Characterization of Three Paris polyphylla Glycosyltransferases from Different UGT Families for Steroid Functionalization

• DOI: 10.1021/acssynbio.2c00103
• Publication Date: 2022-03-14T19:44:15Z
• Authors: Wei Song; Chunchun Zhang; Jiali Wu; Jianzhao Qi; Xin Hua; Liping Kang; Qiang Yuan; Jifeng Yuan; Zheyong Xue
• Keywords: Diosgenin; Sapogenin

Plant steroid glycosides, such as phytosterol steroidal saponins, and glycoalkaloids, are natural products with great pharmaceutical values. In this study, we characterized three UDP-glycosyltransferases (UGTs) involved in the glycosylation of sapogenin from Paris polyphylla. Substrate specificity analysis revealed that UGT73CR1 could glycosylate sapogenins alkaloids, highest affinity for diosgenin. The residues His27 Asp129 conserved corresponding positions plant glycosyltransferases, which crucial activating C-3 OH receptor substrates. comparison, UGT80A33 UGT80A34 exhibited a higher cholesterol than other steroids. UGT80s have larger active pocket, allows them to accommodate side chain sterols. summary, assessed P. polyphylla glycosyltransferases two UGT families functionalization molecules, will provide basis future biomanufacturing diverse bioactive glycosides.