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O -GlcNAcase (OGA) is the only enzyme responsible for removing  N -acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in  O -GlcNAc metabolism. However, the structural features of the sugar moiety recognized by human OGA (hOGA) remain unclear. In this study, a set of glycopeptides with modifications on the GlcNAc residue, were prepared in a recombinant full-length human OGT-catalyzed reaction, using chemoenzymatically synthesized UDP-GlcNAc derivatives. The resulting glycopeptides were used to evaluate the substrate specificity of hOGA toward the sugar moiety. This study will provide insights into the exploration of probes for  O -GlcNAc modification, as well as a better understanding of the roles of O-GlcNAc in cellular physiology.

Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety