| Literature DB >> 20830431 |
Gabriela Ecco1, Javier Vernal, Guilherme Razzera, Priscila Alves Martins, Camila Matiollo, Hernán Terenzi.
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.Entities:
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Year: 2010 PMID: 20830431 DOI: 10.1039/c0cc01704c
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222