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