A-1,3-mannosyl-glycoprotein 2-b-N-acetylglucosaminyltransferase
| Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.101 | ||||||||
| CAS no. | 102576-81-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.101, N-acetylglucosaminyltransferase I, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein beta-1,2-N-acetylglucosaminyltransferase, UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N-acetylglucosaminyltransferase I, UDP-N-acetylglucosaminyl:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I, alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase, GnTI) is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction
- UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
R represents the remainder of the N-linked oligosaccharide in the glycoprotein acceptor.
References
- ^ Harpaz, N.; Schachter, H. (1980). "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". J. Biol. Chem. 255 (10): 4885–4893. PMID 6445358.
- ^ Mendicino, J.; Chandrasekaran, E.V.; Anumula, K.R.; Davila, M. (1981). "Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa". Biochemistry. 20 (4): 967–976. doi:10.1021/bi00507a050. PMID 6452163.
- ^ Miyagi, T.; Tsuiki, S. (1981). "Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas". Biochim. Biophys. Acta. 661 (1): 148–157. doi:10.1016/0005-2744(81)90094-2. PMID 6170335.
- ^ Oppenheimer, C.L.; Eckhardt, A.E.; Hill, R.L. (1981). "The nonidentity of porcine N-acetylglucosaminyltransferases I and II". J. Biol. Chem. 256 (22): 11477–11482. PMID 6457827.
- ^ Oppenheimer, C.L.; Hill, R.L. (1981). "Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase". J. Biol. Chem. 256 (2): 799–804. PMID 6450208.
- ^ Schachter, H.; Narasimhan, S.; Gleeson, P.; Vella, G. (1983). "Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type". Methods Enzymol. 98: 98–134. doi:10.1016/0076-6879(83)98143-0. PMID 6366476.
- ^ Vella, G.J.; Paulsen, H.; Schachter, H. (1984). "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". Can. J. Biochem. Cell Biol. 62 (6): 409–417. doi:10.1139/o84-056. PMID 6235906.
- ^ Unligil, U.M.; Zhou, S.; Yuwaraj, S.; Sarkar, M.; Schachter, H.; Rini, J.M. (2000). "X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily". EMBO J. 19 (20): 5269–5280. doi:10.1093/emboj/19.20.5269. PMID 11032794.
External links
- Alpha-1,3-mannosyl-glycoprotein+2-beta-N-acetylglucosaminyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)