3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate activation mechanism 652498 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate arrangement of two metal ions, a phosphate ion, and amino acid residues in the catalytic site is identical to that of PS/Tpases 665427 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate comparison of kinetic properties of different transmembrane and cytosolic isozymes 650430 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate conformation of active site is favorable for phosphotyrosine binding. Interaction of D115 and R13 to stabilize the conformation of the active cavity. A41 and G45 form a noncharged surface around the active cavity, which is surrounded by a flexible wall made of the loop region from F40 to T48 665402 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate for both alkyl and aryl substrates, including the activated substrate 4-nitrophenyl phosphate with its particularly good leaving group, general acid catalysis in PTPs is highly efficient and fully neutralizes the leaving group in the transition state. Mutating the conserved aspartic acid to glutamine causes the expected reductions in rate of several orders of magnitude and loss of the basic limb in pH-rate profiles, kinetic isotope effects, general acid catalysis mechanism, overview -, 749953 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate H148 acts as a general acid catalyst, D115 assists the protonation of the leaving group of a substrate, and D76 and D112 are involved in binding of magnesium ions 664363 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate in addition to active site, enzyme has a low-affinity noncatalytic aryl phosphate-binding site 664310 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism 650928, 652000, 94997, 95002 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism of the dephosphorylation catalysed by MptpA 714454 3.1.3.48 [a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate mechanism, features required for substrate 652017