Molecular cloning and functional characterization of an isoflavone glucosyltransferase from Pueraria thomsonii
| Autor: | Wang Jian, Yuan Yuan, Peng Huasheng, Duan Haiyan, Huang Luqi, Zhao Yuping, Zha Liangping |
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| Rok vydání: | 2022 |
| Předmět: |
Pueraria
biology Daidzein food and beverages Genistein General Medicine Isoflavones biology.organism_classification carbohydrates (lipids) chemistry.chemical_compound Complementary and alternative medicine chemistry Biochemistry Glucosyltransferases Drug Discovery biology.protein Formononetin Glucosyltransferase Cloning Molecular Liquiritigenin Isoliquiritigenin |
| Zdroj: | Chinese Journal of Natural Medicines. 20:133-138 |
| ISSN: | 1875-5364 |
| Popis: | Pueraria thomsonii has long been used in traditional Chinese medicine, isoflavonoids are the principle pharmacologically active components and they 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 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, whereas exhibited no enzyme activity to flavonones (liquiritigenin, 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. |
| Databáze: | OpenAIRE |
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