Functional characterization of a UDP-xylose-preferring C-glycosyltransferase from Lemna aequinoctialis  

作　　者：Sharpkate Shaker Zhi-Min Hu Zi-Long Wang Guo Ye Jin-Chen Long Xin-Fang Zhai Xue Qiao Min Ye 

机构地区：[1]State Key Laboratory of Natural and Biomimetic Drugs,School of Pharmaceutical Sciences,Peking University,38 Xueyuan Road,Beijing 100191,China

出　　处：《Medicinal Plant Biology》2022年第1期2-7,共6页药用植物生物学（英文）

基　　金：the National Natural Science Foundation of China(Grant No.81725023,82122073);the National Key Research and Development Program of China(No.2017YFC1700405).

摘　　要：C-glycosides are an important class of bioactive natural products,and the C-glycosidic bonds are usually catalyzed by C-glycosyltransferases.In this work,an efficient and rare CGT,LaCGT1,was discovered from the aquatic plant Lemna aequinoctialis.LaCGT1 could accept five sugar donors(UDP-Glc/-Xyl/-Gal/-GlcNAc/-Ara)to catalyze C-glycosylation,and showed strong preference to uridine 5′-diphosphate xylose(UDP-Xyl).LaCGT1 catalyzed at least six substrates using UDP-Xyl as sugar donor,with conversion rates of>95%.Three xylosides were obtained by scaled-up enzymatic catalysis,and their structures were identified by 1D NMR,2D NMR,and HR-ESIMS data analyses.Molecular modeling and site-directed mutagenesis indicated that R271,W357,D378,and Q379 residues were key amino acids contributing to sugar donor recognition of UDP-Xyl.LaCGT1 could be a promising catalyst to prepare bioactive flavonoid C-xylosides.

关 键 词：SUGAR DONOR CATALYZED 

分 类 号：Q946[生物学—植物学]