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Evaluation of the Chemical Reporter Analog PNP-6AzGlcNAc as an O-GlcNAcase Substrate
김은주,Michelle R. Bond,남길수,John A. Hanover 대한화학회 2017 Bulletin of the Korean Chemical Society Vol.38 No.2
6-Azido-6-deoxy-N-acetylglucosamine (6AzGlcNAc) was recently introduced as a new selective metabolic chemical reporter (MCR) for labeling O-GlcNAc-modified proteins in cells. To investigate whether O-6AzGlcNAc is readily cleaved by O-GlcNAcase (OGA), the enzyme responsible for removing the O-GlcNAc modification, we synthesized PNP-6AzGlcNAc. This analog mimics O-GlcNAc and can be used in vitro to define the kinetic parameters for OGA thereby defining whether O-6AzGlcNAc can be employed as an appropriate tool to monitor O-GlcNAc dynamics in cells. Both PNP-6AzGlcNAc and PNP-GlcNAc were efficiently hydrolyzed by OGA with similar kinetics suggesting that an azido-modification at the GlcNAc C6 position does not significantly interfere with the β-hexosaminidase activity of OGA.
Kim, Eun J.,Abramowitz, Lara K.,Bond, Michelle R.,Love, Dona C.,Kang, Dong W.,Leucke, Hans F.,Kang, Dae W.,Ahn, Jong-Seog,Hanover, John A. American Chemical Society 2014 Bioconjugate chemistry Vol.25 No.6
<P/><P>The dynamic glycosylation of serine/threonine residues on nucleocytoplasmic proteins with a single <I>N</I>-acetylglucosamine (<I>O</I>-GlcNAcylation) is critical for many important cellular processes. Cellular <I>O</I>-GlcNAc levels are highly regulated by two enzymes: <I>O</I>-GlcNAc transferase (OGT) is responsible for GlcNAc addition and <I>O</I>-GlcNAcase (OGA) is responsible for removal of the sugar. The lack of a rapid and simple method for monitoring OGT activity has impeded the efficient discovery of potent OGT inhibitors. In this study we describe a novel, single-well OGT enzyme assay that utilizes 6 × His-tagged substrates, a chemoselective chemical reaction, and unpurified OGT. The high-throughput Ni-NTA Plate OGT Assay will facilitate discovery of potent OGT-specific inhibitors on versatile substrates and the characterization of new enzyme variants.</P>