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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

作者： Song, Xuan 1 ; Liu, Chang 3 ; Yi, Chao-qun 1 ; Tang, Zi-yi 1 ; Dhiloo, Khalid Hussain 1 ; Zhang, Tian-tao 1 ; Liu, Wen-tao 1 ; Zhang, Yong-jun 1 ;

作者机构： 1.Chinese Acad Agr Sci, State Key Lab Biol Plant Dis & Insect Pests, Inst Plant Protect, Beijing 100193, Peoples R China

2.Chinese Acad Agr Sci, Zhongyuan Res Ctr, Xinxiang 453500, Peoples R China

3.Ningxia Acad Agr & Forestry Sci, Inst Plant Protect, Yinchuan 750002, Peoples R China

4.Huazhong Agr Univ, Coll Plant Sci & Technol, Wuhan 430070, Peoples R China

5.Sindh Agr Univ, Fac Crop Protect, Dept Entomol, Tandojam 70060, Pakistan

6.Agr Univ Hebei, Coll Plant Protect, Baoding 071000, Peoples R China

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

页码：

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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