Enzymatic N ‐Glycosylation of Diverse Arylamine Aglycones by a Promiscuous Glycosyltransferase from Carthamus tinctorius

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.