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Investigation of novel inhibitory compounds of O-acetyltransferase A (OatA) from Staphylococcus aureus

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dc.contributor.advisor Clarke, Anthony Kell, Laura 2015-12-17T20:53:34Z 2016-12-04T06:00:16Z 2015-12 2015-12-04 2015-12-17
dc.description.abstract O-Acetylation of the N-acetylmuramic acid residue of peptidoglycan (PG) prevents the hydrolysis of the cell wall by autolysins and muramidases and is an important virulence factor in many bacteria. O-Acetylated PG aids in the survival of these bacteria within the host environment while preventing detection and clearance. O-Acetyltransferase A (OatA) has been identified as the enzyme responsible for this modification in Gram-positive bacteria. This study aims to expand our understanding of the O-acetylation of PG, and identify inhibitors of OatA from S. aureus to demonstrate OatA as a potential antibacterial target. Presented here are the kinetic parameters of pseudo-substrate donors and the first direct evidence of a Ser-His-Asp catalytic center of OatA. High-throughput screening has led to the identification of a class of compounds, coumarins, which show promising inhibitory properties in vitro. This research represents the first steps in providing evidence that OatA is a prospective pharmacological target. en_US
dc.language.iso en en_US
dc.publisher University of Guelph en_US
dc.subject OatA en_US
dc.subject peptidoglycan en_US
dc.subject S. aureus en_US
dc.subject coumarin en_US
dc.subject inhibition en_US
dc.subject acetylation en_US
dc.title Investigation of novel inhibitory compounds of O-acetyltransferase A (OatA) from Staphylococcus aureus en_US
dc.type Thesis en_US Molecular and Cellular Biology en_US Master of Science en_US Department of Molecular and Cellular Biology en_US
dc.rights.license All items in the Atrium are protected by copyright with all rights reserved unless otherwise indicated. University of Guelph en_US

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