ArticleThe Journal of biological chemistry2024
Deciphering the stereo-specific catalytic mechanisms of cis-epoxysuccinate hydrolases producing L(+)-tartaric acid.
Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 6 citations in OpenAlex.
- Reprogramming product selectivity and activity in promiscuous terpene synthases via substrate conformation engineering.Nature communications · 2026Article
- Fed-batch strategies for the enhanced biotransformation of cis-epoxysuccinate to L-( +)-tartrate.Bioresources and bioprocessing · 2026Article
- Designing Molecular Solar Thermal Systems Based on the Paternò-Büchi Reaction Coupled to Enzymatic Energy Release.ChemSusChem · 2025Article
- Essential amino acid residues and catalytic mechanism of trans-epoxysuccinate hydrolase for production of meso-tartaric acid.Biotechnology letters · 2024Article
- High-yield production of 5-keto-D-gluconic acid via regulated fermentation strategy ofHeliyon · 2024Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microbial epoxide hydrolases, cis-epoxysuccinate hydrolases (CESHs), have been utilized for commercial production of enantiomerically pure L(+)- and D(-)-tartaric acids for decades. However, the stereo-catalytic mechanism of CESH producing L(+)-tartaric acid (CESH[L]) remains unclear. Herein, the crystal structures of two CESH[L]s in ligand-free, product-complexed, and catalytic intermediate forms were determined. These structures revealed the unique specific binding mode for the mirror-symmetric substrate, an active catalytic triad consisting of Asp-His-Glu, and an arginine providing a proton to the oxirane oxygen to facilitate the epoxide ring-opening reaction, which has been pursued for decades. These results provide the structural basis for the rational engineering of these industrial biocatalysts.
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