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Catalytic promiscuity of glycopeptide N...
Journal article

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 …

Authors

Brieke C; Yim G; Peschke M; Wright GD; Cryle MJ

Journal

Chemical Communications, Vol. 52, No. 94, pp. 13679–13682

Publisher

Royal Society of Chemistry (RSC)

Publication Date

November 17, 2016

DOI

10.1039/c6cc06975d

ISSN

1359-7345