Molecular cloning and functional characterization of an isoflavone glucosyltransferase from Pueraria thomsonii.
10.1016/S1875-5364(21)60105-X
- Author:
Hai-Yan DUAN
1
;
Jian WANG
2
;
Liang-Ping ZHA
3
;
Hua-Sheng PENG
4
;
Yu-Ping ZHAO
2
;
Yuan YUAN
5
,
6
;
Lu-Qi HUANG
6
,
7
Author Information
1. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China; State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China.
2. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China.
3. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China.
4. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China; State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China; Research Unit of DAO-DI Herbs, Chinese Academy of Medical Sciences, Beijing 100700, China.
5. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China. Electronic address: y_yuan0732@
6. com.
7. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China; State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China. Electronic address: huangluqi01@
- Publication Type:Journal Article
- Keywords:
4′-O-glucosylation;
7-O-glucosylation;
Flavonone;
Glucosyltransferase;
Isoflavone
- MeSH:
Cloning, Molecular;
Genistein;
Glucosyltransferases/metabolism*;
Isoflavones/pharmacology*;
Pueraria/chemistry*
- From:
Chinese Journal of Natural Medicines (English Ed.)
2022;20(2):133-138
- CountryChina
- Language:English
-
Abstract:
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.
