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Mechanistic basis for the emergence of EPS1 as a catalyst in plant salicylic acid biosynthesis

By Michael P. Torrens-Spence, Tianjie Li, Ziqi Wang, Christopher M. Glinkerman, Jason O. Matos, Yi Wang, Jing-Ke Weng

Posted 22 Aug 2021
bioRxiv DOI: 10.1101/2021.08.21.457228

Unique to plants in the Brassicaceae family, the production of the plant defense hormone salicylic acid (SA) from isochorismate is accelerated by an evolutionarily young isochorismoyl-glutamate pyruvoyl-glutamate lyase, EPS1, which belongs to the BAHD acyltransferase protein family. Here, we report the crystal structures of apo and substrate-analog-bound EPS1 from Arabidopsis thaliana. Assisted by microsecond molecular dynamics simulations, we uncover a unique pericyclic rearrangement lyase mechanism facilitated by the active site of EPS1. We reconstitute the isochorismate-derived pathway of SA biosynthesis in Saccharomyces cerevisiae, which serves as an in vivo platform that helps identify active-site residues critical for EPS1 activity. This study describes the birth of a new catalyst in plant phytohormone biosynthesis by reconfiguring the ancestral active site of a progenitor enzyme to catalyze alternative reaction.

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