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	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	mechanism, kinetic isotope effects	650353	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	mechanism, overview	651550	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	mechanism, role of residue 182	649774	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	mechanism, transition state of reaction, kinetic isotope effects, overview	649081	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	motif H74C(X)5R81 is involved in catalysis	666291	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	overview on mechanism and transition state	651283	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	ping-pong mechanism, catalysis proceeds through a two-step mechanism involving a phosphocysteine intermediate. In the first step, a nucleophilic cysteine thiolate attacks the phosphate ester moiety of the substrate, resulting in formation of a phosphoenzyme intermediate with release of the peptidyl tyrosine. The second step occurs via attack of water on the phosphoenzyme intermediate, and yields the final products inorganic phosphate and the regenerated enzyme. The central binding site for the substrate is the P-loop, a region at the bottom of a pocket that includes the nucleophilic cysteine and backbone amide groups oriented in a horseshoe fashion, catalytic cycle, detailed overview	709102	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	the phosphatase domain of PTPRs catalyze a two-step phosphate monoester hydrolysis reaction through a highly conserved sequence motif (H/V)CX5R(S/T) with a nucleophilic cysteine	749850	
3.1.3.48	[a protein]-tyrosine phosphate + H2O = [a protein]-tyrosine + phosphate	thermodynamic parameters	650146