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Ginkgo biloba  L., a “living fossil” and medicinal plant, is a well-known rich source of bioactive flavonoids. The molecular mechanism underlying the biosynthesis of flavonoid glucosides, the predominant flavonoids in  G. biloba , remains unclear. To better understand flavonoid glucosylation in  G. biloba , we generated a transcriptomic dataset of  G. biloba  leaf tissue by high-throughput RNA sequencing. We identified 25 putative UDP-glycosyltransferase ( UGT ) unigenes that are potentially involved in the flavonoid glycosylation. Among them, we successfully isolated and expressed eight  UGT  genes in  Escherichia coli , and found that recombinant UGT716A1 protein was active toward broad range of flavonoid/phenylpropanoid substrates. In particular, we discovered the first recombinant UGT protein, UGT716A1 from  G. biloba , possessing unique activity toward flavanol gallates that have been extensively documented to have significant bioactivity relating to human health.  UGT716A1  expression level paralleled the flavonoid distribution pattern in  G. biloba . Ectopic over-expression of  UGT716A1  in  Arabidopsis thaliana  led to increased accumulation of several flavonol glucosides. Identification and comparison of the  in vitro  enzymatic activity of UGT716A1 homologs revealed a UGT from the primitive land species  Physcomitrella patens  also showed broader substrate spectrum than those from higher plants  A. thaliana, Vitis vinifera , and  Medicago truncatula . The characterization of  UGT716A1  from  G. biloba  bridges a gap in the evolutionary history of  UGTs  in gymnosperms. We also discuss the implication of  UGT716A1  for biosynthesis, evolution, and bioengineering of diverse glucosylated flavonoids.

Characterization of UGT716A1 as a Multi-substrate UDP:Flavonoid Glucosyltransferase Gene in Ginkgo biloba