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Investigation of Protein and Inhibitor Binding to O-Acetylpeptidoglycan Esterase 1 from Neisseria gonorrhoeae

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dc.contributor.advisor Clarke, Anthony
dc.contributor.author Ecclestone, Mark
dc.date.accessioned 2015-10-09T17:55:08Z
dc.date.available 2015-10-09T17:55:08Z
dc.date.copyright 2015-10
dc.date.created 2015-10-08
dc.date.issued 2015-10-09
dc.identifier.uri http://hdl.handle.net/10214/9293
dc.description.abstract O-Acetylpeptidoglycan esterase 1 (Ape1) is a periplasmic esterase present in pathogenic organisms that produce O-acetylated peptidoglycan. Ape1a plays a crucial role in the growth of these bacteria by regulating the turnover of peptidoglycan through catalytic removal of the C-6 acetyl group of the modified peptidoglycan. Specifically, Ape1a activity is necessary for peptidoglycan turnover by the main autolytic enzymes, lytic transglycosylases (LTs); LTs are blocked by the presence of an acetyl group on the C-6 hydroxyl of N-acetylmuramic acid. Purpurin has been observed to inhibit the esterase activity of Ape1 in vitro and inhibits the growth of bacteria that produce O-acetylpeptidoglycan. This study found that Ape1 binds to FtsZ in a presumed multi-enzyme complex. The 2-hydroxyl group of anthraquinones, such as purpurin or alizarin, needs to be deprotonated to work as a suitable inhibitor of Ape1. Purpurin was demonstrated to work synergistically with aminoglycosides against Bacillus cereus species. en_US
dc.language.iso en en_US
dc.subject Inhibition en_US
dc.subject O-acetylpeptidoglycan esterase en_US
dc.subject Purpurin en_US
dc.subject O-acetylation en_US
dc.title Investigation of Protein and Inhibitor Binding to O-Acetylpeptidoglycan Esterase 1 from Neisseria gonorrhoeae en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Bachelor of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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