Biochemical Characterization of a Eukaryotic Decalin-Forming Diels-Alderase.
Biochemical Characterization of a Eukaryotic Decalin-Forming Diels-Alderase.
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DOI：
10.1021/jacs.6b10452
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发表时间：
2016-12-14
影响因子：
15
通讯作者：
Tang Y
中科院分区：
文献类型：
--
作者：
Li L;Yu P;Tang MC;Zou Y;Gao SS;Hung YS;Zhao M;Watanabe K;Houk KN;Tang Y
分子内狄尔斯-阿尔德环加成反应形成的反式十氢化萘结构广泛存在于从真菌中分离的生物活性天然产物中。在这项工作中，我们阐明了细胞毒性菌丝体温热酶的简明三酶生物合成途径，并对催化无环底物形成反式十氢萘的狄尔斯-阿尔德酶（DAase）进行了生化表征。反应机制的计算研究合理化了酶的底物选择性和立体选择性。
The trans-decalin structure formed as a result of intramolecular Diels–Alder cycloaddition is widely present among bioactive natural products isolated from fungi. In this work, we elucidated the concise, three-enzyme biosynthetic pathway of the cytotoxic myceliothermophin and biochemically characterized the Diels–Alderase (DAase) that catalyzes formation of trans-decalin from an acyclic substrate. Computational studies on the reaction mechanisms rationalizes both the substrate- and stereoselectivity of the enzyme.