Supplementary materials of GuUGT, a permissive glycosyltransferase from Glycyrrhiza uralensis, exhibits glycyrrhetinic acid 3- and 30‑O‑glycosylation

We identified and characterised a new UGT from G.
uralensis. Phylogenetic analysis suggested that this GuUGT may function on the
3-OH site of substrates. Heterologous expression in E. coli was applied
to investigate whether the recombinant protein functioned via glycosylation of
GA. In addition, expression of GuUGT in Saccharomyces cerevisiae was
performed to test its in vivo glycosylation of 3-OH and 30-COOH groups.

本研究从乌拉尔甘草（G. uralensis）中鉴定并表征了一种新型UDP-糖基转移酶（UGT）。系统发育分析提示，该乌拉尔甘草UGT（GuUGT）可能作用于底物的3-羟基位点。为探究该重组蛋白是否可通过对甘草酸（GA）的糖基化发挥功能，本研究在大肠杆菌（E. coli）中开展了异源表达实验。此外，本研究还在酿酒酵母（Saccharomyces cerevisiae）中表达GuUGT，以检测其对底物3-羟基与30-羧基位点的体内糖基化活性。