ArticleJournal of the American Chemical Society2025
Nucleophilic α-Functionalization of Benzyl Amines Using an Engineered Threonine Aldolase.
Article in Journal of the American Chemical Society, 2025. 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.
- Article
- A pyridoxal phosphate-dependent enzyme platform for stereoselective synthesis of γ-tertiary-nitro-noncanonical amino acids.Nature communications · 2026Article
- α-C-H Functionalization of Benzylamines: A Crucial Yet Challenging Transformation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Chiral amines are ubiquitous in pharmaceuticals and agrochemicals, making their efficient and selective synthesis a significant synthetic challenge. Threonine aldolases synthesize chiral amines via stereoselective C-C bond formation; however, they are restricted to small amino acids as pro-nucleophiles, limiting their utility in chemical synthesis. Here, we report an engineered threonine aldolase capable of α-functionalizing benzylamines. The evolved enzyme has excellent catalytic efficiency and accepts a broad range of (heterocyclic)benzyl amines and structurally diverse aldehydes to yield single-enantiomers of 1,2-amino alcohols in high-yield and diastereoselectivity. Mechanistic and crystallographic studies provide a rationale for how these mutations enable this previously unknown function. Moreover, beneficial mutations can be transferred to a related pyridoxal-dependent protein, highlighting the generality of these insights.
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Registered trials
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