Molecular cloning and functional characterization of an isoflavone glucosyltransferase from Pueraria thomsonii.
10.1016/S1875-5364(21)60105-X
- Author:
Hai-Yan DUAN
1
,
2
;
Jian WANG
3
;
Liang-Ping ZHA
4
;
Hua-Sheng PENG
1
,
5
,
6
;
Yu-Ping ZHAO
3
;
Yuan YUAN
7
;
Lu-Qi HUANG
1
,
8
Author Information
1. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China
2. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China.
3. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China.
4. School of Pharmacy, Anhui University of Chinese Medicine, Hefei 230012, China.
5. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China
6. Research Unit of DAO-DI Herbs, Chinese Academy of Medical Sciences, Beijing 100700, China.
7. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China. Electronic address: y_yuan0732@163.com.
8. State Key Laboratory Breeding Base of Dao-di Herbs, China Academy of Chinese Medical Sciences, Beijing 100700, China. Electronic address: huangluqi01@126.com.
- 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.
