Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins

Sheng Huang, Jioji Tabudravu, Somayah S. Elsayed, Jeanne Travert, Doe Peace, Ming Him Tong, Kwaku Kyeremeh, Sharon M. Kelly, Laurent Trembleau, Rainer Ebel, Marcel Jaspars, Yi Yu* (Corresponding Author), Hai Deng* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)
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Abstract

Pyrrolizidine alkaloids (PAs) are a group of natural products with important biological activities. The discovery and characterization of the multifunctional FAD‐dependent enzyme LgnC is now described. The enzyme is shown to convert indolizidine intermediates into pyrrolizidines through an unusual ring expansion/contraction mechanism, and catalyze the biosynthesis of new bacterial PAs, the so‐called legonmycins. By genome‐driven analysis, heterologous expression, and gene inactivation, the legonmycins were also shown to originate from non‐ribosomal peptide synthetases (NRPSs). The biosynthetic origin of bacterial PAs has thus been disclosed for the first time.
Original languageEnglish
Pages (from-to)12697-12701
Number of pages5
JournalAngewandte Chemie International Edition
Volume54
Issue number43
Early online date17 Jul 2015
DOIs
Publication statusPublished - 19 Oct 2015

Keywords

  • biosynthesis
  • legonmycins
  • multifunctional enzymes
  • non-ribosomal peptide synthetases
  • pyrrolizidine alkaloids

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