B-galaktozid a-2,6-sijaliltransferaza
| B-galaktozid a-2,6-sijaliltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.99.1 | ||||||||
| CAS broj | 9075-81-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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B-galaktozid a-2,6-sijaliltransferaza (EC 2.4.99.1, CMP-N-acetilneuraminat:beta-D-galaktozil-1,4-N-acetil-beta-D-glukozamin alfa-2,6-N-acetilneuraminiltransferaza) je enzim sa sistematskim imenom CMP-N-acetilneuraminat:beta-D-galaktozil-(1->4)-N-acetil-beta-D-glukozamin alfa-(2->6)-N-acetilneuraminiltransferaza.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju
- CMP-N-acetilneuraminat + beta-D-galaktozil-(1->4)-N-acetil-beta-D-glukozamin CMP + alfa-N-acetilneuraminil-(2->6)-beta-D-galaktozil-(1->4)-N-acetil-beta-D-glukozamin
Terminalni beta-D-galaktozilni ostatak oligosaharida glikoproteina, kao i laktoza, mogu da deluju kao akceptori.
Reference
- ↑ Bartholomew, B.A., Jourdian, G.W. and Roseman, S. (1973). „The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum”. J. Biol. Chem. 248: 5751-5762. PMID 4723915.
- ↑ Hickman, J., Ashwell, G., Morell, A.G., van der Hamer, C.J.A. and Scheinberg, I.H. (1970). „Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin”. J. Biol. Chem. 245: 759-766. PMID 4313609.
- ↑ Paulson, J.C., Beranek, W.E. and Hill, R.L. (1977). „Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose”. J. Biol. Chem. 252: 2356-2362. PMID 849932.
- ↑ 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.
- ↑ Spiro, M.H. and Spiro, R.G. (1968). „Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase”. J. Biol. Chem. 243: 6520-6528. PMID 5726897.
Literatura
- 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.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Vanjske veze
- MeSH Beta-galactoside+alpha-2,6-sialyltransferase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
