Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins |
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| Authors: | Sheng Huang Dr Jioji Tabudravu Somayah S Elsayed Jeanne Travert Doe Peace Ming Him Tong Dr Kwaku Kyeremeh Dr Sharon M Kelly Dr Laurent Trembleau Dr Rainer Ebel Prof?Dr Marcel Jaspars Dr Yi Yu Dr Hai Deng |
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| Institution: | 1. Key Laboratory of Combinatory Biosynthesis and Drug Discovery (Ministry of Education), School of Pharmaceutical Sciences, Wuhan University, 185 East Lake Road, Wuhan 430071 (P.R. China);2. Department of Chemistry, University of Aberdeen, Aberdeen (UK);3. Department of Chemistry, University of Ghana, P.O. Box LG56, Legon‐Accra (Ghana);4. Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, G12 8QQ (UK) |
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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. |
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| Keywords: | biosynthesis legonmycins multifunctional enzymes non‐ribosomal peptide synthetases pyrrolizidine alkaloids |
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