Radical SAM Enzyme QmpB Installs Two 9-Membered Ring Sactionine Macrocycles during Biogenesis of a Ribosomal Peptide Natural Product
Radical SAM Enzyme QmpB Installs Two 9-Membered Ring Sactionine Macrocycles during Biogenesis of a Ribosomal Peptide Natural Product
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DOI：
10.1021/acs.joc.1c01507
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发表时间：
2021-08-05
影响因子：
3.6
通讯作者：
Seyedsayamdost, Mohammad R.
中科院分区：
文献类型：
--
作者：
Caruso, Alessio;Seyedsayamdost, Mohammad R.
我们报告的QmpB，一个新的自由基S-腺苷甲硫氨酸酶的核糖体肽天然产物基因簇编码的猪链球菌催化的反应。使用同位素标记，定点诱变，高分辨率质谱，和多维NMR光谱，我们表明，QmpB安装两个9元环sactionine桥，连接一个Cys残基与上游Asn通过一个a-硫醚桥，与两个大环分离的一个单一的残基。QmpB是迄今为止唯一表征的第二种II型sactionine合酶。
We report the reaction catalyzed by QmpB, a new radical S-adenosylmethionine enzyme encoded by a ribosomal peptide natural product gene cluster in Streptococcus suis. Using isotopic labeling, site-directed mutagenesis, high-resolution mass spectrometry, and multidimensional NMR spectroscopy, we show that QmpB installs two 9-membered ring sactionine bridges, connecting a Cys residue with an upstream Asn via an a-thioether bridge, with the two macrocycles separated by a single residue. QmpB is only the second type II sactionine synthase characterized to date.