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OGT inhibitors block O-GlcNAc transferase, which attaches a single sugar to intracellular proteins. O-linked β-N-acetylglucosamine (O-GlcNAc) was first reported in 1984 as a modification of lymphocyte proteins. O-GlcNAc transferase (OGT) moves N-acetylglucosamine from uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) onto serine and threonine residues. O-GlcNAcase removes the sugar, so the modification cycles in response to nutrients and stress. OSMI-1 was reported in 2015 as a small molecule that inhibits OGT activity in cells. OSMI-4 came from structure-based optimization of this series in 2018. OSMI-2, OSMI-3 and ST045849 are other OGT inhibitors in this group. UDP-GlcNAc Disodium Salt supplies the donor substrate for enzyme assays.
Synonyms: UDP-α-D-N-Acetylglucosamine Disodium Salt
UDP-GlcNAc Disodium Salt (UDP-α-D-N-Acetylglucosamine Disodium Salt) is a donor substrate of O-GlcNAc transferase (OGT).
