Pueraria thomsonii has long been used in traditional Chinese medicine.Isoflavonoids are the principle pharmacologically active components,which are primarily observed as glycosyl-conjugates and accumulate in P.thomson...Pueraria thomsonii has long been used in traditional Chinese medicine.Isoflavonoids are the principle pharmacologically active components,which are primarily observed as glycosyl-conjugates and accumulate in P.thomsonii roots.However,the molecular mechanisms underlying the glycosylation processes in(iso)flavonoid biosynthesis have not been thoroughly elucidated.In the current study,an O-glucosyltransferase(PtUGT8)was identified in the medicinal plant P.thomsonii from RNA-seq database.Biochemical assays of the recombinant PtUGT8 showed that it was able to glycosylate chalcone(isoliquiritigenin)at the 4-OH position and glycosylate isoflavones(daidzein,formononetin,and genistein)at the 7-OH or 4′-OH position,exhibiting no enzyme activity to flavonones(liquiritigenin and narigenin)in vitro.The identification of PtUGT8 may provide a useful enzyme catalyst for efficient biotransformation of isoflavones and other natural products for food or pharmacological applications.展开更多
基金supported by the National Key Research and Development Program of China(Nos.2017YFC1702901 and 2017YFC1701601)CAMS Innovation Fund for Medical Sciences(No.2019-I2M-5-065)。
文摘Pueraria thomsonii has long been used in traditional Chinese medicine.Isoflavonoids are the principle pharmacologically active components,which are primarily observed as glycosyl-conjugates and accumulate in P.thomsonii roots.However,the molecular mechanisms underlying the glycosylation processes in(iso)flavonoid biosynthesis have not been thoroughly elucidated.In the current study,an O-glucosyltransferase(PtUGT8)was identified in the medicinal plant P.thomsonii from RNA-seq database.Biochemical assays of the recombinant PtUGT8 showed that it was able to glycosylate chalcone(isoliquiritigenin)at the 4-OH position and glycosylate isoflavones(daidzein,formononetin,and genistein)at the 7-OH or 4′-OH position,exhibiting no enzyme activity to flavonones(liquiritigenin and narigenin)in vitro.The identification of PtUGT8 may provide a useful enzyme catalyst for efficient biotransformation of isoflavones and other natural products for food or pharmacological applications.
