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

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.
Original languageEnglish
Pages (from-to)13679-13682
Number of pages4
JournalChemical Communications
Volume52
Issue number94
DOIs
Publication statusPublished - Nov 2016

Cite this

Brieke, Clara ; Yim, Grace ; Peschke, Madeleine ; Wright, Gerard D. ; Cryle, Max J. / Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates. In: Chemical Communications. 2016 ; Vol. 52, No. 94. pp. 13679-13682.
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Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates. / Brieke, Clara; Yim, Grace; Peschke, Madeleine; Wright, Gerard D.; Cryle, Max J.

In: Chemical Communications, Vol. 52, No. 94, 11.2016, p. 13679-13682.

Research output: Contribution to journalArticleOtherpeer-review

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