The mechanism of the phosphoryl transfer catalyzed by Yersiniaprotein-tyrosine phosphatase: a computational and isotope effect study
Document Type
Article
Journal/Book Title
Biochimica et Biophysica Acta
Publication Date
2001
Volume
1547
First Page
245
Last Page
253
Abstract
In order to evaluate various mechanistic proposals that have been made regarding the mechanism of the first step of the reaction catalyzed by protein-tyrosine phosphatases, new experimental data have been obtained, and some existing data have been carefully reevaluated. New kinetic isotope effect data for the uncatalyzed hydrolysis of p-nitrophenyl phosphate allow a better evaluation of previously reported data from enzymatic reactions with this substrate. The interpretation, and misinterpretation, of pH rate studies is considered. The pathway of this reaction has been modeled computationally and is found to be generally consistent with experimental studies, except for the extent of proton transfer to the leaving group.
Recommended Citation
P. G. Czyryca, A. C. Hengge. “The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: a computational and isotope effect study.” Biochim Biophys Acta 2001, 1547, 245-53
