ExplorEnz: EC 3.2.1.166

Your query returned 1 entry. Printable version

3.2.1.166

Accepted name:

heparanase

Reaction:

endohydrolysis of (1→4)-β-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan

Other name(s):

Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE

Systematic name:

heparan sulfate N-sulfo-D-glucosamine endoglucanase

Comments:

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 [2]. Heparanase-1 cuts macromolecular heparin into fragments of 5000–20000 Da [5]. The enzyme cleaves the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrades them to small oligosaccharides. Inside cells, the enzyme is important for the normal catabolism of heparan sulfate proteoglycans, generating glycosaminoglycan fragments that are then transported to lysosomes and completely degraded. When secreted, heparanase degrades basement membrane heparan sulfate glycosaminoglycans at sites of injury or inflammation, allowing extravasion of immune cells into nonvascular spaces and releasing factors that regulate cell proliferation and angiogenesis [1].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Bame, K.J. Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans. Glycobiology 11 (2001) 91R–98R. [DOI] [PMID: 11445547]
2.	Peterson, S.B. and Liu, J. Unraveling the specificity of heparanase utilizing synthetic substrates. J. Biol. Chem. 285 (2010) 14504–14513. [DOI] [PMID: 20181948]
3.	Pikas, D.S., Li, J.P., Vlodavsky, I. and Lindahl, U. Substrate specificity of heparanases from human hepatoma and platelets. J. Biol. Chem. 273 (1998) 18770–18777. [DOI] [PMID: 9668050]
4.	Okada, Y., Yamada, S., Toyoshima, M., Dong, J., Nakajima, M. and Sugahara, K. 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 (2002) 42488–42495. [DOI] [PMID: 12213822]
5.	Vreys, V. and David, G. Mammalian heparanase: what is the message. J. Cell. Mol. Med. 11 (2007) 427–452. [DOI] [PMID: 17635638]
6.	Gong, F., Jemth, P., Escobar Galvis, M.L., Vlodavsky, I., Horner, A., Lindahl, U. and Li, J.P. Processing of macromolecular heparin by heparanase. J. Biol. Chem. 278 (2003) 35152–35158. [DOI] [PMID: 12837765]
7.	Toyoshima, M. and Nakajima, M. Human heparanase. Purification, characterization, cloning, and expression. J. Biol. Chem. 274 (1999) 24153–24160. [DOI] [PMID: 10446189]
8.	Miao, H.Q., Navarro, E., Patel, S., Sargent, D., Koo, H., Wan, H., Plata, A., Zhou, Q., Ludwig, D., Bohlen, P. and Kussie, P. Cloning, expression, and purification of mouse heparanase. Protein Expr. Purif. 26 (2002) 425–431. [DOI] [PMID: 12460766]
9.	Hammond, E., Li, C.P. and Ferro, V. Development of a colorimetric assay for heparanase activity suitable for kinetic analysis and inhibitor screening. Anal. Biochem. 396 (2010) 112–116. [DOI] [PMID: 19748475]

[EC 3.2.1.166 created 2010]