ArticleScientific reports2020
Significant improvement in catalytic activity and enantioselectivity of a Phaseolus vulgaris epoxide hydrolase, PvEH3, towards ortho-cresyl glycidyl ether based on the semi-rational design.
Article in Scientific reports, 2020. 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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Who cites it
5 citing papers in PubMed.
- Photoenzymatic Decarboxylation to Produce Hydrocarbon Fuels: A Critical Review.Molecular biotechnology · 2025Review
- Improving Hydrolytic Activity and Enantioselectivity of Epoxide Hydrolase fromMolecules (Basel, Switzerland) · 2024Article
- Gut microbiome-derived hydrolases-an underrated target of natural product metabolism.Frontiers in cellular and infection microbiology · 2024Review
- Structure-function relationship between soluble epoxide hydrolases structure and their tunnel network.Computational and structural biotechnology journal · 2022Article
- Machine Learning Enables Selection of Epistatic Enzyme Mutants for Stability Against Unfolding and Detrimental Aggregation.Chembiochem : a European journal of chemical biology · 2021Article
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8 authors.
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Abstract
The investigation of substrate spectrum towards five racemic (rac-) aryl glycidyl ethers (1a-5a) indicated that E. coli/pveh3, an E. coli BL21(DE3) transformant harboring a PvEH3-encoding gene pveh3, showed the highest EH activity and enantiomeric ratio (E) towards rac-3a. For efficiently catalyzing the kinetic resolution of rac-3a, the activity and E value of PvEH3 were further improved by site-directed mutagenesis of selected residues. Based on the semi-rational design of an NC-loop in PvEH3, four single-site variants of pveh3 were amplified by PCR, and intracellularly expressed in E. coli BL21(DE3), respectively. E. coli/pveh3
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