Beta-Glucuronidase, found in humans and E. coli, is a protein that breaks down complex carbohydrates. This protein has been associated with the severe gastrointestinal (GI) side effects associated with administration of some chemotherapeutic drugs, such as CPT-11, for colon cancer. Previous studies have identified several potent inhibitors targeting bacterial beta-glucuronidases to eliminate the GI toxicity of CPT-11; these studies have shown the inhibitor to interact with residues from the enzyme’s active site, specifically the phenylalanine in the 365 position (F365). The purpose of this project is to generate mutations on the F365 position in order to see the importance of its interaction with a Z77 inhibitor in b-glucuronidase. Mutations to the amino acid phenylalanine into leucine, alanine, tyrosine, and tryptophan have been completed, and the effects of the mutations on the enzyme’s activity and inhibitor binding have been studied.

Mutagenic analysis of E. coli b-glucuronidase: Importance of F365 in the bacterial loop in inhibitor binding

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.