Blood group B branched chain alpha-1,3-galactosidase
| Heparanase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.166 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Heparanase (EC 3.2.1.166, Hpa1 heparanase, Hpa1, heparanase 1, heparanase-1, C1A heparanase, HPSE) is an enzyme with systematic name heparan sulfate N-sulfo-D-glucosamine endoglucanase.[1][2][3][4][5][6][7][8][9] This enzyme catalyses the following chemical reaction
- endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan
Heparanase cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group.
See also
References
- ↑ Bame, K.J. (2001). "Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans". Glycobiology. 11 (6): 91R–98R. doi:10.1093/glycob/11.6.91r. PMID 11445547.
- ↑ Peterson, S.B.; Liu, J. (2010). "Unraveling the specificity of heparanase utilizing synthetic substrates". J. Biol. Chem. 285 (19): 14504–14513. doi:10.1074/jbc.M110.104166. PMID 20181948.
- ↑ Pikas, D.S.; Li, J.P.; Vlodavsky, I.; Lindahl, U. (1998). "Substrate specificity of heparanases from human hepatoma and platelets". J. Biol. Chem. 273: 18770–18777. doi:10.1074/jbc.273.30.18770. PMID 9668050.
- ↑ Okada, Y.; Yamada, S.; Toyoshima, M.; Dong, J.; Nakajima, M.; 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 (45): 42488–42495. doi:10.1074/jbc.M206510200. PMID 12213822.
- ↑ Vreys, V.; David, G. (2007). "Mammalian heparanase: what is the message". J. Cell. Mol. Med. 11 (3): 427–452. doi:10.1111/j.1582-4934.2007.00039.x. PMID 17635638.
- ↑ Gong, F.; Jemth, P.; Escobar Galvis, M.L.; Vlodavsky, I.; Horner, A.; Lindahl, U.; Li, J.P. (2003). "Processing of macromolecular heparin by heparanase". J. Biol. Chem. 278 (37): 35152–35158. doi:10.1074/jbc.M300925200. PMID 12837765.
- ↑ Toyoshima, M.; Nakajima, M. (1999). "Human heparanase. Purification, characterization, cloning, and expression". J. Biol. Chem. 274: 24153–24160. doi:10.1074/jbc.274.34.24153. PMID 10446189.
- ↑ Miao, H.Q.; Navarro, E.; Patel, S.; Sargent, D.; Koo, H.; Wan, H.; Plata, A.; Zhou, Q.; Ludwig, D.; Bohlen, P.; Kussie, P. (2002). "Cloning, expression, and purification of mouse heparanase". Protein Expr. Purif. 26 (3): 425–431. doi:10.1016/s1046-5928(02)00558-2. PMID 12460766.
- ↑ Hammond, E.; Li, C.P.; Ferro, V. (2010). "Development of a colorimetric assay for heparanase activity suitable for kinetic analysis and inhibitor screening". Anal. Biochem. 396 (1): 112–116. doi:10.1016/j.ab.2009.09.007. PMID 19748475.
External links
- Heparanase at the US National Library of Medicine Medical Subject Headings (MeSH)
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