ArticleNature communications2024
Unlocking the function promiscuity of old yellow enzyme to catalyze asymmetric Morita-Baylis-Hillman reaction.
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 5 papers.
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Who cites it
5 citing papers in PubMed.
- A programmable bifunctional flavoenzyme for direct amine-to-ester conversion.Science advances · 2026Article
- Propellane Alkaloid Biosynthesis and Total Synthesis via Interrupted Reaction Pathways.ACS central science · 2026Article
- Nature-Inspired Enzymatic Cascades: Emerging Strategies for Sustainable Chemistry.Molecules (Basel, Switzerland) · 2026Review
- Biocatalytic reduction of nitro-sulfonamides: enzyme engineering, process integration, and sustainable pathways toFrontiers in bioengineering and biotechnology · 2026Review
- Reinvestigation of theJournal of the American Chemical Society · 2025Article
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Authors and funding
16 authors.
Funding
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Abstract
Exploring the promiscuity of native enzymes presents a promising strategy for expanding their synthetic applications, particularly for catalyzing challenging reactions in non-native contexts. In this study, we explore the promiscuous potential of old yellow enzymes (OYEs) to facilitate the Morita-Baylis-Hillman reaction (MBH reaction), leveraging substrate similarities between MBH reaction and reduction reaction. Using mass spectrometry and spectroscopic techniques, we confirm promiscuity of GkOYE in both MBH and reduction reactions. By blocking H
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