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

doi:10.1039/c6cc06975d

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 journal › Article › Other › peer-review

3 Citations (Scopus)

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 language	English
Pages (from-to)	13679-13682
Number of pages	4
Journal	Chemical Communications
Volume	52
Issue number	94
DOIs	https://doi.org/10.1039/c6cc06975d
Publication status	Published - Nov 2016

Cite this

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. https://doi.org/10.1039/c6cc06975d

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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Brieke, C, Yim, G, Peschke, M, Wright, GD & Cryle, MJ 2016, 'Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates', Chemical Communications, vol. 52, no. 94, pp. 13679-13682. https://doi.org/10.1039/c6cc06975d

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 journal › Article › Other › peer-review

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