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- W2059557126 abstract "Thiophosphorylated proteins or peptides are poor substrates of protein phosphatases. As a competitive inhibitor of a protein tyrosine phosphatase, a tyrosine-thiophosphorylated nonapeptide ENDYINASL displays a KI value of 0.25 microM, in comparison with the Km value of 3.1 microM exerted by the enzyme toward the phosphorylated form of the peptide. Furthermore, adenosine 5'-O-3-thiotriphosphate is also an effective competitive inhibitor of the enzyme with a KI value of 1.4 microM. In contrast, ATP and 5'-adenylimidodiphosphate are much less effective, indicating that the thiophosphate group plays a major role in the inhibition process. Further supporting this is the fact that sodium thiophosphate is a more effective inhibitor than inorganic phosphate (IC50 = 0.47 mM versus 15 mM). The inhibition by thiophosphate compounds is specific for PTPs. The data suggest the application of thiophosphate derivatives as specific inhibitors of PTPs." @default.
- W2059557126 created "2016-06-24" @default.
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- W2059557126 date "1996-01-01" @default.
- W2059557126 modified "2023-10-18" @default.
- W2059557126 title "Thiophosphate Derivatives as Inhibitors of Tyrosine Phosphatases" @default.
- W2059557126 doi "https://doi.org/10.1006/bbrc.1996.0085" @default.
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