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Journal Article

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

MPS-Authors
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Brieke,  Clara
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Peschke,  Madeleine
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Cryle,  Max J.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://pubs.rsc.org/en/content/articlepdf/2016/cc/c6cc06975d
(Any fulltext)

https://dx.doi.org/10.1039/C6CC06975D
(Any fulltext)

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Citation

Brieke, C., Yim, G., Peschke, M., Wright, G. D., & Cryle, M. J. (2016). Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates. Chemical Communications, 52(94), 13679-13682. doi:10.1039/C6CC06975D.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-B98B-2
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.