5284-78-6Relevant academic research and scientific papers
Synthesis and characterization of a novel class of protein tyrosine phosphatase inhibitors
Ibrahimi, Omar A.,Wu, Li,Zhao, Kang,Zhang, Zhong-Yin
, p. 457 - 460 (2000)
Nonpeptidyl aryloxymethylphosphonates were prepared and evaluated as protein tyrosine phosphatase inhibitors. The results suggest that aryloxymethylphosphonates are effective nonhydrolyzable phosphotyrosine surrogates and provide further insight into the molecular mechanisms by which phosphate mimics inhibit phosphatase function. (C) 2000 Elsevier Science Ltd. All rights reserved.
A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano-phosphonic acids as motifs for inhibition of phosphatases
Iyer, Subashree,Younker, Jarod M.,Czyryca, Przemyslaw G.,Hengge, Alvan C.
, p. 5931 - 5935 (2007/10/03)
Nonhydrolyzable analogues of both stereoisomers of phosphotyrosine, and a series of related aryloxy (or thio) methyl and aryloxy (or thio) ethyl phosphonic acids of the general formula RX-(CH2)n-PO 3H2 (where X = O or S and n = 1 or 2), have been tested as nonhydrolyzable mimetics of phosphatase substrates. These compounds were tested against a panel of phosphatases (two alkaline phosphatases, a protein-tyrosine phosphatase, and two serine/threonine phosphatases) with different active site motifs. The compounds exhibit competitive inhibition toward all enzymes tested, with the best inhibition expressed toward the Ser/Thr phosphatases. The stereoisomers of the phosphotyrosine analogues exhibited an unexpected difference in their inhibitory properties toward the protein-tyrosine phosphatase from Yersinia. The Ki for the d isomer is 33-fold lower than that of the l isomer, and is more than an order of magnitude lower than the reported Km of the substrate l-phosphotyrosine.
