结核分枝杆菌酪氨酸磷酸酶 A（PtpA）的活性受 S-亚硝基化调节。
Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation.
机构信息
Centro de Biologia Molecular Estrutural, BQA CCB UFSC, Florianópolis-SC, Brazil.
出版信息
Chem Commun (Camb). 2010 Oct 28;46(40):7501-3. doi: 10.1039/c0cc01704c. Epub 2010 Sep 9.
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.
结核分枝杆菌 PtpA 和 PtpB 是该病原体中仅有的两种磷酸酪氨酸磷酸酶（Ptps），它们在分枝杆菌在巨噬细胞内的存活中发挥重要作用。本研究旨在研究结核分枝杆菌 PtpA 和 PtpB 对 S-亚硝基化的敏感性，S-亚硝基化是一氧化氮（NO）和蛋白质中特定半胱氨酸（硫）残基之间的一种可逆的共价键。NO 没有修饰 PtpB，相反，通过定点突变鉴定出 PtpA Cys53 是 S-亚硝基化的靶标。
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