Premium
Probing the Aglycon Promiscuity of an Engineered Glycosyltransferase
Author(s) -
Gantt Richard W.,
Goff Randal D.,
Williams Gavin J.,
Thorson Jon S.
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200803508
Subject(s) - glycosyltransferase , glycosylation , mutant , chemistry , information retrieval , computer science , computational biology , stereochemistry , biochemistry , biology , gene
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.