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

Huang, Sheng and Tabudravu, Jioji N. and Elsayed, Somayah Sameer and Travert, Jeanne and Peace, Doe and Tong, Ming Him and Kyeremeh, Kwaku and Kelly, Sharon M. and Trembleau, Laurent and Ebel, Rainer and Jaspars, Marcel and Yu, Yi and Deng, Hai (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. ISSN 1521-3773

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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: Journal Article
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science, Technology and Environment (FSTE) > School of Biological and Chemical Sciences
Depositing User: Fulori Nainoca
Date Deposited: 17 May 2017 16:33
Last Modified: 04 Jul 2017 09:52
URI: http://repository.usp.ac.fj/id/eprint/9896
UNSPECIFIED

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