Galaktozid 2-a-L-fukoziltransferaza
| Galaktozid 2-a-L-fukoziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.1.69 | ||||||||
| CAS broj | 56093-23-3 | ||||||||
| 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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Galaktozid 2-a-L-fukoziltransferaza (EC 2.4.1.69, krvno grupna H alfa-2-fukoziltransferaza, guanozin difosfofukoza-galaktozid 2-L-fukoziltransferaza, alfa-(1->2)-L-fukoziltransferaza, alfa-2-fukoziltransferaza, alfa-2-L-fukoziltransferaza, od krvno-grupne supstance H zavisna fukoziltransferaza, guanozin difosfofukoza-glikoprotein 2-alfa-fukoziltransferaza, guanozin difosfofukoza-laktoza fukoziltransferaza, GDP fukoza-laktoza fukoziltransferaza, guanozin difosfo-L-fukoza-laktoza fukoziltransferaza, guanozin difosfofukoza-beta-D-galaktozil-alfa-2-L-fukoziltransferaza, guanozin difosfofukoza-galaktozilacetilglukozaminilgalaktozilglukozilkeramid alfa-L-fukoziltransferaza, guanozin difosfofukoza-glikoprotein 2-alfa-L-fukoziltransferaza, H-gen-kodirana beta-galaktozid alfa 1->2 fukoziltransferaza, sekretorska tip beta-galaktozid alfa 1->2 fukoziltransferaza, beta-galaktozid alfa 1->2 fukoziltransferaza, GDP-L-fukoza:laktoza fukoziltransferaza, GDP-beta-L-fukoza:beta-D-galaktozil-R 2-alfa-L-fukoziltransferaza) je enzim sa sistematskim imenom GDP-beta-L-fukoza:beta-D-galaktozil-(1->3)-N-acetil-beta-D-glukozaminil-(1->3)-beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid 2-alfa-L-fukoziltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- GDP-beta-L-fukoza + beta-D-galaktozil-(1->3)-N-acetil-beta-D-glukozaminil-(1->3)-beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid GDP + alfa-L-fukozil-(1->2)-beta-D-galaktozil-(1->3)-N-acetil-beta-D-glukozaminil-(1->3)-beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid
Slobodna laktoza može da bude akceptor.
Reference[uredi | uredi kod]
- ↑ Basu, S., Basu, M. and Chien, J.L. (1975). „Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen”. J. Biol. Chem. 250: 2956-2962. PMID 804484.
- ↑ Beyer, T.A. and Hill, R.L. (1980). „Enzymatic properties of the β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland”. J. Biol. Chem. 255: 5373-5379. PMID 7372640.
- ↑ Beyer, T.A., Sadler, J.E. and Hill, R.L. (1980). „Purification to homogeneity of H blood group β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland”. J. Biol. Chem. 255: 5364-5372. PMID 6246105.
- ↑ Grollman, A.P. (1966). „GDP-L-fucose:lactose fucosyltransferase from mammary gland”. Methods Enzymol. 8: 351-353.
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.