Extended Data Fig. 4: Kinetic characterization of OE1.3 and OE1.4 towards the hydrolysis of (R)- and (S)- fluorescein 2-phenylpropanoate.
From: Design and evolution of an enzyme with a non-canonical organocatalytic mechanism
a, Michaelis–Menten plots of fluorescein (R)-2-phenylpropanoate and fluorescein (S)-2-phenylpropanoate hydrolysis (shown in black and red, respectively), catalysed by OE1.3. The averaged initial rates were fitted to the Michaelis–Menten equation using Origin software. b, Michaelis–Menten plots of fluorescein (R)-2-phenylpropanoate and fluorescein (S)-2-phenylpropanoate hydrolysis (shown in black and red, respectively) catalysed by OE1.4. The averaged initial rates were fitted to the equation for Michaelis–Menten with substrate inhibition using Origin software. Data are mean ± s.d. of measurements made in triplicate. c, Table summarizing the kinetic parameters for the hydrolysis of both enantiomers of fluorescein 2-phenylpropanoate catalysed by OE1.3 and OE1.4. Data are mean ± s.d. of measurements made in triplicate.
