75716-11-9Relevant 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.
supporting information; experimental part, p. 8889 - 8892 (2009/05/26)
(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.
A mild and selective method for cleavage of O-acetyl groups with dibutyltin oxide
Liu, Hong-Min,Yan, Xuebin,Li, Wen,Huang, Conghai
, p. 1763 - 1767 (2007/10/03)
A mild and efficient neutral method for the cleavage of O-acetyl groups with dibutyltin oxide has been developed. This method is especially useful in the synthesis of glycosides containing base- or acid-sensitive multifunctional groups.
