Title:
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Investigation of Protein and Inhibitor Binding to O-Acetylpeptidoglycan Esterase 1 from Neisseria gonorrhoeae |
Author:
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Ecclestone, Mark
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Department:
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Department of Molecular and Cellular Biology |
Program:
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Molecular and Cellular Biology |
Advisor:
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Clarke, Anthony |
Abstract:
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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. |
URI:
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http://hdl.handle.net/10214/9293
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Date:
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2015-10 |
Terms of Use:
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