Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 66, Issue 36, Pages 9446-9455Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.8b02544
Keywords
ginsenoside; biosynthesis; UGTs; overexpression; site-directed mutagenesis
Funding
- National Natural Science Foundation of China (NSFC) [81703639]
- Central Significant Increase or Decrease Program of China [2060302-1604-05]
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Ginsenosides attract great attention for their bioactivities. However, their contents are low, and many UDP-glycosyltransferases (UGTs) that play crucial roles in the ginsenoside biosynthesis pathways have not been identified, which hinders the biosynthesis of ginsenosides. In this study, we reported that one UDP-glycosyltransferase, UGTPg71A29, from Panax ginseng could glycosylate C20-OH of Rh-1 and transfer a glucose moiety to Rd, producing ginsenosides Rg(1) and Rb-1 respectively. Ectopic expression of UGTPg71A29 in Saccharomyces cerevisiae stably generated Rg(1) and Rb-1 under its corresponding substrate. Overexpression of UGTPg71A29 in transgenic cells of P. ginseng could significantly enhance the accumulation of Rg(1) and Rb-1 with their contents of 3.2- and 3.5-fold higher than those in the control, respectively. Homology modeling, molecular dynamics, and mutational analysis revealed the key catalytic site, G1n283, which provided insights into the catalytic mechanism of UGTPg71A29. These results not only provide an efficient enzymatic tool for the synthesis of glycosides but also help achieve large-scale industrial production of glycosides.
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