Target type: biologicalprocess
The chemical reactions and pathways involving glycoproteins, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. [GOC:go_curators, ISBN:0198506732]
Glycoprotein metabolic process encompasses a series of intricate biochemical reactions that modify proteins by attaching carbohydrate moieties, known as glycans. These modifications, collectively referred to as glycosylation, play pivotal roles in determining protein structure, function, and localization within cells and organisms. Glycosylation is a highly regulated and complex process involving a multitude of enzymes, including glycosyltransferases, glycosidases, and sugar nucleotide synthases, acting in a coordinated manner. Glycosyltransferases catalyze the addition of specific sugar residues to the protein backbone, while glycosidases remove sugar residues. Sugar nucleotide synthases generate the activated sugar donors required for glycosylation. The process begins in the endoplasmic reticulum (ER), where N-linked glycosylation, the attachment of glycans to asparagine residues, takes place. This initial glycosylation event is crucial for protein folding and stability. As proteins translocate to the Golgi apparatus, further modifications occur, including the trimming and processing of glycans, as well as the addition of complex sugar structures. The resulting glycoproteins exhibit diverse biological functions, including cell-cell recognition, signal transduction, immune response, and protein trafficking. Dysregulation of glycoprotein metabolic processes can lead to a range of diseases, including cancer, diabetes, and autoimmune disorders.'
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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) |
Protein-serine O-palmitoleoyltransferase porcupine | A protein-serine O-palmitoleoyltransferase porcupine that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9H237] | 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-(6-methyl-1,3-benzothiazol-2-yl)-2-[(4-oxo-3-phenyl-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl)thio]acetamide | organic heterobicyclic compound; organonitrogen heterocyclic compound; organosulfur heterocyclic compound | ||
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 | ||
lgk974 | LGK974 : A carboxamide, the structure of which is that of acetamide substituted on carbon by a 2',3-dimethyl-2,4'-bipyridin-5-yl group and on nitrogen by a 5-(pyrazin-2-yl)pyridin-2-yl group. It is a highly potent, selective and orally bioavailable Porcupine inhibitor (a Wnt signalling inhibitor). LGK974: a potent and specific small-molecule inhibitor of Porcupine (PORCN) acyltransferase | bipyridines; pyrazines; pyridines; secondary carboxamide | Wnt signalling inhibitor |
wnt-c59 | 2-(4-(2-methylpyridin-4-yl)phenyl)-N-(4-(pyridin-3-yl)phenyl)acetamide: a PORCN acyltransferase inhibitor; structure in first source | ||
thiamet g |