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Molecular cloning and functional characterization of an isoflavone glucosyltransferase from Pueraria thomsonii

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摘要 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.
出处 《Chinese Journal of Natural Medicines》 SCIE CAS CSCD 2022年第2期133-138,共6页 中国天然药物(英文版)
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)。
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