Issue 40, 2010
From the journal:

Chemical Communications

Mycobacterium tuberculosistyrosinephosphatase A (PtpA) activity is modulated by S-nitrosylation†

Gabriela Ecco,a   Javier Vernal,a   Guilherme Razzera,a   Priscila Alves Martins,a   Camila Matiolloa  and  Hernán Terenzi*a  

* Corresponding authors

a Centro de Biologia Molecular Estrutural, BQA CCB UFSC, Florianópolis-SC, Brazil
E-mail: hterenzi@ccb.ufsc.br
Fax: +55 48 3721 6973
Tel: +55 48 3721 6426

Abstract

M. tuberculosis PtpA and PtpB, the only two phosphotyrosine phosphatases (Ptps) present in this pathogen, play an important role in mycobacteria survival inside macrophages. The aim of the present work was to investigate M. tuberculosis PtpA and PtpB susceptibility to S-nitrosylation, a reversible covalent bond between nitric oxide (NO) and specific cysteine (sulfur) residues in proteins. PtpB was not modified by NO, in contrast, PtpA Cys53 was identified by site directed mutagenesis as the target of S-nitrosylation.

Graphical abstract: Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation

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Article information

DOI
https://doi.org/10.1039/C0CC01704C
Article type
Communication
Submitted
02 Jun 2010
Accepted
21 Aug 2010
First published
09 Sep 2010

Chem. Commun., 2010,46, 7501-7503

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Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation

G. Ecco, J. Vernal, G. Razzera, P. A. Martins, C. Matiollo and H. Terenzi, Chem. Commun., 2010, 46, 7501 DOI: 10.1039/C0CC01704C

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