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Elucidating the enzymatic function of resuscitation promoting factor B, RpfB, from Mycobacterium tuberculosis

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Title: Elucidating the enzymatic function of resuscitation promoting factor B, RpfB, from Mycobacterium tuberculosis
Author: Samson, Jonathan
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Clarke, Anthony
Abstract: The nature of the muralytic activity of resuscitation promoting factor B (RpfB) from Mycobacterium tuberculosis has been the subject of much debate. Whether this enzyme acts similarly to a lytic transglycosylase or glycoside hydrolase (GH) remained unknown until now. In order to investigate the activity of RpfB, a stable and active form of RpfB, containing only the catalytic domain (RpfBC), was obtained. The reaction products of RpfBC were analyzed by reverse phase high performance liquid chromatography and electrospray ionization mass spectrometry on an ion-trap mass spectrometer. Additionally, reactions in [18O]H2O were performed and the products were analyzed using RP-HPLC and ESI-quadrupole time of flight MS. These assays show that RpfBC from M. tuberculosis functions like an endo-acting GH. Although GHs do not make good drug targets, RpfB’s distinction from the paralogs of M. tuberculosis does not exclude the possibility that they might be good targets and warrants further investigation.
URI: http://hdl.handle.net/10214/8699
Date: 2015-01
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