ArticleChem catalysis2024
Expanding the repertoire of imine reductases by mining divergent biosynthetic pathways for promiscuous reactivity.
Article in Chem catalysis, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Data-driven construction of an imine reductase library capable of broad-scope reductive amination at equimolar substrate concentrations.Nature communications · 2026Article
- Stereoselective Biotransformation: Transfer of Learning to Advance Drug Metabolism and Biocatalysis.Angewandte Chemie (International ed. in English) · 2026Review
- Reprogramming Imine Reductases for Enantioselective Reduction of Electron-Rich Enamides.JACS Au · 2026Article
- Phase-Separated Multienzyme Condensates for Efficient Synthesis of Imines from Carboxylic Acids with Enhanced Dual-Cofactor Recycling.International journal of molecular sciences · 2025Article
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Authors and funding
2 authors.
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Abstract
Imine reductases (IREDs) are invaluable catalysts for enantioselective imine reduction and reductive amination of carbonyl compounds. Their synthetic versatility is, however, limited by their substrate scope, and new IREDs are needed. Current IREDs are closely related to the initially characterized enzymes, as their discovery has been driven by sequence homology searches. Here, we demonstrate a
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