Many proteins in the eukaryotic cell are modified by O-linked N-acetylglucosamine (O-GlcNAc) on serines and threonines. 1 O-GlcNAcylation has been shown to be important for regulation of the cell cycle, DNA transcription and translation, insulin sensitivity, and protein degradation. 2,3 Misregulation of O-GlcNAcylation is associated with diabetes and Alzheimer’s disease. 2,4,5 Two enzymes are involved in the dynamic cycling of this posttranslational modification, the O-GlcNAc transferase (OGT, classified as CAZY6 family GT41) and O-GlcNAcase (OGA, GH84). PUGNAc (O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate), a nanomolar inhibitor of OGA, has been extensively used to induce and study the effects of raised O-GlcNAc levels in the cell. 7,8 However, PUGNAc is also a potent inhibitor of the human lysosomal hexosaminidases HexA and HexB, inactivation of which has been associated with the Tay-Sachs an
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