92631-83-9Relevant articles and documents
Functional Characterization and Structural Basis of an Efficient Di-C-glycosyltransferase from Glycyrrhiza glabra
Chi, Chang-Biao,He, Jun-Bin,Li, Fu-Dong,Li, Kai,Liu, Zhen-Ming,Ma, Ming,Qiao, Xue,Shi, Xiao-Meng,Su, Hui-Fei,Wang, Yu-Xi,Wang, Zi-Long,Yang, Dong-Hui,Ye, Min,Yun, Cai-Hong,Zhang, Liang-Ren,Zhang, Meng,Zhang, Zhi-Yong,Zhang, Zhong-Yi
supporting information, p. 3506 - 3512 (2020/03/06)
A highly efficient di-C-glycosyltransferase GgCGT was discovered from the medicinal plant Glycyrrhiza glabra. GgCGT catalyzes a two-step di-C-glycosylation of flopropione-containing substrates with conversion rates of >98%. To elucidate the catalytic mech
Probing the catalytic promiscuity of a regio- and stereospecific C-glycosyltransferase from Mangifera indica
Chen, Dawei,Chen, Ridao,Wang, Ruishan,Li, Jianhua,Xie, Kebo,Bian, Chuancai,Sun, Lili,Zhang, Xiaolin,Liu, Jimei,Yang, Lin,Ye, Fei,Yu, Xiaoming,Dai, Jungui
supporting information, p. 12678 - 12682 (2015/10/28)
The catalytic promiscuity of the novel benzophenone C-glycosyltransferase, MiCGT, which is involved in the biosynthesis of mangiferin from Mangifera indica, was explored. MiCGT exhibited a robust capability to regio- and stereospecific C-glycosylation of 35 structurally diverse druglike scaffolds and simple phenolics with UDP-glucose, and also formed O- and N-glycosides. Moreover, MiCGT was able to generate C-xylosides with UDP-xylose. The OGT-reversibility of MiCGT was also exploited to generate C-glucosides with simple sugar donor. Three aryl-C-glycosides exhibited potent SGLT2 inhibitory activities with IC50 values of 2.6×, 7.6×, and 7.6×10-7-M, respectively. These findings demonstrate for the first time the significant potential of an enzymatic approach to diversification through C-glycosidation of bioactive natural and unnatural products in drug discovery. C-glycodiversification: MiCGT, as the first benzophenone C-glycosyltransferase (CGT) from Mangifera indica, showed robust regio- and stereospecific C-glycosylation activity for 35 structurally diverse acceptors with UDP-glucose or xylose. The aryl-C-glycoside 1 exhibited potent antidiabetic activity toward SGLT2.