Extended Data Fig. 6: The R294/E414/R443 triad is vital for the exo activity in MaDA-3.
From: Enzymatic control of endo- and exo-stereoselective Diels–Alder reactions with broad substrate scope
All these mutations regardless of synonymous mutation or not led to notable decrease of the exo activity of MaDA-3, indicating the hydrogen bonding interactions among the R294/E414/R443 triad are delicate contributors to form strong cation-π interaction between R294 and dienophile for promoting exo selective reaction. The E414 and R443 in MaDA-3 were found to be indispensable for endo activity of MaDA-3 since mutations at these two residues completely lost endo activities. The red and blue columns indicate the exo-activities and endo activities respectively. Enzyme activity values represent mean ± standard deviation (s.d.) of three independent replicates.
