Date of Award

4-19-2024

Document Type

Honors Thesis

Department

Biology

First Advisor

Peter Lyons

Abstract

Enzymes catalyze chemical reactions; however, some proteins related to enzymes lack enzyme activity. To investigate changes that occur as enzymes becomes pseudoenzymes, I studied a unique family of fungal carboxypeptidases. I identified all fungal carboxypeptidase protein sequences in the NCBI database, constructed an alignment and phylogenetic tree for sequence comparison, and used Alphafold2 for 3D modeling of representative proteins. Fourteen unique groups were identified. All fungal proteins selected are separated into 3 categories, predicted to be active, intermediate, and inactive, respectively. Proteins predicted to be pseudoenzymes contained additional loops in mutation hotspots not found in predicted active enzymes. This research integrates modern bioinformatics tools for analyzing enzyme function and contributes to understanding the evolution of enzymes.

Subject Area

Carboxypeptidases; Enzymes: Bioinformatics

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