A novel sterol glycosyltransferase catalyses steroidal sapogenin 3-O glucosylation from Paris polyphylla var. yunnanensis
A novel sterol glycosyltransferase catalyses steroidal sapogenin 3-O glucosylation from Paris polyphylla var. yunnanensis
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DOI：
10.1007/s11033-022-08199-y
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发表时间：
2022-12
影响因子：
2.8
通讯作者：
Min He;Siyuan Guo;Yan Yin;Chi Zhang;Xianan Zhang
中科院分区：
文献类型：
--
作者：
Min He;Siyuan Guo;Yan Yin;Chi Zhang;Xianan Zhang
BackgroundParis polyphyllavar。云南植物是一种重要的药用植物，其主要活性成分是多叶根素，是一种具有药理活性的甾类皂苷。参与聚叶毛素生物合成的中心酶基因逐渐被发现；然而，ugt很少被说明。方法与结果从巴黎多叶黄中克隆了一种新的甾醇糖基转移酶。并对其体外催化功能进行了鉴定。PpUGT6表现出对多叶磷脂中pennogenin皂苷元C-3糖基化的催化能力，PpUGT6对睾酮和甲基睾酮C-17位的甾体和甘次酸C-3位的三萜表现出催化混杂性。对ppugt6蛋白进行了同源性建模，并与糖受体和给体进行了虚拟分子对接，预测了与配体相互作用的关键残基。结论PpUGT6是一种新型的甾醇糖基转移酶，与多叶树素的生物合成有关。重楼,为特征。pppugt6催化C-3糖基化生成多叶树素的pennogenin皂苷元，这是多叶树素生物合成途径的第一步糖基化。有趣的是，PpUGT6在C-17位表现出向睾酮和甲基睾酮的糖多样化，在C-3位表现出甘草次酸的三萜。ppugt6蛋白与配体的虚拟分子对接预测了与配体相互作用的关键残基。本工作表征了一种新的SGT糖基化多叶树素C-3位的丁香苷元皂苷元。为进一步阐明植物甾醇糖基转移酶在催化乱交中的作用以及与底物相互作用的关键残基提供了参考。
BackgroundParis polyphyllavar.yunnanensisis an important medicinal plant, and the main active ingredient of the plant is polyphyllin, which is a steroid saponin with pharmacological activities. The central enzyme genes participating in the biosynthesis of polyphyllin are increasingly being uncovered; however, UGTs are rarely illustrated.Methods and resultsIn this study, we cloned a new sterol glycosyltransferase fromParis polyphyllavar.yunnanensisand identified its catalytic function in vitro.PpUGT6 showed the ability to catalyse the C-3 glycosylation of pennogenin sapogenin of polyphyllin, andPpUGT6 showed catalytic promiscuity towards steroids at the C-17 position of testosterone and methyltestosterone and the triterpene at the C-3 position of glycyrrhetinic acid. Homology modelling of thePpUGT6 protein and virtual molecular docking ofPpUGT6 with sugar acceptors and donors were performed, and we predicted the key residues interacting with ligands.ConclusionsHere,PpUGT6, a novel sterol glycosyltransferase related to the biosynthesis of polyphyllin fromP. polyphylla,was characterized. PpUGT6 catalysed C-3 glycosylation to pennogenin sapogenin of polyphyllin, which is the first glycosylation step of the biosynthetic pathway of polyphyllins. Interestingly,PpUGT6 demonstrated glycodiversification to testosterone and methyltestosterone at C-17 and triterpene of glycyrrhetinic acid at the C-3 position. The virtual molecular docking ofPpUGT6 protein with ligands predicted the key residues interacting with them. This work characterized a novel SGT glycosylating pennogenin sapogenin at C-3 of polyphyllin fromP. polyphyllaand provided a reference for further elucidation of the phytosterol glycosyltransferases in catalytic promiscuity and key residues interacting with substrates.