486-62-4Relevant articles and documents
Xing, Xiaoyan,Sun, Zhonghao,Yang, Meihua,Zhu, Nailiang,Yang, Junshan,Ma, Guoxu,Xu, Xudong
, (2018)
Two trifunctional leloir glycosyltransferases as biocatalysts for natural products glycodiversification
Pandey, Ramesh Prasad,Bashyal, Puspalata,Parajuli, Prakash,Yamaguchi, Tokutaro,Sohng, Jae Kyung
supporting information, p. 8058 - 8064 (2019/10/14)
Two promiscuous Bacillus licheniformis glycosyltransferases, YdhE and YojK, exhibited prominent stereospecific but nonregiospecific glycosylation activity of 20 different classes of 59 structurally different natural and non-natural products. Both enzymes transferred various sugars at three nucleophilic groups (OH, NH2, SH) of diverse compounds to produce O-, N-, and S-glycosides. The enzymes also displayed a catalytic reversibility potential for a one-pot transglycosylation, thus bestowing a cost-effective application in biosynthesis of glycodiversified natural products in drug discovery.
Regio- and Stereospecific O-Glycosylation of Phenolic Compounds Catalyzed by a Fungal Glycosyltransferase from Mucor hiemalis
Feng, Jin,Zhang, Peng,Cui, Yinglu,Li, Kai,Qiao, Xue,Zhang, Ying-Tao,Li, Shu-Ming,Cox, Russell J.,Wu, Bian,Ye, Min,Yin, Wen-Bing
, p. 995 - 1006 (2017/03/27)
Glycosylated small molecules are often bioactive and obtained mainly via microbial biotransformation especially by fungi. However, no responsible glycosylation gene/enzyme has yet been uncovered in a filamentous fungus. We report here the first identification of a phenolic glycosyltransferase MhGT1 from Mucor hiemalis. The substrate promiscuity of the new phenolic O-glycosyltransferase was explored by using phenols from Traditional Chinese Medicinal herbs as substrates. MhGT1 exhibited robust capabilities for the regio- and stereospecific O-glycosylation of 72 structurally diverse drug-like scaffolds and sterols with uridine diphosphate (UDP) glucose as a sugar donor. Unprecedentedly, MhGT1 showed higher regiospecificities and activities for prenylated phenols than for their non-prenylated analogues. Computational modelling of MhGT1 uncovered a truncated N-terminal domain of the enzyme consisting of hydrophobic and charged amino acid residues which contributed to the broad substrate scope and regiospecificity towards prenylated compounds. Our findings expand the ways to obtain new glycosyltransferases and also effectively apply the enzymatic approach to obtain glycosylated compounds in drug discovery. (Figure presented.).
