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The chloroalkaloid (−)-acutumine is biosynthesized via a Fe(II)- and 2-oxoglutarate-dependent halogenase in Menispermaceae plants

Author

Listed:
  • Colin Y. Kim

    (Whitehead Institute for Biomedical Research
    Massachusetts Institute of Technology)

  • Andrew J. Mitchell

    (Whitehead Institute for Biomedical Research)

  • Christopher M. Glinkerman

    (Whitehead Institute for Biomedical Research)

  • Fu-Shuang Li

    (Whitehead Institute for Biomedical Research)

  • Tomáš Pluskal

    (Whitehead Institute for Biomedical Research)

  • Jing-Ke Weng

    (Whitehead Institute for Biomedical Research
    Massachusetts Institute of Technology)

Abstract

Plant halogenated natural products are rare and harbor various interesting bioactivities, yet the biochemical basis for the involved halogenation chemistry is unknown. While a handful of Fe(II)- and 2-oxoglutarate-dependent halogenases (2ODHs) have been found to catalyze regioselective halogenation of unactivated C–H bonds in bacteria, they remain uncharacterized in the plant kingdom. Here, we report the discovery of dechloroacutumine halogenase (DAH) from Menispermaceae plants known to produce the tetracyclic chloroalkaloid (−)-acutumine. DAH is a 2ODH of plant origin and catalyzes the terminal chlorination step in the biosynthesis of (−)-acutumine. Phylogenetic analyses reveal that DAH evolved independently in Menispermaceae plants and in bacteria, illustrating an exemplary case of parallel evolution in specialized metabolism across domains of life. We show that at the presence of azide anion, DAH also exhibits promiscuous azidation activity against dechloroacutumine. This study opens avenues for expanding plant chemodiversity through halogenation and azidation biochemistry.

Suggested Citation

  • Colin Y. Kim & Andrew J. Mitchell & Christopher M. Glinkerman & Fu-Shuang Li & Tomáš Pluskal & Jing-Ke Weng, 2020. "The chloroalkaloid (−)-acutumine is biosynthesized via a Fe(II)- and 2-oxoglutarate-dependent halogenase in Menispermaceae plants," Nature Communications, Nature, vol. 11(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15777-w
    DOI: 10.1038/s41467-020-15777-w
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