Radical S-Adenosylmethionine Protein NosN Forms the Side Ring System of Nosiheptide by Functionalizing the Polythiazolyl Peptide S-Conjugated lndolic Moiety
Radical S-Adenosylmethionine Protein NosN Forms the Side Ring System of Nosiheptide by Functionalizing the Polythiazolyl Peptide S-Conjugated lndolic Moiety
复制标题
自由基 S-腺苷甲硫氨酸蛋白 NosN 通过功能化聚噻唑基肽 S-共轭吲哚部分形成那西肽的侧环系统
DOI：
10.1021/acs.orglett.9b00293
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发表时间：
2019
期刊：
影响因子：
5.2
通讯作者：
Liu Wen
中科院分区：
文献类型：
--
作者：
Qiu Yanping;Du Yanan;Wang Shoufeng;Zhou Shuaixiang;Guo Yinlong;Liu Wen
NosN 是在双环硫肽那西肽的生物合成中观察到的自由基 S-腺苷甲硫氨酸蛋白。文章对 NosN 作用的时间、催化机制及其在侧环形成中的作用提供了见解。除了作为甲基转移酶之外，NosN 还通过功能化 S-共轭吲哚部分来转化聚噻唑基肽中间体，以选择性地构建 C1 单元，与硫肽框架形成酯键，并建立那西肽特异的侧环系统。
NosN is a radicalS-adenosylmethionine protein observed in the biosynthesis of the bicyclic thiopeptide nosiheptide. Insights are provided in terms of the timing of NosN action, its catalytic mechanism, and its role in side ring formation. Beyond being a methyltransferase, NosN transforms a polythiazolyl peptide intermediate by functionalizing theS-conjugated indolic moiety to selectively build a C1 unit, form an ester linkage to the thiopeptide framework, and establish the side ring system specific for nosiheptide.