Fig. 3. A) Extracted initial velocities plotted over substrate concentration. Michaelis–Menten equation is fitted on data for determination of K_m constant. B) 3D structure of active dimer of RgDAAOx with one monomer showing the surface structure. Sites mutated in variants are highlighted as red spheres. FAD is colored in yellow and d-alanine substrate is shown in orange (PDB: 1c0p). C) Mutations and Michaelis–Menten constants for yeast surface displayed wild type and DAAOx-variants.