N-acetillaktozamin sintaza
| N-acetillaktozamin sintaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.90 | ||||||||
| CAS broj | 9054-94-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
N-acetillaktozamin sintaza (EC 2.4.1.90, UDP-galaktoza N-acetilglukozamin beta-D-galaktoziltransferaza, uridin difosfogalaktoza-acetilglukozamin galaktoziltransferaza, beta-1,4-galaktoziltransferaza, acetillaktozamin sintetaza, laktozamin sintaza, laktozamin sintetaza, laktoza sintetaza A protein, N-acetillaktozamin sintetaza, UDP-galaktoza N-acetilglukozamin beta-4-galaktoziltransferaza, UDP-galaktoza-acetilglukozamin galaktoziltransferaza, UDP-galaktoza-N-acetilglukozamin beta-1,4-galaktoziltransferaza, UDP-galaktoza-N-acetilglukozamin galaktoziltransferaza, beta1-4-galaktoziltransferaza, UDP-Gal:N-acetilglukozamin beta1-4-galaktoziltransferaza, beta1-4GalT, NAL sintetaza, UDP-beta-1,4-galaktoziltransferaza, Gal-T, UDP-galaktoza:N-acetilglukozaminide beta1-4-galaktoziltransferaza, UDPgalaktoza:N-acetilglukozaminil(beta1-4)galaktoziltransferaza, beta-N-acetilglukozaminide beta1-4-galaktoziltransferaza, UDP-galaktoza:N-acetil-D-glukozamin 4-beta-D-galaktoziltransferaza) je galaktozil-transferazni enzim sa sistematskim imenom UDP-alfa-D-galaktoza:N-acetil-D-glukozamin 4-beta-D-galaktoziltransferaza.[1][2][3][4][5][6] On je komponenta laktozne sintaze.[7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- UDP-alfa-D-galaktoza + N-acetil-D-glukozamin UDP + N-acetillaktozamin
Ovu reakciju katalizuje komponenta enzima EC 2.4.1.22 (laktozna sintaze), koja je identična sa EC 2.4.1.38 (beta-N-acetilglukozaminil-glikopeptid beta-1,4-galaktoziltransferazom), i enzim iz Goldžijevog aparata životinjskih tkiva.
Vidi još[uredi | uredi kod]
Reference[uredi | uredi kod]
- ↑ Deshmukh, D.S., Bear, W.D. and Soifer, D. (1978). „Isolation and characterization of an enriched Golgi fraction from rat brain”. Biochim. Biophys. Acta 542: 284-295. PMID 99178.
- ↑ Helting, T. and Erbing, B. (1973). „Galactosyl transfer in mouse mastocytoma: purification and properties of N-acetyllactosamine synthetase”. Biochim. Biophys. Acta 293: 94-104. PMID 4631039.
- ↑ Hill, R.L. and Brew, K. (1975). „Lactose synthetase”. Adv. Enzymol. Relat. Areas Mol. Biol. 43: 411-490. PMID 812340.
- ↑ Humphreys-Beher, M.G. (1984). „Isolation and characterization of UDP-galactose:N-acetylglucosamine 4 β-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol”. J. Biol. Chem. 259: 5797-5802. PMID 6201486.
- ↑ Schachter, H., Jabbal, I., Hudgin, R.L., Pinteric, L., McGuire, E.J. and Roseman, S. (1970). „Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction”. J. Biol. Chem. 245: 1090-1100. PMID 4392041.
- ↑ Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda (2002). Handbook of glycosyltransferases and related genes (1st ed izd.). Springer.
- ↑ Webb, Edwin C. (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5.
- ↑ Funderburgh, James L. (2000). „Mini reveiw, Keratan sulfate: structure, biosynthesis, and function”. Glycobiology 10: 951-958. DOI:10.1093/glycob/10.10.951.
Literatura[uredi | uredi kod]
- 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.
- Webb, Edwin C. (1992). Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the nomenclature and classification of enzymes. San Diego: Published for the International Union of Biochemistry and Molecular Biology by Academic Press. ISBN 0-12-227164-5.
- Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda (2002). Handbook of glycosyltransferases and related genes (1st ed izd.). Springer.