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Yersinia protein tyrosine phosphatase

Zhang, Z.-Y., Dixon, J. E. Active site labeling of the yersinia protein tyrosine phosphatase The determination of the pKa of active site cysteine and the function of the conserved histidine 402. Biochem. 32 (1993) 9340-9345. [Pg.196]

Stuckey, I-A., Schubert, H.L., Baumann, E.B., Zhang, Z., Dixon, IE. and Saper, M.A. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate (1994) Nature 370, 571-575... [Pg.322]

Hu, X., Stebbins, C. E. Molecular Docking and 3D QSAR Studies of Yersinia Protein Tyrosine Phosphatase YopH Inhibitors. Bioorg. Med. Chem. 2005, 13, 1101-1109. [Pg.248]

Hu X, Stebbins CE. Molecular docking and 3D-QSAR studies of Yersinia protein tyrosine phosphatase YopH inhibitors. Bioorg. Med. Chem. 2005 13 1101-1109. [Pg.2046]

Keng YF, Wu L, Zhang ZY (1999) Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase. Eur J Biochem 259 809-814... [Pg.215]

The best-studied protein tyrosine phosphatases are the high molecular weight cytoplasmic enzymes of the FTP family. X-ray structures of the human FTP IB cytosolic tyrosine phosphatase, have been solved by David Barford et and that of a Yersinia tyrosine phosphatase by Fauman et In Fig. 3.9a and b the structures of the... [Pg.41]

Hoff RH, Hengge AC, Wu L et al (2000) Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia. Biochemistry 39 46-54... [Pg.215]

Guan K, Dixon JE. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science. 1990 249 553-556. [Pg.501]

The PTPs catalyze the hydrolysis of phosphorylated tyrosine residues in proteins, to yield the free tyrosine side chains and inorganic phosphate. They are classified according to substrate specificity (1) tyrosine-specific PTPs, such as the Yersinia PTP (YopH) and the mammalian PTPIB and PTPl, which in vivo hydrolyze only pTyr residues as well as (2) the dual-specificity phosphatases (DSPs), such as the human VHR and Cdc25, which hydrolyze pTyr and pSer and pThr residues of protein substrates. Based on their cellular localization, PTPs are classified as receptor-like or intracellular. ... [Pg.331]


See other pages where Yersinia protein tyrosine phosphatase is mentioned: [Pg.263]    [Pg.233]    [Pg.55]    [Pg.56]    [Pg.263]    [Pg.233]    [Pg.55]    [Pg.56]    [Pg.191]    [Pg.72]    [Pg.313]    [Pg.379]    [Pg.121]    [Pg.23]    [Pg.343]    [Pg.229]    [Pg.250]    [Pg.504]    [Pg.383]   
See also in sourсe #XX -- [ Pg.229 ]

See also in sourсe #XX -- [ Pg.229 ]

See also in sourсe #XX -- [ Pg.56 ]




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