Structural highlights
Function
OGA_CLOP1 Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
Publication Abstract from PubMed
Posttranslational modification of metazoan nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) is essential, dynamic, and inducible and can compete with protein phosphorylation in signal transduction. Inhibitors of O-GlcNAcase, the enzyme removing O-GlcNAc, are useful tools for studying the role of O-GlcNAc in a range of cellular processes. We report the discovery of nanomolar OGA inhibitors that are up to 900,000-fold selective over the related lysosomal hexosaminidases. When applied at nanomolar concentrations on live cells, these cell-penetrant molecules shift the O-GlcNAc equilibrium toward hyper-O-GlcNAcylation with EC values down to 3 nM and are thus invaluable tools for the study of O-GlcNAc cell biology.
Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases.,Dorfmueller HC, Borodkin VS, Schimpl M, Zheng X, Kime R, Read KD, van Aalten DM Chem Biol. 2010 Nov 24;17(11):1250-5. PMID:21095575[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dorfmueller HC, Borodkin VS, Schimpl M, Zheng X, Kime R, Read KD, van Aalten DM. Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases. Chem Biol. 2010 Nov 24;17(11):1250-5. PMID:21095575 doi:10.1016/j.chembiol.2010.09.014