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J. Biol. Chem., Vol. 266, Issue 26, 17026-17030, Sep, 1991
KL Guan and JE Dixon
A recombinant protein-tyrosine-phosphatase has been expressed in
Escherichia coli and purified to a single band by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis using affinity chromatography.
When the phosphatase was allowed to react with 32P- labeled substrates and
then rapidly denaturated, a 32P-labeled phosphoprotein could be visualized
by sodium dodecyl sulfate- polyacrylamide gel electrophoresis. Transient
formation of a 32P- labeled phosphoprotein was observed, and the
32P-labeled protein disappeared as substrate was consumed. In the presence
of 32P-labeled p- nitrophenyl phosphate, 0.27 mol of phosphate was
incorporated per mol of protein-tyrosine-phosphatase. Site-directed
mutagenesis of a catalytically essential cystine residue (position 215) in
the recombinant protein resulted in an inactive enzyme, and no
phosphoprotein was formed. The 32P-labeled phosphoprotein showed a maximum
lability between pH 2.5 and 3.5 and was rapidly decomposed in the presence
of iodine. These properties, along with additional site- directed
mutations, suggest that the protein-tyrosine-phosphatase forms a covalent
thiol phosphate linkage between Cys215 and phosphate.
Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
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A. J. Flint, T. Tiganis, D. Barford, and N. K. Tonks Development of "substrate-trapping" mutan |
