Work

Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase

Year: 2008

Type: article

Abstract: 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.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.200803508

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

Institution: University of Wisconsin–Madison

Language: English

Topic: Carbohydrate Chemistry and Synthesis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of Allergy and Infectious Diseases

Awards: UWCCC National Cooperative Drug Discovery Group for Can*, G1956070232, In Vitro Glycorandomization of Natural Products, In Vitro Glycorandomization of Natural Products