@article{50512452f41446c2a48c884b59dd9ff8,
title = "Probing the aglycon promiscuity of an engineered glycosyltransferase",
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.",
keywords = "Carbohydrates, Enzymes, Glycosides, Glycosylation, Natural products",
author = "Gantt, \{Richard W.\} and Goff, \{Randal D.\} and Williams, \{Gavin J.\} and Thorson, \{Jon S.\}",
year = "2008",
month = nov,
day = "3",
doi = "10.1002/anie.200803508",
language = "English",
volume = "47",
pages = "8889--8892",
number = "46",
}