Molecular cloning and functional characterization of an isoflavone glucosyltransferase from Pueraria

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Pueraria thomsonii has long been used in traditional Chinese medicine.Isoflavonoids are the principle pharmacologic-ally active components,which are primarily observed as glycosyl-conjugates and accumulate in P.thomsonii roots.However,the mo-lecular 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.Bio-chemical 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 bio-transformation of isoflavones and other natural products for food or pharmacological applications.
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