Alfa-1,3-mannosil-glicoproteina 2-beta-N-acetilglucosaminiltransferasi
enzima
La alfa-1,3-mannosil-glicoproteina 2-beta-N-acetilglucosaminiltransferasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione:
| alfa-1,3-mannosil-glicoproteina 2-beta-N-acetilglucosaminiltransferasi | |
|---|---|
 Puoi caricare tu un'immagine dell'enzima (se disponibile) cercandola qui e seguendo le istruzioni. Grazie! | |
| Numero EC | 2.4.1.101 |
| Classe | Transferasi |
| Nome sistematico | |
| UDP-N-acetil-D-glucosammina:3-(α-D-mannosil)-β-D-mannosil-glicoproteina 2-β-N-acetil-D-glucosamminiltransferasi | |
| Altri nomi | |
| N-acetilglucosamminiltransferasi I; N-glicosil-oligosaccaride-glicoproteina N-acetilglucosamminiltransferasi I; uridina difosfoacetilglucosammina-α-1,3-mannosilglicoproteina β-1,2-N-acetilglucosamminiltransferasi; UDP-N-acetilglucosamminil:α-1,3-D-mannoside-β-1,2-N-acetilglucosamminiltransferasi I; UDP-N-acetilglucosamminil:α-3-D-mannoside β-1,2-N-acetilglucosamminiltransferasi I; α-1,3-mannosil-glicoproteina β-1,2-N-acetilglucosamminiltransferasi; GnTI | |
| Banche dati | BRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum) |
| Fonte: IUBMB | |
- UDP-N-acetil-D-glucosammina + 3-(α-D-mannosil)-β-D-mannosil-R ⇄ UDP + 3-(2-[N-acetil-β-D-glucosamminil]-α-D-mannosil)-β-D-mannosil-R
R rappresenta il resto dell'oligosaccaride legato all'N nell'accettore della glicoproteina. Da notare che l'enzima agisce prima delle N-acetilglucosaminiltransferasi II (numero EC 2.4.1.143[1]), III (numero EC 2.4.1.144[2]), IV (numero EC 2.4.1.145[3]), V (numero EC 2.4.1.155[4]), VI (numero EC 2.4.1.201[5])[6]
Note
modifica- ^ (EN) 2.4.1.143, in ExplorEnz — The Enzyme Database, IUBMB.
- ^ (EN) 2.4.1.144, in ExplorEnz — The Enzyme Database, IUBMB.
- ^ (EN) 2.4.1.145, in ExplorEnz — The Enzyme Database, IUBMB.
- ^ (EN) 2.4.1.155, in ExplorEnz — The Enzyme Database, IUBMB.
- ^ (EN) 2.4.1.201, in ExplorEnz — The Enzyme Database, IUBMB.
- ^ Diagram
Bibliografia
modifica- Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M., X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily, in EMBO J., vol. 19, 2000, pp. 5269–5280, Entrez PubMed 11032794.
- Vella, G.J., Paulsen, H. and Schachter, H., Control of glycoprotein synthesis. IX. A terminal Man alphal-3Man β1- sequence in the substrate is the minimum requirement for UDP-N-acetyl-D-glucosamine: α-D-mannoside (GlcNAc to Man α1-3) β2-N-acetylglucosaminyltransferase I, in Can. J. Biochem. Cell Biol., vol. 62, 1984, pp. 409–417, Entrez PubMed 6235906.
- Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G., Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type, in Methods Enzymol., vol. 98, 1983, pp. 98–134, Entrez PubMed 6366476.
- Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L., The nonidentity of porcine N-acetylglucosaminyltransferases I and II, in J. Biol. Chem., vol. 256, 1981, pp. 11477–11482, Entrez PubMed 6457827.
- Oppenheimer, C.L. and Hill, R.L., Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase, in J. Biol. Chem., vol. 256, 1981, pp. 799–804, Entrez PubMed 6450208.
- Miyagi, T. and Tsuiki, S., Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas, in Biochim. Biophys. Acta, vol. 661, 1981, pp. 148–157, Entrez PubMed 6170335.
- Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M., Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa, in Biochemistry, vol. 20, 1981, pp. 967–976, Entrez PubMed 6452163.
- Harpaz, N. and Schachter, H., Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:α-D-mannoside β2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity, in J. Biol. Chem., vol. 255, 1980, pp. 4885–4893, Entrez PubMed 6445358.
