ABSTRACT
The general mechanism for enzymatic hydrolysis of glycosides has been studied for a number of glycosidases and the topic has been reviewed. The relative ease of glycoside hydrolysis is partly due to the ability of the oxygen to act as a leaving group when protonated. C-Glycosides are well suited to serve as delivery mechanisms for these types of intermediates since the sugars can bind in certain enzyme active sites and the carbon chain is robust enough to tolerate the required chemistry to install the carbene precursor. The C-glycoside serves as a stable analog that cannot undergo enzymatic cleavage and the required conformational change required for glycosyl transfer. Lehmann and co-workers have also used the C-glycoside disaccharide 69 as an affinity label for Immunoglobulin A X24. The bioisosteric acid C-glycosides do not seem to offer any therapeutic advantage over the phosphorylated O-glycosides.
