UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius
10.1016/j.chmed.2020.05.010
- Author:
Song-yang SUI
1
Author Information
1. College of Life and Environmental Sciences, Minzu University of China
- Publication Type:Journal Article
- Keywords:
Carthamus tinctorius L.;
enzyme promiscuity;
glycosyltransferase;
O-glycosides
- From:
Chinese Herbal Medicines
2020;12(4):440-445
- CountryChina
- Language:Chinese
-
Abstract:
Objective: In order to obtain new glycosyltransferases with highly efficient catalysis, the glycosyltransferases from Carthamus tinctorius which contains diverse types of glycosides were mined. Methods: A new glycosyltransferase gene (UGT88B2) with full length was obtained by PCR and further transformed into Escherichia coli for heterologous expression. The catalytic activity of recombinant UGT88B2 was determined by HPLC-MSn. The structures of representative catalytic products were elucidated by MS and NMR. Results: UGT88B2 exhibited catalytic promiscuity and various patterns in glycosylation of flavonoids with high efficiency. Conclusion: A new glycosyltransferase named UGT88B2 was successfully mined and can be employed as enzymatic tools in glycosylation of flavonoids.
