Probing the aglycon promiscuity of an engineered glycosyltransferase

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

Research output: Contribution to journalArticlepeer-review

117 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 languageEnglish
Pages (from-to)8889-8892
Number of pages4
JournalAngewandte Chemie - International Edition
Volume47
Issue number46
DOIs
StatePublished - Nov 3 2008

Keywords

  • Carbohydrates
  • Enzymes
  • Glycosides
  • Glycosylation
  • Natural products

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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