Base-modified donor analogues reveal novel dynamic features of a glycosyltransferase.

ABSTRACT: Glycosyltransferases (GTs) are enzymes that are involved, as Nature's "glycosylation reagents," in many fundamental biological processes including cell adhesion and blood group biosynthesis. Although of similar importance to that of other large enzyme families such as protein kinases and proteases, the undisputed potential of GTs for chemical biology and drug discovery has remained largely unrealized to date. This is due, at least in part, to a relative lack of GT inhibitors and tool compounds for structural, mechanistic, and cellular studies. In this study, we have used a novel class of GT donor analogues to obtain new structural and enzymological information for a representative blood group GT. These analogues interfere with the folding of an internal loop and the C terminus, which are e

SUBMITTER: Jorgensen R 

PROVIDER: S-EPMC3764824 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature