, our group wished investigate this post-translational modification on PDI. Flanking each active site motif of PDI is a lysine residue. These active site-flanking lysine residues were mutated individually and together to observe if any catalytic change occurred. Mutation of the lysine residue to glutamine, alanine, or glutamic acid resulted in a decrease in activity, indicating the importance of the lysine residue for optimal PDI activity. Acetylation of PDI was performed by acetic anhydride, where through mass spectrometry, PDI was observed to be partially acetylated. The catalytic efficiency of the acetylated wt-PDI was observed to decrease in comparison to un-acetylated PDI. Indicating that acetylation of PDI may be a possible regulator of PDI redox activity.
Recommended Citation
Ali Khan, Hyder, "Investigations into the Regulation of the Redox Activity of Protein Disulfide Isomerase by Active Site-Flanking Lysines" (2015). Electronic Theses and Dissertations. 5501.
https://scholar.uwindsor.ca/etd/5501