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. 2019 Oct 31;9(1):175.
doi: 10.1186/s13568-019-0898-y.

XszenFHal, a novel tryptophan 5-halogenase from Xenorhabdus szentirmaii

Jérémy Domergue  1 , Diane Erdmann  1 , Aurélie Fossey-Jouenne  1 , Jean-Louis Petit  1 , Adrien Debard  1 , Véronique de Berardinis  1 , Carine Vergne-Vaxelaire  1 , Anne Zaparucha  2
Affiliations

XszenFHal, a novel tryptophan 5-halogenase from Xenorhabdus szentirmaii

Jérémy Domergue et al. AMB Express. .

Abstract

Flavin-dependent halogenases (FHals) catalyse the halogenation of electron-rich substrates, mainly aromatics. Halogenated compounds have many applications, as pharmaceutical, agrochemicals or as starting materials for the synthesis of complex molecules. By exploring the sequenced bacterial diversity, we discovered and characterized XszenFHal, a novel FHal from Xenorhabdus szentirmaii, a symbiotic bacterium of entomopathogenic nematode. The substrate scope of XszenFHal was examined and revealed activities towards tryptophan, indole and indole derivatives, leading to the formation of the corresponding 5-chloro products. XszenFHal makes a valuable addition to the panel of flavin-dependent halogenases already discovered and enriches the potential for biotechnology applications by allowing access to 5-halogenated indole derivatives.

Keywords: Biocatalysis; Electrophilic halogenation; Flavin-dependent halogenases; Indole derivatives; Regioselectivity.

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Conflict of interest statement

The authors declare that they have no competing interests.

Figures

Fig. 1
Fig. 1
Substrate structures
Scheme 1
Scheme 1
Chlorination of l-tryptophan catalyzed by XszenFHal
Fig. 2
Fig. 2
a d- and l-tryptophan conversions by XszenFHal with NaCl over 24 h. b Time course of l-tryptophan conversion by XszenFHal with NaCl over 24 h
See this image and copyright information in PMC

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