The Cys(X)5Arg Catalytic Motif in Phosphoester Hydrolysis

Zhong yin Zhang, Yuan Wang, Li Wu, Eric B. Fauman, Jeanne A. Stuckey, Heidi L. Schubert, Mark A. Saper, Jack E. Dixon

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161 Scopus citations

Abstract

The Yersinia protein tyrosine phosphatase (PTPase) was identified in the genus of bacteria responsible for the plague or the Black Death and was shown to be essential for pathogenesis. The threedimensional structure of the catalytic domain of the Yersinia PTPase has been solved, and this information along with a detailed kinetic analysis has led to a better understanding of the catalytic mechanism of the PTPase. Mutational and chemical modification experiments have established that an invariant Cys residue (Cys403) is directly involved in formation of a covalent phosphoenzyme intermediate. We have shown that Arg409 plays a critical role in PTPase action and that the Cys(X)5Arg active site motif forms a phosphate-binding loop which appears to represent the essential features necessary for catalysis by the PTPases, the dual specific phosphatases, and the low molecular weight acid phosphatases.

Original languageEnglish (US)
Pages (from-to)15266-15270
Number of pages5
JournalBiochemistry
Volume33
Issue number51
DOIs
StatePublished - Dec 1 1994

ASJC Scopus subject areas

  • Biochemistry

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    Zhang, Z. Y., Wang, Y., Wu, L., Fauman, E. B., Stuckey, J. A., Schubert, H. L., Saper, M. A., & Dixon, J. E. (1994). The Cys(X)5Arg Catalytic Motif in Phosphoester Hydrolysis. Biochemistry, 33(51), 15266-15270. https://doi.org/10.1021/bi00255a007