ArticleNature chemistry2022
Engineering an efficient and enantioselective enzyme for the Morita-Baylis-Hillman reaction.
Article in Nature chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 104 citations in OpenAlex.
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- PCA-Based Database Mining Enables the Discovery of Bacterial Carbene Transferases for Stereodivergent Cyclopropanation.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering LmrR protein for L-proline-based asymmetric aldol biocatalysis.Nature communications · 2026Article
- Attractive Noncovalent Interactions versus Steric Confinement in Asymmetric Supramolecular Catalysis.Journal of the American Chemical Society · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
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- Active site diversification of a non-canonical amino acid decarboxylase by merging substrate multiplexed screening with computationally guided recombination.Protein science : a publication of the Protein Society · 2025Article
- Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release.Nature communications · 2025Article
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- Nanosecond-scale single-molecule reaction dynamics for scalable synthesis on a chip.National science review · 2025Article
- Highly selective aldehyde coupling on the heterointerface of molybdenum selenide and graphdiyne.Science advances · 2025Article
- Reinvestigation of theJournal of the American Chemical Society · 2025Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
- Targeted TPS Shooting Using Computer Vision to Generate Ensemble of Trajectories.Journal of chemical theory and computation · 2025Article
- Promiscuity Guided Evolution of Decarboxylative Aldolases for Synthesis of Tertiary γ-Hydroxy Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- Rational engineering of a thermostable α-oxoamine synthase biocatalyst expands the substrate scope and synthetic applicability.Communications chemistry · 2025Article
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9 authors at 2 institutions in 2 countries.
Funding
Abstract
The combination of computational design and directed evolution could offer a general strategy to create enzymes with new functions. So far, this approach has delivered enzymes for a handful of model reactions. Here we show that new catalytic mechanisms can be engineered into proteins to accelerate more challenging chemical transformations. Evolutionary optimization of a primitive design afforded an efficient and enantioselective enzyme (BH32.14) for the Morita-Baylis-Hillman (MBH) reaction. BH32.14 is suitable for preparative-scale transformations, accepts a broad range of aldehyde and enone coupling partners and is able to promote selective monofunctionalizations of dialdehydes. Crystallographic, biochemical and computational studies reveal that BH32.14 operates via a sophisticated catalytic mechanism comprising a His23 nucleophile paired with a judiciously positioned Arg124. This catalytic arginine shuttles between conformational states to stabilize multiple oxyanion intermediates and serves as a genetically encoded surrogate of privileged bidentate hydrogen-bonding catalysts (for example, thioureas). This study demonstrates that elaborate catalytic devices can be built from scratch to promote demanding multi-step processes not observed in nature.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.