40656-65-3Relevant academic research and scientific papers
Probing the aglycon promiscuity of an engineered glycosyltransferase
Gantt, Richard W.,Goff, Randal D.,Williams, Gavin J.,Thorson, Jon S.
, p. 8889 - 8892 (2008)
(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.
