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

10 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

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10.1039/c6cc06975d

Cite this

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title = "Catalytic promiscuity of glycopeptide N-methyltransferases enables bio-orthogonal labelling of biosynthetic intermediates",

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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AU - Brieke, Clara

AU - Yim, Grace

AU - Peschke, Madeleine

AU - Wright, Gerard D.

AU - Cryle, Max J.

PY - 2016/11

Y1 - 2016/11

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84996899124

U2 - 10.1039/c6cc06975d

DO - 10.1039/c6cc06975d

M3 - Article

AN - SCOPUS:84996899124

SN - 1359-7345

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SP - 13679

EP - 13682

JO - Chemical Communications

JF - Chemical Communications

IS - 94

ER -

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

Abstract

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ARC Centre of Excellence in Advanced Molecular Imaging

Australian Synchrotron

Cite this

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

Abstract

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Projects

ARC Centre of Excellence in Advanced Molecular Imaging

Equipment

Australian Synchrotron

Cite this