Target type: molecularfunction
Catalysis of the reaction: 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl/L-threonyl-[protein] + H2O = L-seryl//L-threonyl-[protein] + N-acetyl-D-glucosamine. [EC:3.2.1.169]
This enzyme catalyzes the hydrolysis of the N-acetyl-D-glucosamine moiety from the O-linked N-acetyl-D-glucosamine (GlcNAc) modification on serine or threonine residues of proteins. This modification, known as O-GlcNAcylation, is a dynamic and reversible post-translational modification that plays crucial roles in various cellular processes, including transcription, signal transduction, and protein trafficking. The enzyme specifically removes the terminal GlcNAc residue from the O-GlcNAc-modified protein, thereby de-glycosylating the substrate and potentially altering its function. It is involved in the regulation of the cellular O-GlcNAc cycle, which is a balance between O-GlcNAc transferase (OGT) activity, responsible for adding GlcNAc to proteins, and O-GlcNAcase (OGA) activity, responsible for removing it. OGA plays a crucial role in maintaining cellular homeostasis by regulating protein function and signaling pathways through its O-GlcNAc de-glycosylation activity.'
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Protein | Definition | Taxonomy |
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Protein O-GlcNAcase | A protein O-GlcNAcase that is encoded in the genome of human. [PRO:DNx, UniProtKB:O60502] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
2-acetamido-1,5-imino-1,2,5-trideoxy-d-glucitol | 2-acetamido-1,5-imino-1,2,5-trideoxy-D-glucitol: structure given in first source | ||
n-acetylglucosamine thiazoline | N-acetylglucosamine thiazoline: an analog of the oxazolinium bicyclic intermediate leading from N-acetylglucosamine to 1,6-anhydro-N-acetylmuramic acid | ||
n-acetylglucosaminono-1,5-lactone o-(phenylcarbamoyl)oxime | N-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oxime: structure given in first source | ||
thiamet g |