Probing the aglycon promiscuity of an engineered glycosyltransferase

Richard W. Gantt; Randal D. Goff; Gavin J. Williams; Jon S. Thorson

doi:10.1002/anie.200803508

Probing the aglycon promiscuity of an engineered glycosyltransferase

Richard W. Gantt, Randal D. Goff, Gavin J. Williams, Jon S. Thorson

Research output: Contribution to journal › Article › peer-review

119 Scopus citations

Abstract

(Figure Presented) A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes.

Original language	English
Pages (from-to)	8889-8892
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	47
Issue number	46
DOIs	https://doi.org/10.1002/anie.200803508
State	Published - Nov 3 2008

Keywords

Carbohydrates
Enzymes
Glycosides
Glycosylation
Natural products

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.200803508

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AU - Williams, Gavin J.

AU - Thorson, Jon S.

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N2 - (Figure Presented) A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes.

AB - (Figure Presented) A sweet library: Two variants (wild-type (WT) and a triple mutant) of glycosyltransferase (GT) OleD have been shown to catalyze glycosylation of over 70 substrates, formation of O-, S- and N-glycosidic bonds, and iterative glycosylation (see scheme). Identified substrates include nucleophiles not previously known to act in GT reactions and span numerous natural product and therapeutic drug classes.

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KW - Enzymes

KW - Glycosides

KW - Glycosylation

KW - Natural products

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Probing the aglycon promiscuity of an engineered glycosyltransferase

Abstract

Keywords

ASJC Scopus subject areas

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