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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., (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

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. [ABSTRACT FROM AUTHOR]

The multifunctional Baeyer–Villiger enzyme LgnC catalyzes the transformation of indolizidines into pyrrolizidines by carbamate formation, hydrolysis, decarboxylation‐driven ring contraction, and hydroxylation. In their Communication on page 12697 ff., H. Deng, Y. Yu et al. show that these are the crucial steps for the biosynthesis of the legonmycins, new bacterial pyrrolizidine alkaloids named after their association with Legon, Ghana. [ABSTRACT FROM AUTHOR]