A-1,3-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza
| A-1,3-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.101 | ||||||||
| CAS broj | 102576-81-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
A-1,3-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza (EC 2.4.1.101, N-acetilglukozaminiltransferaza I, N-glikozil-oligosaharid-glikoprotein N-acetilglukozaminiltransferaza I, uridin difosfoacetilglukozamin-alfa-1,3-manozilglikoprotein beta-1,2-N-acetilglukozaminiltransferaza, UDP-N-acetilglukozaminil:alfa-1,3-D-manozid-beta-1,2-N-acetilglukozaminiltransferaza I, UDP-N-acetilglukozaminil:alfa-3-D-manozid beta-1,2-N-acetilglukozaminiltransferaza I, alfa-1,3-manozil-glikoprotein beta-1,2-N-acetilglukozaminiltransferaza, GnTI) je enzim sa sistematskim imenom UDP-N-acetil-D-glukozamin:3-(alfa-D-manozil)-beta-D-manozil-glikoprotein 2-beta-N-acetil-D-glukozaminiltransferaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- UDP-N-acetil-D-glukozamin + 3-(alfa-D-manozil)-beta-D-manozil-R UDP + 3-(2-[N-acetil-beta-D-glukozaminil]-alfa-D-manozil)-beta-D-manozil-R
R predstavlja ostatak N-vezanog oligosaharida u glikoproteinskom akceptoru.
- ↑ Harpaz, N. and 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: 4885-4893. PMID 6445358.
- ↑ Mendicino, J., Chandrasekaran, E.V., Anumula, K.R. and Davila, M. (1981). „Isolation and properties of α-D-mannose:β-1,2-N-acetylglucosaminyltransferase from trachea mucosa”. Biochemistry 20: 967-976. PMID 6452163.
- ↑ Miyagi, T. and Tsuiki, S. (1981). „Studies on UDP-N-acetylglucosamine : α-mannoside β-N-acetylglucosaminyltransferase of rat liver and hepatomas”. Biochim. Biophys. Acta 661: 148-157. PMID 6170335.
- ↑ Oppenheimer, C.L., Eckhardt, A.E. and Hill, R.L. (1981). „The nonidentity of porcine N-acetylglucosaminyltransferases I and II”. J. Biol. Chem. 256: 11477-11482. PMID 6457827.
- ↑ Oppenheimer, C.L. and Hill, R.L. (1981). „Purification and characterization of a rabbit liver α1→3 mannoside β1→2 N-acetylglucosaminyltransferase”. J. Biol. Chem. 256: 799-804. PMID 6450208.
- ↑ Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. (1983). „Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type”. Methods Enzymol. 98: 98-134. PMID 6366476.
- ↑ Vella, G.J., Paulsen, H. and 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: 409-417. PMID 6235906.
- ↑ Unligil, U.M., Zhou, S., Yuwaraj, S., Sarkar, M., Schachter, H. and Rini, J.M. (2000). „X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily”. EMBO J. 19: 5269-5280. PMID 11032794.
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- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
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