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

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 process...

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Bibliographic Details
Published in:Chinese journal of natural medicines 2022-02, Vol.20 (2), p.133-138
Main Authors: DUAN, Hai-Yan, WANG, Jian, ZHA, Liang-Ping, PENG, Hua-Sheng, ZHAO, Yu-Ping, YUAN, Yuan, HUANG, Lu-Qi
Format: Article
Language:English
Subjects:
4′-O-glucosylation
7-O-glucosylation
Cloning, Molecular
Flavonone
Genistein
Glucosyltransferase
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
Isoflavone
Isoflavones - pharmacology
Pueraria - chemistry
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Summary: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.
ISSN:1875-5364
1875-5364
DOI:10.1016/S1875-5364(21)60105-X