ArticleChembiochem : a European journal of chemical biology2021
Engineered RebH Halogenase Variants Demonstrating a Specificity Switch from Tryptophan towards Novel Indole Compounds.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Continuous evolution of a halogenase enzyme with improved solubility and activity for sustainable bioproduction.Nature communications · 2026Article
- Metagenomic Identification of Brominated Indole Biosynthetic Machinery from Cyanobacteria.Journal of natural products · 2025Article
- Crystallographic and Thermodynamic Evidence of Negative Coupling in the Flavin-Dependent Tryptophan Halogenases AbeH and BorH.ACS omega · 2025Article
- Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC.Communications chemistry · 2024Article
- Indole and azaindole halogenation catalyzed by the RebH enzyme variant 3-LSR utilizing co-purifiedFrontiers in bioengineering and biotechnology · 2022Article
- Engineered RebH Halogenase Variants Demonstrating a Specificity Switch from Tryptophan towards Novel Indole Compounds.Chembiochem : a European journal of chemical biology · 2021Article
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9 authors.
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Abstract
Activating industrially important aromatic hydrocarbons by installing halogen atoms is extremely important in organic synthesis and often improves the pharmacological properties of drug molecules. To this end, tryptophan halogenase enzymes are potentially valuable tools for regioselective halogenation of arenes, including various industrially important indole derivatives and similar scaffolds. Although endogenous enzymes show reasonable substrate scope towards indole compounds, their efficacy can often be improved by engineering. Using a structure-guided semi-rational mutagenesis approach, we have developed two RebH variants with expanded biocatalytic repertoires that can efficiently halogenate several novel indole substrates and produce important pharmaceutical intermediates. Interestingly, the engineered enzymes are completely inactive towards their natural substrate tryptophan in spite of their high tolerance to various functional groups in the indole ring. Computational modelling and molecular dynamics simulations provide mechanistic insights into the role of gatekeeper residues in the substrate binding site and the dramatic switch in substrate specificity when these are mutated.
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