UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius

Song-Yang Sui; Rui-Mingqian Guo; Ke-Bo Xie; Lin Yang; Jun-Gui Dai

doi:10.1016/j.chmed.2020.05.010

UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius

Chin Herb Med. 2020 Sep 18;12(4):440-445. doi: 10.1016/j.chmed.2020.05.010. eCollection 2020 Oct.

Authors

Song-Yang Sui¹, Rui-Mingqian Guo¹, Ke-Bo Xie², Lin Yang¹, Jun-Gui Dai²

Affiliations

¹ College of Life and Environmental Sciences, Minzu University of China, Beijing 100081, China.
² State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China.

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.

Keywords: Carthamus tinctorius L.; O-glycosides; enzyme promiscuity; glycosyltransferase.