ArticleNature chemistry2024
Biocatalytic asymmetric aldol addition into unactivated ketones.
Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Catalytically Promiscuous PLP-Dependent Aminotransferases Are Biocatalysts for C-C Bond Formation.ACS central science · 2026Article
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Stereoretentive decarbonylative C(spNature · 2026Article
- Pyridoxal 5'-Phosphate-Dependent Enzymatic Decarboxylative Annulation.Journal of the American Chemical Society · 2026Article
- Biocatalytic Regioselective C-Formylation of Resorcinol Derivatives.Angewandte Chemie (International ed. in English) · 2026Article
- Biocatalytic Synthesis of N-Protected α-Amino Acids through 1,3-Nitrogen Migration by Nonheme Iron Enzymes.Journal of the American Chemical Society · 2025Article
- Mechanistic and Structural Analyses of Non-Heme Iron Enzyme TqaM for α-Tertiary Amino Acid Synthesis.Journal of the American Chemical Society · 2025Article
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 2025Article
- Cofactor-independent photo-enzymatic reductions with water mediated by reductive graphene quantum dots.Nature communications · 2025Article
- Article
- Profiling of Diverse Pyridoxal-5'-Phosphate Dependent Enzymes Reveals Promiscuous Aldolase Activity with (2-Azaaryl)methanamines.Journal of the American Chemical Society · 2025Article
- Nucleophilic α-Functionalization of Benzyl Amines Using an Engineered Threonine Aldolase.Journal of the American Chemical Society · 2025Article
- Diversity of ThDP-Dependent Enzymes Forming Chiral Tertiary Alcohols.Chembiochem : a European journal of chemical biology · 2025Review
- Engineering of the Thiamine Diphosphate-Dependent JanthE for the Synthesis of Tertiary Alcohols.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Promiscuity Guided Evolution of Decarboxylative Aldolases for Synthesis of Tertiary γ-Hydroxy Amino Acids.Angewandte Chemie (International ed. in English) · 2025Article
- Chemoenzymatic Cascade Synthesis of Metal-ChelatingChemCatChem · 2025Article
- Occupational modulation in the (3+1)-dimensional incommensurate structure of (2S,3S)-2-amino-3-hydroxy-3-methyl-4-phenoxybutanoic acid dihydrate.Acta crystallographica. Section C, Structural chemistry · 2024Article
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10 authors.
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Abstract
Enzymes are renowned for their catalytic efficiency and selectivity, but many classical transformations in organic synthesis have no biocatalytic counterpart. Aldolases are prodigious C-C bond-forming enzymes, but their reactivity has only been extended past activated carbonyl electrophiles in special cases. To probe the mechanistic origins of this limitation, we use a pair of aldolases whose activity is dependent on pyridoxal phosphate. Our results reveal how aldolases are limited by kinetically favourable proton transfer with solvent, which undermines aldol addition into ketones. We show how a transaldolase can circumvent this limitation, enabling efficient addition into unactivated ketones. The resulting products are highly sought non-canonical amino acids with side chains that contain chiral tertiary alcohols. Mechanistic analysis reveals that transaldolase activity is an intrinsic feature of pyridoxal phosphate chemistry and identifies principles for extending aldolase catalysis beyond its previous limits to enable convergent, enantioselective C-C bond formation from simple starting materials.
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