Endo-alfa-sijalidaza
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Endo-alfa-sijalidaza | |||||||||
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Identifikatori | |||||||||
EC broj | 3.2.1.129 | ||||||||
CAS broj | 91195-87-8 | ||||||||
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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Endo-alfa-sijalidaza (EC 3.2.1.129, endo-N-acilneuraminidaza, endoneuraminidaza, endo-N-acetilneuraminidaza, poli(alfa-2,8-sijalozil) endo-N-acetilneuraminidaza, poli(alfa-2,8-sijalozid) alfa-2,8-sijalozilhidrolaza, endosijalidaza, endo-N) je enzim sa sistematskim imenom polisijalozid (2->8)-alfa-sijalozilhidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- Endohidroliza (2->8)-alfa-sijalozil veza u oligo- ili poli(sijaliskoj) kiselini
Dejstvo ovog enzima je ograničeno na acetilisane supstrate.
- ↑ Finne, J., Mäkelä, P.H. (1985). „Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid”. J. Biol. Chem. 260: 1265-1270. PMID 3968060.
- ↑ Hallenbeck, P.C., Vimr, E.R., Yu, F., Bassler, B. and Troy, F.A. (1987). „Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-α-2,8-sialosyl carbohydrate units”. J. Biol. Chem. 262: 3553-3561. PMID 3546309.
- ↑ Kitakima, K., Inoue, S., Inoue, Y. and Troy, F.A. (1988). „Use of a bacteriophage-derived endo-N-acetylneuraminidase and an equine antipolysialyl antibody to characterize the polysialyl residues in salmonid fish egg polysialoglycoproteins. Substrate and immunospecificity studies”. J. Biol. Chem. 263: 18269-18276. PMID 3142874.
- ↑ Kwiatkowski, B., Boscheck, B., Thicle, H. and Stirm, S. (1982). „Endo-N-acetylneuraminidase associated with bacteriophage particles”. J. Virol. 43: 697-704. PMID 7109038.
- ↑ Pelkonen, S., Pelkonen, J. and Finne, J. (1989). „Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins”. J. Virol. 65: 4409-4416. PMID 2778882.
- ↑ Tombinson, S. and Taylor, P.W. (1985). „Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide”. J. Virol. 55: 374-378. PMID 3894684.
- ↑ Cabezas, J.A. (1991). „Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase”. Biochem. J. 278: 311-312. PMID 1883340.
- 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.