Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates. Issue 94 (4th November 2016)

• Record Type: Journal Article
• Authors: Brieke, Clara; Yim, Grace; Peschke, Madeleine; Wright, Gerard D.; Cryle, Max J.
• Is Part Of: Chemical communications. Volume 52:Issue 94(2016)
• Page Start: 13679
• Page End: 13682
• Publication Date: 2016-11-04
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c6cc06975d
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Remarkable promiscuity of N -methyltransferases enables modulation of biological activity as well as bio-orthogonal labelling of glycopeptide antibiotics and biosynthetic intermediates. Abstract : We show that two α- N -methyltransferases involved in the biosynthesis of glycopeptide antibiotics (GPAs) already recognise partly crosslinked precursor peptides of teicoplanin aglycone indicating that in vivo N -methylation can occur as an early tailoring step during GPA biosynthesis. This relaxed substrate specificity is accompanied by a remarkable promiscuity regarding the co-substrate enabling modulation of biological activity and the introduction of reactive handles which could be further modified using bio-orthogonal chemistry.