Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities
Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities
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DOI：
10.1016/j.bmc.2008.07.052
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发表时间：
2008-09-01
影响因子：
3.5
通讯作者：
Kuzuyama, Tomohisa
中科院分区：
文献类型：
--
作者：
Kumano, Takuto;Richard, Stephane B.;Kuzuyama, Tomohisa
NphB是来自链霉菌属菌株CL 190的可溶性异戊二烯基转移酶，其在抗氧化剂萘的生物合成期间将香叶基连接至1，3，6，8-四羟基萘衍生的聚酮化合物。在这里，我们报告了多种化学酶促合成的各种异戊二烯化合物从芳香底物，包括黄酮类化合物使用两个异戊二烯转移酶NphB和SCO 7190，NphB同系物从天蓝色链霉菌A3（2），作为生物催化剂。NphB催化多种含羟基芳香族受体的碳-碳基和碳-氧基香叶基化。因此，这种使用异戊二烯基转移酶的简单方法可用于探索具有生物活性的新型异戊二烯化芳香族化合物。NphB的动力学研究表明，异戊烯化反应遵循顺序有序的机制。(C)2008爱思唯尔有限公司保留所有权利。
NphB is a soluble prenyltransferase from Streptomyces sp. strain CL190 that attaches a geranyl group to a 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during the biosynthesis of anti-oxidant naphterpin. Here we report multiple chemoenzymatic syntheses of various prenylated compounds from aromatic substrates including flavonoids using two prenyltransferases NphB and SCO7190, a NphB homolog from Streptomyces coelicolor A3( 2), as biocatalysts. NphB catalyzes carbon-carbon-based and carbon-oxygen-based geranylation of a diverse collection of hydroxyl-containing aromatic acceptors. Thus, this simple method using the prenyltransferases can be used to explore novel prenylated aromatic compounds with biological activities. Kinetic studies with NphB reveal that the prenylation reaction follows a sequential ordered mechanism. (C) 2008 Elsevier Ltd. All rights reserved.