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Issue Date
2021-10-14
Metadata
Show full item recordAbstract
Halogenation often improves the bioactive properties of natural products and is used in pharmaceutical research for the generation of new potential drug leads. High regio- and stereospecificity, simple reaction conditions and straightforward downstream processing are the main advantages of halogenation using enzymatic biocatalysts compared to chemical synthetic approaches. The identification of new promiscuous halogenases for the modification of various natural products is of great interest in modern drug discovery. In this paper, we report the identification of a new promiscuous FAD-dependent halogenase, DklH, from Frankia alni ACN14a. The identified halogenase readily modifies various flavonoid compounds, including those with well-studied biological activities. This halogenase has been demonstrated to modify not only flavones and isoflavones, but also flavonols, flavanones and flavanonols. The structural requirements for DklH substrate recognition were determined using a feeding approach. The homology model of DklH and the mechanism of substrate recognition are also proposed in this paper.Citation
Molecules. 2021 Oct 14;26(20):6220. doi: 10.3390/molecules26206220.Affiliation
HIPS, Helmholtz-Institut für Pharmazeutische Forschung Saarland, Universitätscampus E8.1 66123 Saarbrücken, Germany.Publisher
MDPIJournal
Molecules (Basel, Switzerland)PubMed ID
34684801Type
ArticleLanguage
enEISSN
1420-3049ae974a485f413a2113503eed53cd6c53
10.3390/molecules26206220
Scopus Count
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- Creative Commons