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Issue 94, 2016
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Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates

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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.

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

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Supplementary files

Article information


Submitted
25 Aug 2016
Accepted
28 Oct 2016
First published
01 Nov 2016

Chem. Commun., 2016,52, 13679-13682
Article type
Communication

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

C. Brieke, G. Yim, M. Peschke, G. D. Wright and M. J. Cryle, Chem. Commun., 2016, 52, 13679
DOI: 10.1039/C6CC06975D

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