ArticleACS catalysis2022
Efficient chemoenzymatic synthesis of α-aryl aldehydes as intermediates in C-C bond forming biocatalytic cascades.
Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 22 citations in OpenAlex.
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Phage-assisted continuous evolution of enzymes for noncanonical tyrosine biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Enhanced Stereochemical Analysis of β‑Diastereomeric Amino Acids with Variants of Marfey's Reagent.ACS omega · 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
- Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase.Nature chemistry · 2024Article
- Engineered Biocatalytic Synthesis of β-N-Substituted-α-Amino Acids.Angewandte Chemie (International ed. in English) · 2023Article
- Concise synthesis of (Chemical science · 2023Article
- Discovery of L-threonine transaldolases for enhanced biosynthesis of beta-hydroxylated amino acids.Communications biology · 2023Article
- Multiplexed Assessment of Promiscuous Non-Canonical Amino Acid Synthase Activity in a Pyridoxal Phosphate-Dependent Protein Family.ACS catalysis · 2023Article
- Engineering Enzyme Substrate Scope Complementarity for Promiscuous Cascade Synthesis of 1,2-Amino Alcohols.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Multi-enzyme biocatalytic cascades are emerging as practical routes for the synthesis of complex bioactive molecules. However, the relative sparsity of water-stable carbon electrophiles limits the synthetic complexity of molecules made from such cascades. Here, we develop a chemoenzymatic platform that leverages styrene oxide isomerase (SOI) to covert readily accessible aryl epoxides into α-aryl aldehydes through a Meinwald rearrangement. These unstable aldehyde intermediates are then intercepted with a C-C bond forming enzyme, ObiH, that catalyzes a transaldolase reaction with l-threonine to yield synthetically challenging β-hydroxy-α-amino acids. Co-expression of both enzymes in
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