Journal
CHEMICAL SCIENCE
Volume 6, Issue 6, Pages 3454-3460Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5sc00913h
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Funding
- BBSRC [BB/K00199X/1, BB/I020764/1]
- GlaxoSmithKline
- CoEBio3
- Biotechnology and Biological Sciences Research Council [BB/K00199X/1, BB/M017702/1, BB/I020764/1] Funding Source: researchfish
- BBSRC [BB/M017702/1] Funding Source: UKRI
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Flavin-dependent halogenases are potentially valuable biocatalysts for the regioselective halogenation of aromatic compounds. These enzymes, utilising benign inorganic halides, offer potential advantages over traditional non-enzymatic halogenation chemistry that often lacks regiocontrol and requires deleterious reagents. Here we extend the biocatalytic repertoire of the tryptophan halogenases, demonstrating how these enzymes can halogenate a range of alternative aryl substrates. Using structure guided mutagenesis we also show that it is possible to alter the regioselectivity as well as increase the activity of the halogenases with non-native substrates including anthranilic acid; an important intermediate in the synthesis and biosynthesis of pharmaceuticals and other valuable products.
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