ORIGINAL RESEARCH article
Front. Plant Sci.
Sec. Plant Metabolism and Chemodiversity
This article is part of the Research TopicPlant Natural Products: Biosynthesis, Regulation, and Function, Volume IIView all 4 articles
Systematic characterization and functional analysis of trans-prenyltransferases in Curcuma wenyujin
Provisionally accepted
Qian Wang
Yi SuTingyu YeShiyi WuHuan LiuJingwen SunXiu YinTianyuan Hu
Ma XiaoxiaShujuan Zhao
Xiaopu Yin*
Qiuhui Wei*- Hangzhou Normal University, Hangzhou, China
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Curcuma wenyujin (Zingiberaceae), a medicinally significant species within the Curcuma genus, is highly regarded in traditional Chinese medicine for its rich terpenoid constituents. These specialized metabolites serve as the principal bioactive components underpinning the plant's therapeutic effects. As key enzymes in terpenoid biosynthesis, trans-prenyltransferases (trans-PTs) play crucial roles in regulating metabolic flux. However, a systematic characterization of the trans-PT family members and their catalytic specificities has yet to be achieved in C. wenyujin. Through a comprehensive transcriptome-wide analysis, eight trans-PT homologs (CwPTs) were identified. Phylogenetic classification revealed that five CwPTs function as geranylgeranyl pyrophosphate synthases (GGPS), two as solanesyl pyrophosphate synthases (SPS), and one as farnesyl pyrophosphate synthase (FPS). The expression profile assay showed more significant changes in the transcription levels of CwPTs in response to abscisic acid (ABA) and methyl jasmonate (MeJA) than to gibberellic acid (GA). Functional validation indicated that purified recombinant enzyme of CwFPS1 catalyzed the biosynthesis of farnesyl pyrophosphate (FPP) through the sequential condensation of dimethylallyl pyrophosphate (DMAPP) and isopentenyl pyrophosphate (IPP), as well as geranyl pyrophosphate (GPP) and IPP in vitro. Purified recombinant enzyme of CwGGPS1 catalyzed the condensation of GPP or FPP with IPP to generate geranylgeranyl pyrophosphate (GGPP). Furthermore, the catalytic function of CwFPS1 and CwGGPS1 was confirmed in Escherichia coli. Our research establishes a molecular foundation for understanding terpenoid biosynthesis in C. wenyujin.
Keywords: trans-prenyltransferases (trans-PTs), Curcuma wenyujin, Geranylgeranyl pyrophosphate synthase (GGPS), Farnesyl pyrophosphate synthase (FPS), Catalytic function
Received: 25 Sep 2025; Accepted: 31 Oct 2025.
Copyright: © 2025 Wang, Su, Ye, Wu, Liu, Sun, Yin, Hu, Xiaoxia, Zhao, Yin and Wei. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Xiaopu Yin, yinxp@hznu.edu.cn
Qiuhui Wei, wqh_268@163.com
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