Laktozilkeramid a-2,3-sijaliltransferaza
| Laktozilkeramid a-2,3-sijaliltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.4.99.9 | ||||||||
| CAS broj | 125752-90-1 | ||||||||
| 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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Laktozilkeramid a-2,3-sijaliltransferaza (EC 2.4.99.9, citidin monofosfoacetilneuraminat-laktozilkeramid alfa2,3- sijaliltransferaza, CMP-acetilneuraminat-laktozilkeramid-sijaliltransferaza, CMP-acetilneuraminska kiselina:laktozilkeramid sijaliltransferaza, CMP-sijalinska kiselina:laktozilkeramid-sijaliltransferaza, citidin monofosfoacetilneuraminat-laktozilkeramid sijaliltransferaza, gangliozid GM3 sintetaza, GM3 sintaza, GM3 sintetaza, SAT 1, CMP-N-acetilneuraminat:laktozilkeramid alfa-2,3-N-acetilneuraminiltransferaza, CMP-N-acetilneuraminat:beta-D-galaktozil-(1->4)-beta-D-glukozil(1<->1)keramid alfa-(2->3)-N-acetilneuraminiltransferaza) je enzim sa sistematskim imenom CMP-N-acetilneuraminat:beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid alfa-(2->3)-N-acetilneuraminiltransferaza.[1][2][3] Ovaj enzim katalizuje sledeću hemijsku reakciju
- CMP-N-acetilneuraminat + beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid CMP + alfa-N-acetilneuraminil-(2->3)-beta-D-galaktozil-(1->4)-beta-D-glukozil-(1<->1)-keramid
Laktoza ne može da deluje kao akceptor.
Reference[uredi | uredi kod]
- ↑ Basu, S., Kaufman, B. and Roseman, S. (1973). „Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain”. J. Biol. Chem. 248: 1388-1394. PMID 4631392.
- ↑ Fishman, P.H., Bradley, R.M. and Henneberry, R.C. (1976). „Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase”. Arch. Biochem. Biophys. 172: 618-626. PMID 4022.
- ↑ Higashi, H., Basu, M. and Basu, S. (1985). „Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain”. J. Biol. Chem. 260: 824-828. PMID 3838172.
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.