A-1,6-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza
A-1,6-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza (EC 2.4.1.143, N-acetilglukozaminiltransferaza II, N-glikozil-oligosaharid-glikoprotein N-acetilglukozaminiltransferaza II, acetilglukozaminiltransferaza II, uridin difosfoacetilglukozamin-manozid alfa1->6-acetilglukozaminiltransferaza, uridin difosfoacetilglukozamin-alfa-1,6-manozilglikoprotein beta-1-2-N-acetilglukozaminiltransferaza, uridin difosfoacetilglukozamin-alfa-D-manozid beta1-2-acetilglukozaminiltransferaza, UDP-GlcNAc:manozid alfa1-6 acetilglukozaminiltransferaza, alfa-1,6-manozil-glikoprotein beta-1,2-N-acetilglukozaminiltransferaza, GnTII) je enzim sa sistematskim imenom UDP-N-acetil-D-glukozamin:6-(alfa-D-manozil)-beta-D-manozil-glikoprotein 2-beta-N-acetil-D-glukozaminiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
A-1,6-manozil-glikoprotein 2-b-N-acetilglukozaminiltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.4.1.143 | ||||||||
CAS broj | 105913-04-0 | ||||||||
Baze podataka | |||||||||
IntEnz | IntEnz pregled | ||||||||
BRENDA | BRENDA pristup | ||||||||
ExPASy | NiceZyme pregled | ||||||||
KEGG | KEGG pristup | ||||||||
MetaCyc | metabolički put | ||||||||
PRIAM | profil | ||||||||
Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- UDP-N-acetil-D-glukozamin + 6-(alfa-D-manozil)-beta-D-manozil-R UDP + 6-(2-[N-acetil-beta-D-glukozaminil]-alfa-D-manozil)-beta-D-manozil-R
R označava ostatak N-vezanog oligosaharida u glikoproteinskom akceptoru.
Reference
uredi- ^ Bendiak, B. & Schacter, H. (1987). „Control of glycoprotein synthesis. Purification of UDP-N-acetylglucosamine:α-D-mannoside β1-2 N-acetylglucosaminyltransferase II from rat liver”. J. Biol. Chem. 262: 5775—5783. PMID 2952644.
- ^ 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: 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.
- ^ 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.
- ^ 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.
- ^ Bendiak, B. & Schachter, H. (1987). „Control of glycoprotein synthesis. Kinetic mechanism, substrate specificity, and inhibition characteristics of UDP-N-acetylglucosamine:α-D-mannoside β-1-2 N-acetylglucosaminyltransferase II from rat liver”. J. Biol. Chem. 262: 5784—5790. PMID 2952644.
Literatura
uredi- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- 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.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
uredi- Alpha-1,6-mannosyl-glycoprotein+2-beta-N-acetylglucosaminyltransferase na US National Library of Medicine Medical Subject Headings (MeSH)