ArticleACS catalysis2024
Boron Designer Enzyme with a Hybrid Catalytic Dyad.
Article in ACS catalysis, 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.
- Using enantioselective biosensors to evolve asymmetric biocatalysts.Nature chemical biology · 2026Article
- Bioorthogonal Gold-Catalyzed Hydrothiolation Leading to Amide Bond Cleavage of Ethynylated Biarylbutanamide Precursors.Journal of the American Chemical Society · 2026Article
- Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026Article
- Article
- Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genetically encoded noncanonical amino acids can introduce new-to-nature activation modes into enzymes. While these amino acids can act as catalysts on their own due to their inherent chemical properties, interactions with adjacent residues in an enzyme, such as those present in natural catalytic dyads or triads, unlock a higher potential for designer enzymes. We incorporated a boron-containing amino acid into the protein scaffold RamR to create an active enzyme for the kinetic resolution of α-hydroxythioesters. We found that a closely positioned lysine residue is crucial for the catalytic activity of the designer enzyme by forming a hybrid catalytic dyad with the boronic acid residue. The enzyme is capable of resolving differently substituted α-hydroxythioesters with good selectivities. High-resolution mass spectrometry,
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Registered trials
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