Blood group B branched chain alpha-1,3-galactosidase
(Redirected from HPA1)
| Heparanase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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[edit]
References[edit]
- ^ Bame KJ (June 2001). "Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans". Glycobiology. 11 (6): 91R–98R. doi:10.1093/glycob/11.6.91r. PMID 11445547.
- ^ Peterson SB, Liu J (May 2010). "Unraveling the specificity of heparanase utilizing synthetic substrates". The Journal of Biological Chemistry. 285 (19): 14504–13. doi:10.1074/jbc.M110.104166. PMC 2863188. PMID 20181948.
- ^ Pikas DS, Li JP, Vlodavsky I, Lindahl U (July 1998). "Substrate specificity of heparanases from human hepatoma and platelets". The Journal of Biological Chemistry. 273 (30): 18770–7. doi:10.1074/jbc.273.30.18770. PMID 9668050.
- ^ Okada Y, Yamada S, Toyoshima M, Dong J, Nakajima M, Sugahara K (November 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". The Journal of Biological Chemistry. 277 (45): 42488–95. doi:10.1074/jbc.M206510200. PMID 12213822.
- ^ Vreys V, David G (2007). "Mammalian heparanase: what is the message?". Journal of Cellular and Molecular Medicine. 11 (3): 427–52. doi:10.1111/j.1582-4934.2007.00039.x. PMC 3922351. PMID 17635638.
- ^ Gong F, Jemth P, Escobar Galvis ML, Vlodavsky I, Horner A, Lindahl U, Li JP (September 2003). "Processing of macromolecular heparin by heparanase". The Journal of Biological Chemistry. 278 (37): 35152–8. doi:10.1074/jbc.M300925200. PMID 12837765.
- ^ Toyoshima M, Nakajima M (August 1999). "Human heparanase. Purification, characterization, cloning, and expression". The Journal of Biological Chemistry. 274 (34): 24153–60. doi:10.1074/jbc.274.34.24153. PMID 10446189.
- ^ Miao HQ, Navarro E, Patel S, Sargent D, Koo H, Wan H, Plata A, Zhou Q, Ludwig D, Bohlen P, Kussie P (December 2002). "Cloning, expression, and purification of mouse heparanase". Protein Expression and Purification. 26 (3): 425–31. doi:10.1016/s1046-5928(02)00558-2. PMID 12460766.
- ^ Hammond E, Li CP, Ferro V (January 2010). "Development of a colorimetric assay for heparanase activity suitable for kinetic analysis and inhibitor screening" (PDF). Analytical Biochemistry. 396 (1): 112–6. doi:10.1016/j.ab.2009.09.007. PMID 19748475.
External links[edit]
- Heparanase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
