Heparanaza
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| Heparanaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.166 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Heparanaza (EC 3.2.1.166, Hpa1 heparanaza, Hpa1, heparanaza 1, heparanaza-1, C1A heparanaza, HPSE) je enzim sa sistematskim imenom heparan sulfat N-sulfo-D-glukozamin endoglukanaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- endohidroliza (1->4)-beta-D-glikozidnih veza heparan sulfatnih lanaca u heparan sulfatnom proteoglikanu
Heparanaza razlaže veze između glukuronsko kiselinskih jedinica i N-sulfo glukozaminskih jedinica koje nose bilo 3-O-sulfo ili 6-O-sulfo grupe.
Reference[uredi | uredi kod]
- ↑ Bame, K.J. (2001). „Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans”. Glycobiology 11: 91R-98R. PMID 11445547.
- ↑ Peterson, S.B. and Liu, J. (2010). „Unraveling the specificity of heparanase utilizing synthetic substrates”. J. Biol. Chem. 285: 14504-14513. PMID 20181948.
- ↑ Pikas, D.S., Li, J.P., Vlodavsky, I. and Lindahl, U. (1998). „Substrate specificity of heparanases from human hepatoma and platelets”. J. Biol. Chem. 273: 18770-18777. PMID 9668050.
- ↑ Okada, Y., Yamada, S., Toyoshima, M., Dong, J., Nakajima, M. and Sugahara, K. (2002). „Structural recognition by recombinant human heparanase that plays critical roles in tumor metastasis. Hierarchical sulfate groups with different effects and the essential target disulfated trisaccharide sequence”. J. Biol. Chem. 277: 42488-42495. PMID 12213822.
- ↑ Vreys, V. and David, G. (2007). „Mammalian heparanase: what is the message”. J. Cell. Mol. Med. 11: 427-452. PMID 17635638.
- ↑ Gong, F., Jemth, P., Escobar Galvis, M.L., Vlodavsky, I., Horner, A., Lindahl, U. and Li, J.P. (2003). „Processing of macromolecular heparin by heparanase”. J. Biol. Chem. 278: 35152-35158. PMID 12837765.
- ↑ Toyoshima, M. and Nakajima, M. (1999). „Human heparanase. Purification, characterization, cloning, and expression”. J. Biol. Chem. 274: 24153-24160. PMID 10446189.
- ↑ Miao, H.Q., Navarro, E., Patel, S., Sargent, D., Koo, H., Wan, H., Plata, A., Zhou, Q., Ludwig, D., Bohlen, P. and Kussie, P. (2002). „Cloning, expression, and purification of mouse heparanase”. Protein Expr. Purif. 26: 425-431. PMID 12460766.
- ↑ Hammond, E., Li, C.P. and Ferro, V. (2010). „Development of a colorimetric assay for heparanase activity suitable for kinetic analysis and inhibitor screening”. Anal. Biochem. 396: 112-116. PMID 19748475.
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.