Literature DB >> 25199451

Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds.

Daniel Rueda1, Patricia Sheen1, Robert H Gilman2, Carlos Bueno1, Marco Santos1, Victoria Pando-Robles3, Cesar V Batista4, Mirko Zimic5.   

Abstract

Recombinant wild-pyrazinamidase from H37Rv Mycobacterium tuberculosis was analyzed by gel electrophoresis under differential reducing conditions to evaluate its quaternary structure. PZAse was fractionated by size exclusion chromatography under non-reducing conditions. PZAse activity was measured and mass spectrometry analysis was performed to determine the identity of proteins by de novo sequencing and to determine the presence of disulfide bonds. This study confirmed that M. tuberculosis wild type PZAse was able to form homo-dimers in vitro. Homo-dimers showed a slightly lower specific PZAse activity compared to monomeric PZAse. PZAse dimers were dissociated into monomers in response to reducing conditions. Mass spectrometry analysis confirmed the existence of disulfide bonds (C72-C138 and C138-C138) stabilizing the quaternary structure of the PZAse homo-dimer.
Copyright © 2014 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Dimer; Drug resistance; Multimer; Mycobacterium; Nicotinamidase; Nicotinamide; Pyrazinamidase; Pyrazinamide; Reducing stress; Tuberculosis

Mesh：

Substances：

Year:  2014        PMID： 25199451      PMCID： PMC4258149          DOI： 10.1016/j.tube.2014.08.008

Source DB:  PubMed          Journal:  Tuberculosis (Edinb)        ISSN： 1472-9792            Impact factor:   3.131


  15 in total

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1.  Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity.

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