Discovery of a single monooxygenase that catalyzes carbamate formation and ring contraction in the biosynthesis of the legonmycins

Huang, S. et al. (2015) Discovery of a single monooxygenase that catalyzes carbamate formation and ring contraction in the biosynthesis of the legonmycins. Angewandte Chemie (International Edition), 54(43), pp. 12697-12701. (doi:10.1002/anie.201502902) (PMID:26206556)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Kelly, Dr Sharon
Authors: 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., and Deng, H.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Angewandte Chemie (International Edition)
Publisher:Wiley - V C H Verlag GmbH & Co. KGaA
ISSN:1433-7851
ISSN (Online):1521-3773

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