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Bibliographic Details
Main Authors: Subthain, Hizar, Guo, Fei, Zhang, Chengjie, Fang, Peng, Zhang, Lingli, Su, Qixuan, Tang, Dandan, Chi, Luping, Liu, Changning, Urlacher, Vlada B, Li, Jing, Du, Lei, Li, Shengying
Format: Artículo científico
Language:en
Published: Synthetic and systems biotechnology 2026
Online Access:https://pubmed.ncbi.nlm.nih.gov/42058439/
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Table of Contents:
  • Functional characterization of four glycosyltransferases for biosynthesis of steroidal saponins in medicinal plant . Subthain, Hizar Guo, Fei Zhang, Chengjie Fang, Peng Zhang, Lingli Su, Qixuan Tang, Dandan Chi, Luping Liu, Changning Urlacher, Vlada B Li, Jing Du, Lei Li, Shengying species are renowned for the production of important medicinal steroidal saponins (, polyphyllins). UDP-dependent glycosyltransferases (UGTs) play important roles in saponin biosynthesis. However, the glycosylation steps have not been fully elucidated. Here, we investigate four candidate UGTs (, UGT91BP2, UGT703R1, UGT703R2 and UGT703R3) from the medicinal herb var. , followed by their phylogenetic, biochemical, and functional characterization as saponin biosynthetic enzymes. These four recombinant UGTs expressed in catalyze the glucosylation of diosgenin to produce diosgenin 3--glucoside (trillin); while UGT703R1, UGT703R2 and UGT703R3 glucosylate pennogenin to pennogenin 3--glucoside o. Transient expression of these UGTs in leaves, supplemented with diosgenin substrate, confirms their roles in trillin biosynthesis. Subcellular localization analysis in tobacco cells reveals their presence in both cytoplasm and nucleus. Gene transcript analysis reveals that the four exhibit higher expression in leaves and flowers than in stems, indicating distinct tissue-specific patterns. This work identifies key UGTs involved in polyphyllin biosynthesis, enriching the enzymatic toolbox involved in the glucosylation of diosgenin and pennogenin aglycones, and provides a valuable reference for future studies on overproduction of bioactive steroidal glycosides in heterologous hosts.