Senior Project Advisor
Jeanine Amacher
Document Type
Project - Campus-only Access
Publication Date
Spring 2025
Keywords
Sortase, Enzyme, Bacteria, Protein, Biochemistry
Abstract
Class A Sortase enzymes covalently attach virulence factors to the cell wall of gram-positive bacteria. The mechanism by which this happens is thought to be mainly performed by the catalytic domain of the Sortase. However, a helical region on the N-terminus of the catalytic domain may be affecting the function of the enzyme as well. To investigate this region, extended catalytic domains were designed to include different amounts of the N-terminal helix. Results found that Sortase enzymes with these extended domains selectively showed lower enzymatic activity in class A Sortase for both staphylococcus aureus and streptococcus pyogenes, depending on the substrate. This opens the door for further studies on this region of Sortase.
Department
Chemistry
Recommended Citation
Ernst, Sarah and Amacher, Jeanine, "Extended N-terminal helix domains selectively decrease enzymatic activity in Sortase A" (2025). WWU Honors College Senior Projects. 944.
https://cedar.wwu.edu/wwu_honors/944
Type
Text
Rights
Copying of this document in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this document for commercial purposes, or for financial gain, shall not be allowed without the author’s written permission.
Language
English
Format
application/pdf