Extended Data Fig. 3: The effect of buffer composition on the Michaelis–Menten kinetic profile of SNAr1.3.
From: Engineered enzymes for enantioselective nucleophilic aromatic substitutions
Michaelis–Menten plots for the SNAr reaction between 1 and 2 catalysed by SNAr1.3, acquired with SNAr1.3 in either PBS (10 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl) or sodium phosphate (NaPi) (46.4 mM Na2HPO4, 3.6 mM NaH2PO4). Assays were performed at a fixed concentration of 1 (75 mM) and varying concentrations of 2 in PBS pH 8.0 (grey circle markers) or NaPi pH 8.0 (blue square markers). The plots show the averaged initial rates that were fitted to the second-order polynomial (quadratic) using GraphPad Prism software, as saturation of 2 was not achieved. Error bars represent the standard deviation of measurements made in triplicate. See Supplementary Data for source data.
