Enzymatic N‐Glycosylation of Diverse Arylamine Aglycones by a Promiscuous Glycosyltransferase from Carthamus tinctorius. Issue 4 (18th January 2017)

• Record Type: Journal Article
• Authors: Xie, Kebo; Chen, Ridao; Chen, Dawei; Li, Jianhua; Wang, Ruishan; Yang, Lin; Dai, Jungui
• Is Part Of: Advanced synthesis & catalysis. Volume 359:Issue 4(2017)
• Page Start: 603
• Page End: 608
• Publication Date: 2017-01-18
• Subjects: Carthamus tinctorius -- catalytic promiscuity -- enzyme catalysis -- glycosylation -- glycosyltransferases -- N-glycosylation; Catalysis -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Chemistry -- Periodicals; Chemistry, Technical -- Periodicals; Chemistry -- Periodicals; Catalysis -- Periodicals; Technology, Pharmaceutical -- Periodicals; 547.2
• DOI: 10.1002/adsc.201601128
• Languages: English
• ISSNs: 1615-4150

Abstract

Abstract: 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. Abstract :