title: O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation.
abstract: The addition of N-acetylglucosamine (GlcNAc) O-linked to serine and threonine residues of proteins is known as O-GlcNAc. This post-translational modification is found within multicellular eukaryotes on hundreds of nuclear and cytoplasmic proteins. O-GlcNAc transferase (OGT) installs O-GlcNAc onto target proteins and O-GlcNAcase (OGA) removes O-GlcNAc. Their combined action makes O-GlcNAc reversible and serves to regulate cellular O-GlcNAc levels. Here I review select recent literature on the catalytic mechanism of these enzymes and studies on the molecular basis by which these enzymes identify and process their substrates. Molecular level understanding of how these enzymes work, and the basis for their specificity, should aid understanding how O-GlcNAc contributes to diverse cellular processes ranging from cellular signaling through to transcriptional regulation.
authors.affiliation: Department of Chemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6, Canada. dvocadlo@sfu.ca
authors.forename: David J
authors.initials: DJ
authors.lastname: Vocadlo
mesh_terms: D000818:Animals; D006801:Humans; D008958:Models, Molecular; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity; D001619:beta-N-Acetylhexosaminidases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase; C110628:hexosaminidase C; D001619:beta-N-Acetylhexosaminidases