野大豆黄酮 UDP-糖基转移酶 GsUGT1 的 挖掘及功能表征

Wild soya (Glycine soja Siebold & Zucc.) is an important cereal and oil crop, rich in flavonoids and with a variety of pharmacological activities. Glycosylation can transform aglycones into glycosides with greater stability, stronger biological activity and more diverse structures. Through genome analysis and enzyme mining, a flavonoid UDP- glycosyltransferase GsUGT1 from wild soybean was reported, which acts mainly on the 7-OH position of liquiritigenin and has catalytic activity on 6 types of flavonoid receptors. In addition, GsUGT1 was successfully heterologously expressed in E. coli and then purified. Enzymatic characterization revealed that the catalytic activity of the enzyme was maximal at pH 7.0 and temperature 35°C. AMichaelis-Menten kinetics study showed that the catalytic efficiency kCat/Km of GsUGT1 was 6.70 × 10^_5 μmol/(L · S). Through molecular docking, the catalytic mechanism of GsUGT1 was preliminarily explored. To the best of our knowledge, this is the first study to report the UDP-glycosyltransferase GsUGT1 in wild soybean, which is expected to become an effective tool for the enzymatic synthesis of flavonoid glycoside derivatives.