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Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
Data indicate a dissociative transition state with the leaving group departing as the nitrophenolate anion but suggest more nucleophilic participation than in the solution reaction, indicating that the chemical step is rate-limiting for V/K. Expand
Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.
Property of the three mutant proteins in partial reactions were examined to define more clearly the roles of these residues in the catalytic cycle and suggest that Lys 345 functions as the base in the ionization of 2-PGA and that Glu 211 participates in the second step of the reaction. Expand