Probing synergy between two catalytic strategies in the glycoside hydrolase O-GlcNAcase using multiple linear free energy relationships

…, MS Macauley, IH Williams, DJ Vocadlo

Index: Greig, Ian R.; Macauley, Matthew S.; Williams, Ian H.; Vocadlo, David J. Journal of the American Chemical Society, 2009 , vol. 131, # 37 p. 13415 - 13422

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Citation Number: 25

Abstract

Human O-GlcNAcase plays an important role in regulating the post-translational modification of serine and threonine residues with β-O-linked N-acetylglucosamine monosaccharide unit (O-GlcNAc). The mechanism of O-GlcNAcase involves nucleophilic participation of the 2-acetamido group of the substrate to displace a glycosidically linked leaving group. The tolerance of this enzyme for variation in substrate structure has ...