欢迎访问云南西力生物技术股份有限公司!证券代码:871574
首页 成 果 源于西力产品的客户论文
FAD-Dependent Enzyme-Catalysed Intermolecular [4+2] Cycloaddition in Natural Product Biosynthesis. Nat. Chem., 2020, 12: 620–628.
发布时间:2020-10-23 阅读数:339 来源:Nat. Chem.
分享到:

Abstract:

The Diels-Alder reaction is one of the most powerful and widely used methods in synthetic chemistry for the stereospecific construction of carbon-carbon bonds. Despite the importance of Diels-Alder reactions in the biosynthesis of numerous secondary metabolites, no naturally occurring stand-alone Diels-Alderase has been demonstrated to catalyse intermolecular Diels-Alder transformations. Here we report a flavin adenine dinucleotide-dependent enzyme, Morus alba Diels-Alderase (MaDA), from Morus cell cultures, that catalyses an intermolecular [4+2] cycloaddition to produce the natural isoprenylated flavonoid chalcomoracin with a high efficiency and enantioselectivity. Density functional theory calculations and preliminary measurements of the kinetic isotope effects establish a concerted but asynchronous pericyclic pathway. Structure-guided mutagenesis and docking studies demonstrate the interactions of MaDA with the diene and dienophile to catalyse the [4+2] cycloaddition. MaDA exhibits a substrate promiscuity towards both dienes and dienophiles, which enables the expedient syntheses of structurally diverse natural products. We also report a biosynthetic intermediate probe (BIP)-based target identification strategy used to discover MaDA.



ewm.jpg 微信公众号
11.jpg 移动官网
特别声明:禁止在未经同意情况下转载本网站信息,BioBioPha品牌产品均由西力生物独家生产与销售,仅用于科学研究或企业研发!
版权所有 2019-2020 云南西力生物技术股份有限公司 BioBioPha 滇ICP备09000810号-1滇公安备案号 53019002000069号
技术支持:奥远科技

联系客服