Functional characterization of prenyltransferases involved in de novo synthesis of isoprenoids in the leaf beetle Monolepta hieroglyphica

文献类型： 外文期刊

第一作者： Song, Xuan

作者： Song, Xuan;Yi, Chao-qun;Tang, Zi-yi;Dhiloo, Khalid Hussain;Zhang, Tian-tao;Liu, Wen-tao;Zhang, Yong-jun;Song, Xuan;Zhang, Yong-jun;Liu, Chang;Tang, Zi-yi;Dhiloo, Khalid Hussain;Liu, Wen-tao

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关键词： Farnesyl diphosphate synthase; Protein prenyltransferases; Enzyme catalysis; Molecular docking and kinetic analysis; Synthesis and transmission; Leaf beetle

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2024 年 280 卷

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收录情况： SCI

摘要： Prenyltransferases play a pivotal role in the isoprenoid biosynthesis and transfer in insects. In the current study, two classes of prenyltransferases (MhieFPPS1 and MhieFPPS2, MhiePFT-beta and MhiePF/GGT-alpha) were identified in the leaf beetle, Monolepta hieroglyphica. Phylogenetic analysis revealed that MhieFPPS1, MhieFPPS2, MhiePFT-beta and MhiePF/GGT-alpha were clustered in one clade with homologous in insects. Moreover, MhieFPPS2 lacked one aspartate-rich motif SARM. Molecular docking and kinetic analysis indicated that the (E)-GPP displayed higher affinity with MhieFPPS1 compared to DMAPP within the binding pocket containing metal binding sites (MG). The other class of prenyltransferases (MhiePFT-beta and MhiePF/GGT-alpha) lack the aspartate-rich motif. Docking results indicated that binding site of MhiePFT-beta involved divalent metal ions (Zn) and bound farnesyl or geranylgeranyl. In vitro, only recombiant MhieFPPS1 could catalyze the formation of (E)-farnesol against different combination of substrates, including IPP/DMAPP and IPP/(E)-GPP, highlighting the importance of SARM for enzyme activities. Kinetic analysis further indicated that MhiePFT-beta operated via Zn2+-dependent substrate binding, while MhiePF/GGT-alpha stabilized the beta-subunit during catalytic reaction. These findings contribute to a valuable insight in to understanding of the mechanisms involved in the biosynthesis and delivery of isoprenoid products in beetles.

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