Browsing by Author "Trembleau, L."
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Item Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins.(Angewandte Chemie International Edition, 2015-07) Huang, S.; Tabudravu, J.; Elsayed, S.S.; Travert, J.; Peace, D.; Tong, M.H.; Kyeremeh, K.; Kelly, S.M.; Trembleau, L.; Ebel, R.; Jaspars, M.; Yu, Y.; Deng, H.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.Item Enzymatic Reconstitution and Biosynthetic Investigation of the Bacterial Carbazole Neocarazostatin A(The Journal of Organic Chemistry, 2019-11-15) Kyeremeh, K.; Liu, Y.; Su, L.; Fang, Q.; Tabudravu, J.; Yang, X.; Rickaby, K.; Trembleau, L.; Deng, Z.; Deng, H.; Yu, Y.Tricyclic carbazole is an important scaffold in many naturally occurring metabolites, as well as valuable building blocks. Here we report the reconstitution of the ring A formation of the bacterial neocarazostatin A carbazole metabolite. We provide evidence of the involvement of two unusual aromatic polyketide proteins. This finding suggests how new enzymatic activities can be recruited to specific pathways to expand biosynthetic capacities. Finally, we leveraged our bioinformatics survey to identify the untapped capacity of carbazole biosynthesis