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Investigating the Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii
Author(s) -
Jie Gao,
Baowei Ma,
Yun Lü,
Yifeng Zhang,
Yuru Tong,
Siyuan Guo,
Wei Gao,
Luqi Huang
Publication year - 2020
Publication title -
acs omega
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.9b02919
Subject(s) - tripterygium wilfordii , glycosyltransferase , flavonoid , chemistry , quercetin , glycoside , luteolin , glucoside , enzyme , glucosyltransferases , acacetin , biochemistry , phloretin , substrate (aquarium) , o methyltransferase , stereochemistry , apigenin , antioxidant , biology , methyltransferase , medicine , ecology , alternative medicine , pathology , methylation , gene
Flavonoid glycosides have shown many pharmacological activities in clinical studies. However, the main way to obtain flavonoid glycosides is to extract and separate them from plants, which wastes both time and resources. Here, we identified the O -glycosyltransferase (UGTs) TwUGT3 from Tripterygium wilfordii and analyzed its bioinformatics. First, the enzyme was found to utilize phloretin and uridine diphosphate glucose (UDPG) as substrates to produce an acid-tolerant glucoside. Then, it also can use quercetin and UDPG as substrates to produce the corresponding O -glucoside. In addition, we further explored the substrate specificity of TwUGT3, which suggested that it also accepts luteolin, pinocembrin, and genistein to produce the corresponding O -glucosides. Subsequently, the optimum pH, reaction time, reaction temperature, and enzymatic kinetic parameters of TwUGT3 were determined.

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