Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates

Clara Brieke, Grace Yim, Madeleine Peschke, Gerard D. Wright, Max J. Cryle

Research output: Contribution to journalArticleOtherpeer-review

5 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)13679-13682
Number of pages4
JournalChemical Communications
Issue number94
Publication statusPublished - Nov 2016

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