文献类型： 外文期刊

作者： Song, Xuan ¹ ; Liu, Chang ² ; Dhiloo, Khalid H. ¹ ; Yi, Chao-qun ¹ ; Zhang, Tian-tao ¹ ; Zhang, Yong-jun ¹ ;

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

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

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

4.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing 100193, Peoples R China

关键词： catalytic activity; geranylgeranyl diphosphate synthase; molecular docking; Monolepta hieroglyphica; recombinant expression

期刊名称：ARCHIVES OF INSECT BIOCHEMISTRY AND PHYSIOLOGY （ 影响因子：2.2； 五年影响因子：2.1 ）

ISSN： 0739-4462

年卷期： 2024 年 115 卷 2 期

页码：

收录情况： SCI

摘要： Geranylgeranyl diphosphate synthase (GGPPS) as the short-chain prenyltransferases for catalyzing the formation of the acyclic precursor (E)-GGPP has been extensively investigated in mammals, plants, and microbes, but its functional plasticity is poorly understood in insect species. Here, a single GGPPS in leaf beetle Monolepta hieroglyphica, MhieGGPPS, was functionally investigated. Phylogenetic analysis showed that MhieGGPPS was clustered in one clade with homologs and had six conserved motifs. Molecular docking results indicated that binding sites of dimethylallyl diphosphate (DMAPP), (E)-geranyl pyrophosphate (GPP), and (E)-farnesyl pyrophosphate (FPP) were in the chain-length determination region of MhieGGPPS, respectively. In vitro, recombiant MhieGGPPS could catalyze the formation of (E)-geranylgeraniol against different combinations of substrates including isopentenyl pyrophosphate (IPP)/DMAPP, IPP/(E)-GPP, and IPP/(E)-FPP, suggesting that MhieGGPPS could not only use (E)-FPP but also (E)-GPP and DMAPP as the allylic cosubstrates. In kinetic analysis, the (E)-FPP was most tightly bound to MhieGGPPS than that of others. It was proposed that MhieGGPPS as a multifunctional enzyme is differentiated from the other GGPPSs in the animals and plants, which only accepted (E)-FPP as the allylic cosubstrate. These findings provide valuable insights into understanding the functional plasticity of GGPPS in M. hieroglyphica and the novel biosynthesis mechanism in the isoprenoid pathway.