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Science 26 November 1993:
Vol. 262. no. 5138, pp. 1451 - 1453
DOI: 10.1126/science.8248785
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Articles

Science, Vol 262, Issue 5138, 1451-1453
Copyright © 1993 by American Association for the Advancement of Science

articles

Mechanism-based inactivation of prostatic acid phosphatase

JK Myers and TS Widlanski

Department of Chemistry, Indiana University, Bloomington 47405.

Protein phosphatases play important roles in the regulation of cell growth and metabolism, yet little is known about their enzymatic mechanism. By extrapolation from data on inhibitors of other types of hydrolases, an inhibitor of prostatic acid phosphatase was designed that is likely to function as a mechanism-based phosphotyrosine phosphatase inactivator. This molecule, 4-(fluoromethyl)phenyl phosphate, represents a useful paradigm for the design of potent and specific phosphatase inhibitors.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mechanism-Based Inhibition: Deriving KI and kinact Directly from Time-Dependent IC50 Values.
B.-F. Krippendorff, R. Neuhaus, P. Lienau, A. Reichel, and W. Huisinga (2009)
J Biomol Screen 14, 913-923
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Covalent inhibitors of glycosidases and their applications in biochemistry and biology.
B. P Rempel and S. G Withers (2008)
Glycobiology 18, 570-586
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Activity-based probes for protein tyrosine phosphatases.
S. Kumar, B. Zhou, F. Liang, W.-Q. Wang, Z. Huang, and Z.-Y. Zhang (2004)
PNAS 101, 7943-7948
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Chemical Strategies for Functional Proteomics.
G. C. Adam, E. J. Sorensen, and B. F. Cravatt (2002)
Mol. Cell. Proteomics 1, 781-790
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4-(Fluoromethyl)phenyl Phosphate Acts as a Mechanism-based Inhibitor of Calcineurin.
T. L. Born, J. K. Myers, T. S. Widlanski, and F. Rusnak (1995)
J. Biol. Chem. 270, 25651-25655
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Are Protein-tyrosine Phosphatases Specific for Phosphotyrosine?.
Z.-Y. Zhang and Z. Y. Zhang (1995)
J. Biol. Chem. 270, 16052-16055
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