Sandbox Reserved 381: Difference between revisions
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== O-GlcNAc Modifications == | == O-GlcNAc Modifications == | ||
O-GlcNAc modification has been described for a large and still increasing number of proteins, many of which are key modulators of cellular signalling. O-GlcNAc modifications are catalysed by a OGT, and are removed by the antagonistic enzyme B-N-acetylglucosaminidase (O-GlcNAcase). The general scheme of O-linked N-acetylglucosamine modification suggests that N-acetylglucosamine is added to serine/threonine (Ser/Thr) residues of target proteins by the enzyme OGT using <scene name='Sandbox_Reserved_381/ | O-GlcNAc modification has been described for a large and still increasing number of proteins, many of which are key modulators of cellular signalling. O-GlcNAc modifications are catalysed by a OGT, and are removed by the antagonistic enzyme B-N-acetylglucosaminidase (O-GlcNAcase). The general scheme of O-linked N-acetylglucosamine modification suggests that N-acetylglucosamine is added to serine/threonine (Ser/Thr) residues of target proteins by the enzyme OGT using <scene name='Sandbox_Reserved_381/Binding_site/2'>UDP-GlcNAc</scene> as substrate. The N-acetylglucosamine group is removed by the antagonistic activity of O-GlcNAcase. <ref>Alexander G, Danilo G. The O-linked N-acetylglucosamine modification in cellular signalling and the immune system. EMBO reports. 2008 June;9:748-753[http://www.nature.com/embor/journal/v9/n8/full/embor2008129.html]</ref> | ||
== Tetanospasmin (TeNT) == | == Tetanospasmin (TeNT) == | ||
