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

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dc.contributor.authorHuang, S.
dc.contributor.authorTabudravu, J.
dc.contributor.authorElsayed, S.S.
dc.contributor.authorTravert, J.
dc.contributor.authorPeace, D.
dc.contributor.authorTong, M.H.
dc.contributor.authorKyeremeh, K.
dc.contributor.authorKelly, S.M.
dc.contributor.authorTrembleau, L.
dc.contributor.authorEbel, R.
dc.contributor.authorJaspars, M.
dc.contributor.authorYu, Y.
dc.contributor.authorDeng, H.
dc.date.accessioned2018-09-11T10:48:15Z
dc.date.available2018-09-11T10:48:15Z
dc.date.issued2015-07
dc.description.abstractPyrrolizidine 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.en_US
dc.identifier.otherVolume 54, Issue 43,Pages 12697-12701
dc.identifier.otherhttps://doi.org/10.1002/anie.201502902
dc.identifier.urihttp://ugspace.ug.edu.gh/handle/123456789/24051
dc.language.isoenen_US
dc.publisherAngewandte Chemie International Editionen_US
dc.subjectbiosynthesisen_US
dc.subjectlegonmycinsen_US
dc.subjectmultifunctional enzymesen_US
dc.subjectnon-ribosomal peptide synthetasesen_US
dc.subjectpyrrolizidine alkaloidsen_US
dc.titleDiscovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins.en_US
dc.typeArticleen_US

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