Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins
Discovery of a Single Monooxygenase that Catalyzes Carbamate Formation and Ring Contraction in the Biosynthesis of the Legonmycins
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DOI：
10.1002/anie.201502902
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发表时间：
2015-10-19
影响因子：
16.6
通讯作者：
Deng, Hai
中科院分区：
文献类型：
--
作者：
Huang, Sheng;Tabudravu, Jioji;Deng, Hai
吡咯里西啶生物碱是一类具有重要生物活性的天然产物。现在描述多功能FAD依赖性酶LgnC的发现和表征。该酶显示通过不寻常的环膨胀/收缩机制将吲哚里西啶中间体转化为吡咯里西啶，并催化新的细菌PA（所谓的legonmycins）的生物合成。通过基因组驱动的分析，异源表达和基因失活，也表明legonmycins来源于非核糖体肽合成酶（NRPS）。因此，首次公开了细菌PA的生物合成来源。
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.