CHEBI:67168 - UDP-N-acetyl-α-D-galactosamine

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ChEBI Name UDP-N-acetyl-α-D-galactosamine ChEBI ID CHEBI:67168 ChEBI ASCII Name UDP-N-acetyl-alpha-D-galactosamine Definition A UDP-N-acetyl-D-galactosamine in which the anomeric centre of the galactosamine moiety has α-configuration. Stars This entity has been manually annotated by the ChEBI Team. Secondary ChEBI IDs CHEBI:46285 Supplier Information ZINC000008551132 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C17H27N3O17P2 Net Charge 0 Average Mass 607.35370 Monoisotopic Mass 607.08157 InChI InChI=1S/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11+,12-,13-,14-,15-,16-/m1/s1 InChIKey LFTYTUAZOPRMMI-NESSUJCYSA-N SMILES CC(=O)N[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1ccc(=O)[nH]c1=O Metabolite of Species Details Homo sapiens (NCBI:txid9606) See: PubMed Roles Classification Biological Role(s): human metabolite Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens). View more via ChEBI Ontology ChEBI Ontology Outgoing UDP-N-acetyl-α-D-galactosamine (CHEBI:67168) has role human metabolite (CHEBI:77746) UDP-N-acetyl-α-D-galactosamine (CHEBI:67168) is a UDP-N-acetyl-D-galactosamine (CHEBI:16650) UDP-N-acetyl-α-D-galactosamine (CHEBI:67168) is conjugate acid of UDP-N-acetyl-α-D-galactosamine(2−) (CHEBI:67138) Incoming UDP-N-acetyl-α-D-galactosamine(2−) (CHEBI:67138) is conjugate base of UDP-N-acetyl-α-D-galactosamine (CHEBI:67168) IUPAC Name uridine 5'-[3-(2-acetamido-2-deoxy-α-D-galactopyranosyl) dihydrogen diphosphate] Synonyms Sources (2R,3R,4R,5R,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate (non-preferred name) PDBeChem UDP-GalNac ChEBI URIDINE-DIPHOSPHATE-N-ACETYLGALACTOSAMINE PDBeChem Manual Xrefs Databases 22161 ChemSpider C00203 KEGG COMPOUND G10611 KEGG GLYCAN HMDB0000304 HMDB UD2 PDBeChem UDP-N-ACETYL-GALACTOSAMINE MetaCyc View more database links Registry Numbers Types Sources 7277-98-7 CAS Registry Number ChemIDplus 78983 Reaxys Registry Number Reaxys Citations Ten Hagen KG, Fritz TA, Tabak LA (2003) All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 13, 1R-16R [PubMed:12634319] [show Abstract] Mucin-type linkages (GalNAcalpha1-O-Ser/Thr) are initiated by a family of glycosyltransferases known as the UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases, EC 2.4.1.41). These enzymes transfer GalNAc from the sugar donor UDP-GalNAc to serine and threonine residues, forming an alpha anomeric linkage. Despite the seeming simplicity of ppGaNTase catalytic function, it is estimated on the basis of in silico analysis that there are 24 unique ppGaNTase human genes. ppGaNTase isoforms display tissue-specific expression in adult mammals as well as unique spatial and temporal patterns of expression during murine development. In vitro assays suggest that a subset of the ppGaNTases have overlapping substrate specificities, but at least two ppGaNTases (ppGaNTase-T7 and -T9 [now designated -T10]) appear to require the prior addition of GalNAc to a synthetic peptide before they can catalyze sugar transfer to this substrate. Site-specific O-glycosylation by several ppGaNTases is influenced by the position and structure of previously added O-glycans. Collectively, these observations argue in favor of a hierarchical addition of core GalNAc residues to the apomucin. Various forms of O-glycan pathobiology may be reexamined in light of the existence of an extensive ppGaNTase family of enzymes. Recent work has demonstrated that at least one ppGaNTase isoform is required for normal development in Drosophila melanogaster. Structural insights will no doubt lead to the development of isoform-specific inhibitors. Such tools will prove valuable to furthering our understanding of the functional roles played by O-glycans. Porowska H, Paszkiewicz-Gadek A, Gindzieński A (1999) Activity of partially purified UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase with different peptide acceptors. Acta biochimica Polonica 46, 365-370 [PubMed:10547037] [show Abstract] As part of investigations on the role of the UDP-GalNAc-ribosome complex in the initial O-glycosylation of proteins, we have isolated from porcine gastric mucosa GalNAc-transferase, mucin and apomucin, and its three fractions containing carbohydrate in the amounts: I - 1.6%, II - 0.65% and III - 0.00% (wt/wt) of apomucin mass. Amino acid analysis showed that fractions I and II contained slightly higher amounts of serine and threonine as compared to native mucin and apomucin. The short peptide Pro-Thr-Ser-Ser-Pro-Ile-Ser-Thr was the most effectively glycosylated. Our apomucin preparations are also good acceptors of GalNAc and can be used for testing of O-glycosylation in vitro. GREGOIRE J, LIMOZIN N, GREGOIRE J (1960) [On the presence of uridine diphosphate-N-acetylgalactosamine in the thyroid glands of cattle and sheep]. Comptes rendus hebdomadaires des seances de l'Academie des sciences 250, 2290-2292 [PubMed:13851695] Last Modified 14 February 2017