ArticleACS catalysis2017
Understanding Flavin-Dependent Halogenase Reactivity via Substrate Activity Profiling.
Article in ACS catalysis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed.
- Promiscuity-Guided Enzyme Evolution via Substrate Multiplexed Screening.Angewandte Chemie (International ed. in English) · 2026Review
- Systematic discovery of enzyme promiscuity in Escherichia coli using in vitro metabolomics.Communications biology · 2026Article
- Flavin-dependent monooxygenases as versatile biocatalysts in biomanufacturing: mechanisms, engineering, and applications.Biotechnology for biofuels and bioproducts · 2026Review
- Structural Basis of Regioselective Bromination of Tricyclic Tryptoline by the Tryptophan Halogenase Thal.Chembiochem : a European journal of chemical biology · 2025Article
- Crystallographic and Thermodynamic Evidence of Negative Coupling in the Flavin-Dependent Tryptophan Halogenases AbeH and BorH.ACS omega · 2025Article
- Identifying and Engineering Flavin Dependent Halogenases for Selective Biocatalysis.Accounts of chemical research · 2024Article
- Fitness landscape of substrate-adaptive mutations in evolved amino acid-polyamine-organocation transporters.eLife · 2024Article
- Descriptor-augmented machine learning for enzyme-chemical interaction predictions.Synthetic and systems biotechnology · 2024Article
- Selective C-H Halogenation of Alkenes and Alkynes Using Flavin-Dependent Halogenases.Angewandte Chemie (International ed. in English) · 2024Article
- Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC.Communications chemistry · 2024Article
- Non-Native Site-Selective Enzyme Catalysis.Chemical reviews · 2023Review
- Asymmetric catalysis by flavin-dependent halogenases.Chirality · 2023Review
- Qualitative metabolomics-based characterization of a phenolic UDP-xylosyltransferase with a broad substrate spectrum fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Further Characterization of Fungal Halogenase RadH and Its Homologs.Biomolecules · 2023Article
- How to Recruit a Promiscuous Enzyme to Serve a New Function.Biochemistry · 2023Article
- The Single-Component Flavin Reductase/Flavin-Dependent Halogenase AetF is a Versatile Catalyst for Selective Bromination and Iodination of Arenes and Olefins.Angewandte Chemie (International ed. in English) · 2022Article
- Adaptive evolvability through direct selection instead of indirect, second-order selection.Journal of experimental zoology. Part B, Molecular and developmental evolution · 2022Review
- Analysis of Laboratory-Evolved Flavin-Dependent Halogenases Affords a Computational Model for Predicting Halogenase Site Selectivity.Chem catalysis · 2022Article
- Directed Evolution of Flavin-Dependent Halogenases for Site- and Atroposelective Halogenation of 3-Aryl-4(3Journal of the American Chemical Society · 2022Article
- Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis.Nature communications · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
The activity of four native FDHs and four engineered FDH variants on 93 low molecular weight arenes was used to generate FDH substrate activity profiles. These profiles provided insights into how substrate class, functional group substitution, electronic activation, and binding impact FDH activity and selectivity. The enzymes studied could halogenate a far greater range of substrates than previously recognized, but significant differences in their substrate specificity and selectivity were observed. Trends between the electronic activation of each site on a substrate and halogenation conversion at that site were established, and these data, combined with docking simulations, suggest that substrate binding can override electronic activation even on compounds differing appreciably from native substrates. These findings provide a useful framework for understanding and exploiting FDH reactivity for organic synthesis.
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