ArticleNature communications2024
Mechanistic basis for the emergence of EPS1 as a catalyst in salicylic acid biosynthesis of Brassicaceae.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia.Science advances · 2026Article
- The BAHD Acyltransferase Gene Family: Evolutionary Dynamics, Biochemical Mechanisms, and Roles in Plant Stress Adaptation.Plant biotechnology journal · 2026Review
- Molecular basis of very-long-chain fatty acid elongation by the CER6-GL2 enzyme complex in plant wax biosynthesis.Science advances · 2025Article
- Salicylic acid biosynthesis via the PAL pathway requires benzaldehyde synthase and a benzyl salicylate-specific esterase.The Plant cell · 2025Article
- Metabolomic Insights into Cross-Feeding Interactions Between Priestia megaterium PM and Pseudomonas fluorescens NO4: Unveiling Microbial Communication in Plant Growth-Promoting Rhizobacteria.Microbial ecology · 2025Article
- A SlMYB78-regulated bifunctional gene cluster for phenolamide and salicylic acid biosynthesis during tomato domestication, reducing disease resistance.Journal of integrative plant biology · 2025Article
- Modulation of Plant Interactions with Whitefly and Whitefly-Borne Viruses by Salicylic Acid Signaling Pathway: A Review.Viruses · 2025Review
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Authors and funding
11 authors.
Funding
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Abstract
Salicylic acid (SA) production in Brassicaceae plants is uniquely accelerated from isochorismate by EPS1, a newly identified enzyme in the BAHD acyltransferase family. We present crystal structures of EPS1 from Arabidopsis thaliana in both its apo and substrate-analog-bound forms. Integrating microsecond-scale molecular dynamics simulations with quantum mechanical cluster modeling, we propose a pericyclic rearrangement lyase mechanism for EPS1. We further reconstitute the isochorismate-derived SA biosynthesis pathway in Saccharomyces cerevisiae, establishing an in vivo platform to examine the impact of active-site residues on EPS1 functionality. Moreover, stable transgenic expression of EPS1 in soybean increases basal SA levels, highlighting the enzyme's potential to enhance defense mechanisms in non-Brassicaceae plants lacking an EPS1 ortholog. Our findings illustrate the evolutionary adaptation of an ancestral enzyme's active site to enable a novel catalytic mechanism that boosts SA production in Brassicaceae plants.
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