N-acetilneuraminilgalaktozilglukozilkeramid b-1,4-N-acetilgalaktozaminiltransferaza
N-acetilneuraminilgalaktozilglukozilkeramid b-1,4-N-acetilgalaktozaminiltransferaza (EC 2.4.1.165, uridin difosfoacetilgalaktozamin-acetilneuraminil(alfa2->3)galaktozil(beta1->4)glukozil beta1->4-acetilgalaktozaminiltransferaza, UDP-N-acetil-D-galaktozamin:N-acetilneuraminil-2,3-alfa-D-galaktozil-1,4-beta-D-glukozilkeramid beta-1,4-N-acetilgalaktozaminiltransferaza, UDP-N-acetil-D-galaktozamin:N-acetilneuraminil-(2->3)-alfa-D-galaktozil-(1->4)-beta-D-glukozil(1<->1)keramid 4-beta-N-acetilgalaktozaminiltransferaza) je enzim sa sistematskim imenom UDP-N-acetil-D-galaktozamin:N-acetilneuraminil-(2->3)-alfa-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid 4-beta-N-acetilgalaktozaminiltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
| N-acetilneuraminilgalaktozilglukozilkeramid b-1,4-N-acetilgalaktozaminiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.165 | ||||||||
| CAS broj | 109136-50-7 | ||||||||
| 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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- UDP-N-acetil-D-galaktozamin + N-acetilneuraminil-(2->3)-alfa-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid UDP + N-acetil-D-galaktozaminil-(1->4)-beta-N-acetilneuraminil-(2->3)-alfa-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid
Za rad ovog enzima je neophodan Mn2+. Jedino supstance koje sadrže ostatke sijalinske kiseline mogu da deluju kao akceptori. Goveđi fetuin je najbolji poznati akceptor.
Reference
uredi- ↑ Chien, J.-L., Williams, T. and Basu, S. (1973). „Biosynthesis of a globoside-type glycosphingolipid by a β-N-acetylgalactosaminyltransferase from embryonic chicken brain”. J. Biol. Chem. 248: 1778-1785. PMID 4632917.
- ↑ Piller, F., Blanchard, D., Huet, M. and Cartron, J.-P. (1986). „Identification of a α-NeuAc-(2-3)-β-D-galactopyranosyl N-acetyl-β-D-galactosaminyltransferase in human kidney”. Carbohydr. Res. 149: 171-184. PMID 2425965.
- ↑ Takeya, A., Hosomi, O. and Kogure, T. (1987). „Identification and characterization of UDP-GalNAc: NeuAc α2-3Gal β1-4Glc(NAc) β1-4(GalNAc to Gal)N-acetylgalactosaminyltransferase in human blood plasma”. J. Biochem. (Tokyo) 101: 251-259. PMID 3106337.
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.
- 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.