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Enzymatic N ‐Glycosylation of Diverse Arylamine Aglycones by a Promiscuous Glycosyltransferase from Carthamus tinctorius
Author(s) -
Xie Kebo,
Chen Ridao,
Chen Dawei,
Li Jianhua,
Wang Ruishan,
Yang Lin,
Dai Jungui
Publication year - 2017
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201601128
Subject(s) - carthamus , glycosylation , glycosyltransferase , chemistry , glycoside , enzyme , biochemistry , stereochemistry , amine gas treating , organic chemistry , traditional medicine , medicine
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.