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GuUGT, a glycosyltransferase from Glycyrrhiza uralensis , exhibits glycyrrhetinic acid 3- and 30-O-glycosylation
Author(s) -
Ying Huang,
Da Li,
Jinhe Wang,
Cai Yi,
Zhubo Dai,
Dan Jiang,
Chunsheng Liu
Publication year - 2019
Publication title -
royal society open science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.84
H-Index - 51
ISSN - 2054-5703
DOI - 10.1098/rsos.191121
Subject(s) - glycyrrhiza uralensis , glycosyltransferase , glucosyltransferase , glycosylation , glycoside , biochemistry , gene , chemistry , glucosyltransferases , transcriptome , biosynthesis , glucoside , yeast , biology , gene expression , stereochemistry , medicine , alternative medicine , pathology
Glycyrrhiza uralensis is a well-known herbal medicine that contains triterpenoid saponins as the predominant bioactive components, and these compounds include glycyrrhetinic acid (GA)-glycoside derivatives. Although two genes encoding UDP-glycosyltransferases (UGTs) that glycosylate these derivates have been functionally characterized in G. uralensis , the mechanisms of glycosylation by other UGTs remain unknown. Based on the available transcriptome data, we isolated a UGT with expression in the roots of G. uralensis . This UGT gene possibly encodes a glucosyltransferase that glycosylates GA derivatives at the 3-OH site. Biochemical analyses revealed that the recombinant UGT enzyme could transfer a glucosyl moiety to the free 3-OH or 30-COOH groups of GA. Furthermore, engineered yeast harbouring genes involved in the biosynthetic pathway for GA-glycoside derivates produced GA-3- O -β-D-glucoside, implying that the enzyme has GA 3-O-glucosyltransferase activity in vivo . Our results could provide a frame for understand the function of the UGT gene family, and also is important for further studies of triterpenoids biosynthesis in G. uralensis .

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