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.