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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. Copyright © 2012 Elsevier Ltd. All rights reserved.

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PubMed ID:: 23146438

DOI:: 10.1016/j.cbpa.2012.10.021

ScienceOpen disciplines: Chemistry

Keywords: Animals,Humans,Models, Molecular,N-Acetylglucosaminyltransferases,chemistry,metabolism,Protein Processing, Post-Translational,Substrate Specificity,beta-N-Acetylhexosaminidases

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ScienceOpen disciplines: Chemistry

Keywords: Animals, Humans, Models, Molecular, N-Acetylglucosaminyltransferases, chemistry, metabolism, Protein Processing, Post-Translational, Substrate Specificity, beta-N-Acetylhexosaminidases

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