ArticleACS omega2018
Structural Insights from Molecular Dynamics Simulations of Tryptophan 7-Halogenase and Tryptophan 5-Halogenase.
Article in ACS omega, 2018. 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, 36 citations in OpenAlex.
- Discovery and Functional Characterization of SnFDHal, an Efficient Tryptophan 5-Halogenase from Streptomyces noursei.Applied biochemistry and biotechnology · 2026Article
- Crystallographic and Thermodynamic Evidence of Negative Coupling in the Flavin-Dependent Tryptophan Halogenases AbeH and BorH.ACS omega · 2025Article
- Natural Compound Dioscin Targeting Multiple Cancer Pathways through its High Affinity Binding to B Cell Lymphoma-2.Current computer-aided drug design · 2025Article
- Identifying and Engineering Flavin Dependent Halogenases for Selective Biocatalysis.Accounts of chemical research · 2024Article
- Discovery and substrate specificity engineering of nucleotide halogenases.Nature communications · 2024Article
- Asymmetric catalysis by flavin-dependent halogenases.Chirality · 2023Review
- 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
- Mechanism of Action of Flavin-Dependent Halogenases.ACS catalysis · 2022Article
- Expanding the Reactivity of Flavin Dependent Halogenases Toward Olefins via Enantioselective Intramolecular Haloetherification and Chemoenzymatic Oxidative Rearrangements.ACS catalysis · 2022Article
- 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
- Engineered RebH Halogenase Variants Demonstrating a Specificity Switch from Tryptophan towards Novel Indole Compounds.Chembiochem : a European journal of chemical biology · 2021Article
- Genomic Determinants Encode the Reactivity and Regioselectivity of Flavin-Dependent Halogenases in Bacterial Genomes and Metagenomes.mSystems · 2021Article
- AoiQ Catalyzes Geminal Dichlorination of 1,3-Diketone Natural Products.Journal of the American Chemical Society · 2021Article
- Closing the Gap: An Atomistic Structural and Functional Perspective of S. mansoni Universal Stress G4LZI3 Protein in Complex with Phenolic Compounds.Current drug discovery technologies · 2021Article
- Structure of apo flavin-dependent halogenase Xcc4156 hints at a reason for cofactor-soaking difficulties.Acta crystallographica. Section D, Structural biology · 2020Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Many natural organic compounds with pharmaceutical applications, including antibiotics (chlortetracycline and vancomycin), antifungal compounds (pyrrolnitrin), and chemotherapeutics (salinosporamide A and rebeccamycin) are chlorinated. Halogenating enzymes like tryptophan 7-halogenase (PrnA) and tryptophan 5-halogenase (PyrH) perform regioselective halogenation of tryptophan. In this study, the conformational dynamics of two flavin-dependent tryptophan halogenases-PrnA and PyrH-was investigated through molecular dynamics simulations, which are in agreement with the crystallographic and kinetic experimental studies of both enzymes and provide further explanation of the experimental data at an atomistic level of accuracy. They show that the binding sites of the cofactor-flavin adenine dinucleotide and the substrate do not come into close proximity during the simulations, thus supporting an enzymatic mechanism without a direct contact between them. Two catalytically important active site residues, glutamate (E346/E354) and lysine (K79/K75) in PrnA and PyrH, respectively, were found to play a key role in positioning the proposed chlorinating agent, hypochlorous acid. The changes in the regioselectivity between PrnA and PyrH arise as a consequence of differences in the orientation of substrate in its binding site.
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Registered trials
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