71802-05-6Relevant academic research and scientific papers
Molecular and Structural Characterization of a Promiscuous C-Glycosyltransferase from Trollius chinensis
He, Jun-Bin,Zhao, Peng,Hu, Zhi-Min,Liu, Shuang,Kuang, Yi,Zhang, Meng,Li, Bin,Yun, Cai-Hong,Qiao, Xue,Ye, Min
supporting information, p. 11513 - 11520 (2019/07/16)
Herein, the catalytic promiscuity of TcCGT1, a new C-glycosyltransferase (CGT) from the medicinal plant Trollius chinensis is explored. TcCGT1 could efficiently and regio-specifically catalyze the 8-C-glycosylation of 36 flavones and other flavonoids and could also catalyze the O-glycosylation of diverse phenolics. The crystal structure of TcCGT1 in complex with uridine diphosphate was determined at 1.85 ? resolution. Molecular docking revealed a new model for the catalytic mechanism of TcCGT1, which is initiated by the spontaneous deprotonation of the substrate. The spacious binding pocket explains the substrate promiscuity, and the binding pose of the substrate determines C- or O-glycosylation activity. Site-directed mutagenesis at two residues (I94E and G284K) switched C- to O-glycosylation. TcCGT1 is the first plant CGT with a crystal structure and the first flavone 8-C-glycosyltransferase described. This provides a basis for designing efficient glycosylation biocatalysts.
Comparing the acceptor promiscuity of a Rosa hybrida glucosyltransferase RhGT1 and an engineered microbial glucosyltransferase OleDPSA toward a small flavonoid library
Wang, Lu,Han, Weiqing,Xie, Chenying,Hou, Jingli,Fang, Qinghong,Gu, Jianchun,Wang, Peng George,Cheng, Jiansong
supporting information, p. 73 - 77 (2013/03/14)
Glycosylation is a widespread modification of plant secondary metabolites, and catalyzed by a superfamily of enzymes called UDP-glycosyltransferases (UGTs). UGTs are often involved in late biosynthetic steps and show broad substrate specificity or regioselectivity. In this study, the acceptor promiscuity of a Rosa hybrid UGT RhGT1 and an evolved microbial UGT OleD PSA toward a small flavonoid library was probed and compared. Interestingly, RhGT1 showed comparable acceptor promiscuity in comparison with OleDPSA, though the acceptor binding pocket of the latter is much more open and large. This clearly indicates that stabilization of the acceptor position by suitable hydrophobic interactions is important for the specificity or regioselectivity determination as well as overall fit of the acceptor into a 'big enough' binding pocket. This also poses a challenge for structure-based UGT engineering to alter the glucosylation pattern of flavonoids.
Highly efficient glucosylation of flavonoids
Semeniuchenko, Volodymyr,Garazd, Yana,Garazd, Myroslav,Shokol, Tetyana,Groth, Ulrich,Khilya, Volodymyr
experimental part, p. 1503 - 1512 (2010/06/19)
A highly efficient procedure for glucosylation of flavonoids by acetobromoglucose is described. Glucosylation is carried out in a two-phase system CHCl3/H2O over 96 h using tetrabutylammonium bromide as phase-transfer catalyst. A pur
Synthesis of flavonoid 7-O-β-D-glycosides by phase transfer catalysis
Wu, Zheng,Jiang, Ling,Chen, He,Wang, Qiu-An
experimental part, p. 195 - 197 (2009/11/30)
Six flavonoid 7-O-β-D-glycosides 1a-3a and 1b-3b were synthesised from the flavones 7a and 7b by glycosidation and deacetylation with the corresponding a-acetylglycosyl bromides. 7a and 7b were prepared in high yield by an improved Baker-Venkataraman rearrangement using 2, 4- dihydro×yacetophenone as starting material and tetrabutylammonium bromide (TBAB) as a phase transfer catalyst. The glycosidation procedure was modified by using anhydrous K2CO3 in a solvent mixture of DMF/acetone (3:2v/v) and TBAB as a phase transfer catalyst.
