Extended Data Fig. 1: Kinetic characterization of BH32.
From: Design and evolution of an enzyme with a non-canonical organocatalytic mechanism
Michaelis–Menten plot showing the rate of His23 acylation (the ‘burst phase’) with varying concentrations of fluorescein 2-phenylacetate. Averaged initial rates were fitted to the Michaelis–Menten equation to derive rate constant kobs 1.3 ± 0.03 min−1 and the enzyme–substrate dissocation constant KS 30.9 ± 1.8 µM (R2 = 0.99). Data are mean ± s.d. of measurements made in triplicate.
