IiUGT71B2 catalyzes lignan glycosylation in Isatis indigotica with substrates specificity

Lignans are a major class of secondary metabolites distributed widely in the plant kingdom that are derived from coupling of phenylpropanoid (C6-C3) units. Most lignans are 8-8'-linked, and are often found in their glycosylated forms, which are catalyzed by UDP-dependent glycosyltransferase (UGT). Up to now, all UGTs involved in lignans biosynthesis are determined with substrate promiscuity. Here, IiUGT71B2 is reported from Isatis indigotica that specific catalyzes 4-O and 4 '-O glycosylation of furan (lariciresinol) and dibenzylbutyrolactone (matairesinol) type lignans. Transcriptional profile of IiUGT71B2 indicates its involvement in lignan glycosides biosynthesis, which is co-expressed with other lignan biosynthetic genes, and is consistent with metabolic distribution of lignans in organs and tissues as well. Both in vitro and in vivo experiments demonstrate IiUGT71B2 catalyzes the mono- and di- glycosylation of lariciresinol and mono-glycosylation of matairesinol. The ligand docking and site-directed mutagenesis suggest Asn261, Ser289, Ala356, and Tyr395 as key residues, which may determine its catalytic efficiency together with the narrow binding pocket of IiUGT71B2. This study provides insights into lignan metabolism and functional diversity of plant UGTs.

Automated summary

This study reports the discovery of an enzyme called IiUGT71B2, which specifically catalyzes the glycosylation of certain lignan compounds. This provides insights into the metabolism of lignans and the functional diversity of plant glycosyltransferases.