882048-86-4Relevant academic research and scientific papers
Enzymatic N-Glycosylation of Diverse Arylamine Aglycones by a Promiscuous Glycosyltransferase from Carthamus tinctorius
Xie, Kebo,Chen, Ridao,Chen, Dawei,Li, Jianhua,Wang, Ruishan,Yang, Lin,Dai, Jungui
, p. 603 - 608 (2017)
A new glycosyltransferase (UGT71E5) from Carthamus tinctorius exhibited a robust promiscuity towards 30 structurally diverse drug-like aromatic amine scaffolds, making it the first reported glycosyltransferase capable of catalyzing N-glycosylation with multiple diverse nitrogen-heterocyclic aromatic compounds. The catalytic promiscuity and reversibility of UGT71E5 was exploited to generate the rare N-glycoside from the abundant O-glycoside with high efficiency. These findings demonstrate the significant potential of UGT71E5 in the enzymatic synthesis of diverse bioactive N-glycosides. (Figure presented.).
