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

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.

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Brieke, Clara1, Author              
Yim, Grace, Author
Peschke, Madeleine1, Author              
Wright, Gerard D., Author
Cryle, Max J.1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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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.

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Language(s): eng - English
 Dates: 2016-08-252016-10-282016-11-012016-11-17
 Publication Status: Published in print
 Pages: 4
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 Rev. Type: Peer
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Title: Chemical Communications
  Other : Chem. Commun.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 52 (94) Sequence Number: - Start / End Page: 13679 - 13682 Identifier: ISSN: 1359-7345
CoNE: https://pure.mpg.de/cone/journals/resource/954928495413