ArticleChembiochem : a European journal of chemical biology2017
Aromatic Halogenation by Using Bifunctional Flavin Reductase-Halogenase Fusion Enzymes.
Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 48 citations in OpenAlex.
- Total Synthesis of Allocyclinone A via Late-Stage Halogen Swapping.Angewandte Chemie (International ed. in English) · 2026Article
- Engineering fusion enzymes for enhanced catalysis and stability: strategies and biotechnological applications.Molecular biology reports · 2026Review
- Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Nature communications · 2026Article
- Identifying and Engineering Flavin Dependent Halogenases for Selective Biocatalysis.Accounts of chemical research · 2024Article
- Functional characterization of a novel flavin reductase from a deep-sea sediment metagenomic library and its application for indirubin production.Applied and environmental microbiology · 2024Article
- Fermentative aminopyrrolnitrin production by metabolically engineered Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Developing and enhancing promiscuous activity for NAD(P)H-dependent flavin reductase via elimination of cofactor.Heliyon · 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
- From Tryptophan to Toxin: Nature's Convergent Biosynthetic Strategy to Aetokthonotoxin.Journal of the American Chemical Society · 2022Article
- Design of fusion enzymes for biocatalytic applications in aqueous and non-aqueous media.Frontiers in bioengineering and biotechnology · 2022Review
- Indole and azaindole halogenation catalyzed by the RebH enzyme variant 3-LSR utilizing co-purifiedFrontiers in bioengineering and biotechnology · 2022Article
- A Promiscuous Halogenase for the Derivatization of Flavonoids.Molecules (Basel, Switzerland) · 2021Article
- Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Review
- Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021Review
- Production of Tyrian purple indigoid dye from tryptophan in Escherichia coli.Nature chemical biology · 2021Article
- Flavin Adenine Dinucleotide-Dependent Halogenase XanH and Engineering of Multifunctional Fusion Halogenases.Applied and environmental microbiology · 2020Article
- Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds.Frontiers in bioengineering and biotechnology · 2020Review
- Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes.Chembiochem : a European journal of chemical biology · 2019Review
- Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities.Biology · 2018Review
- Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis.Annual review of biochemistry · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The remarkable site selectivity and broad substrate scope of flavin-dependent halogenases (FDHs) has led to much interest in their potential as biocatalysts. Multiple engineering efforts have demonstrated that FDHs can be tuned for non-native substrate scope and site selectivity. FDHs have also proven useful as in vivo biocatalysts and have been successfully incorporated into biosynthetic pathways to build new chlorinated aromatic compounds in several heterologous organisms. In both cases, reduced flavin cofactor, usually supplied by a separate flavin reductase (FR), is required. Herein, we report functional synthetic, fused FDH-FR proteins containing various FDHs and FRs joined by different linkers. We show that FDH-FR fusion proteins can increase product titers compared to the individual components for in vivo biocatalysis in Escherichia coli.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.