A novel flavonoid prenyltransferase gene PcPT11 with broad substrate promiscuity in Psoralea corylifolia L.

文献类型： 外文期刊

第一作者： Wang, Yuanyue

作者： Wang, Yuanyue;Luo, Yanjiao;Zhang, Yixin;Xu, Chaoqun;Yao, Yu;Gu, Jiajun;Ding, Gang;Suo, Fengmei;Shen, Guoan;Guo, Baolin;Peng, Yude;Pang, Yongzhen;Jia, Shangang

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关键词： Psoralea corylifolia L; Prenyltransferases; Flavonoids; Prenylation; PcPT11

期刊名称：INDUSTRIAL CROPS AND PRODUCTS （ 影响因子：5.9； 五年影响因子：6.0 ）

ISSN： 0926-6690

年卷期： 2023 年 199 卷

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收录情况： SCI

摘要： Prenylated polyphenols have attracted a lot of interest because of their significant pharmacological activities. The chemoenzymatic synthesis of prenylated polyphenols using prenyltransferase (PT) has been regarded as a promising alternative to chemical synthesis or plant-based production. Psoralea corylifolia L. with abundance of diversified prenylated polyphenol compounds is an ideal material for the discovery of prenyltransferases available in synthetic biology. In this study, we investigated the transcriptomic data from P. corylifolia for pre-nyltransferases (PcPTs) involved in the biosynthesis of prenylated phenols. Among 11 PcPTs, our yeast expres-sion in vitro survey showed that PcPT11 was able to utilize 23 substrates, including 22 flavonoids and 1 coumarin, and was the one able to use the most substrates. PcPT11 acts in a highly regio-specific way to pre-nylate flavonoids at the C-6 position to produce compounds with important pharmacological effects such as corylifolinin, wighteone, and bavachin, which are the major ingredients in P. corylifolia. Finally, PcPT11 exhibited strong expression in fruits and leaves, and a GFP-PcPT11 fusion protein was shown to be localized in chloroplasts when expressed in Nicotiana benthamiana. Our study laid a foundation for understanding the biosynthetic pathway of prenylated flavonoids in P. corylifolia, and demonstrated that PcPT11 is a valuable enzyme to produce these pharmaceutically important prenylated polyphenols through biosynthetic approaches.

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