KEGG   ENZYME: 3.2.1.166Help
Entry
EC 3.2.1.166                Enzyme                                 

Name
heparanase;
Hpa1 heparanase;
Hpa1;
heparanase 1;
heparanase-1;
C1A heparanase;
HPSE
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
heparan sulfate N-sulfo-D-glucosamine endoglucanase
Reaction(IUBMB)
endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan
Reaction(KEGG)
(other) R07811(G)
Show
Comment
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].
History
EC 3.2.1.166 created 2010
Pathway
ec00531  Glycosaminoglycan degradation
ec01100  Metabolic pathways
Orthology
K07964  heparanase
Genes
HSA: 10855(HPSE)
PTR: 461206(HPSE)
PPS: 100996218(HPSE)
GGO: 101150800(HPSE)
PON: 100448281(HPSE)
NLE: 100596185(HPSE)
MCC: 707583(HPSE)
MCF: 102123028(HPSE)
CSAB: 103235901(HPSE)
RRO: 104658833(HPSE)
RBB: 108531149(HPSE)
CJC: 100402671(HPSE)
SBQ: 101043067(HPSE)
MMU: 15442(Hpse)
RNO: 64537(Hpse)
CGE: 100755610(Hpse)
NGI: 103744984(Hpse)
HGL: 101721140(Hpse)
CCAN: 109683307(Hpse)
OCU: 100101601(HPSE)
TUP: 102501533(HPSE)
CFA: 608707(HPSE)
AML: 100470911(HPSE)
UMR: 103665420(HPSE)
ORO: 101371822(HPSE)
FCA: 101090101(HPSE)
PTG: 102965445(HPSE)
AJU: 106987077(HPSE)
BTA: 281230(HPSE)
BOM: 102265641(HPSE)
BIU: 109560640(HPSE)
PHD: 102318817(HPSE)
CHX: 102188207(HPSE)
OAS: 101118612(HPSE)
SSC: 100271932(HPSE)
CFR: 102517816(HPSE)
CDK: 105092018(HPSE)
BACU: 102999760(HPSE)
LVE: 103084178(HPSE)
OOR: 101283118(HPSE)
ECB: 100061267(HPSE)
EPZ: 103549090(HPSE)
EAI: 106846420(HPSE)
MYB: 102245458(HPSE)
MYD: 102774009(HPSE)
HAI: 109387924(HPSE)
RSS: 109447231(HPSE)
PALE: 102888805(HPSE)
LAV: 100676520(HPSE)
TMU: 101360212
MDO: 100026183(HPSE)
SHR: 100923804(HPSE)
GGA: 373981(HPSE)
MGP: 100545679(HPSE)
CJO: 107313425(HPSE)
APLA: 101797825(HPSE)
ACYG: 106041934(HPSE)
TGU: 100218163(HPSE)
GFR: 102040930(HPSE)
FAB: 101809526(HPSE)
PHI: 102109966(HPSE)
PMAJ: 107203573(HPSE)
CCW: 104697252(HPSE)
FPG: 101912317(HPSE)
FCH: 102057366(HPSE)
CLV: 102085346(HPSE)
EGZ: 104127343(HPSE)
AAM: 106494822(HPSE)
ASN: 102369021
AMJ: 102571669(HPSE)
PSS: 102450514(HPSE)
CMY: 102946031(HPSE)
CPIC: 101942907(HPSE)
ACS: 100565376(hpse)
PVT: 110083349(HPSE)
PBI: 103050955(HPSE)
GJA: 107116059(HPSE)
XLA: 108719705(hpse.L)
XTR: 100145320(hpse)
NPR: 108804446(HPSE)
DRE: 563020(hpse)
SRX: 107722827(hpse)
SGH: 107589237(hpse) 107591750
IPU: 108278991(hpse)
AMEX: 103027675(hpse)
TRU: 101076415(hpse)
LCO: 104939605(hpse)
NCC: 104957343
MZE: 101471023(hpse)
OLA: 101156941(hpse)
XMA: 102231016(hpse)
PRET: 103473150(hpse)
NFU: 107390264(hpse)
CSEM: 103390393(hpse)
LCF: 108892286(hpse)
HCQ: 109517543(hpse) 109519583
BPEC: 110161656(hpse)
SASA: 106563622(hpse) 106568158
ELS: 105014724(hpse)
SFM: 108935179(hpse)
LCM: 102346905(HPSE)
CMK: 103187960(hpse)
CIN: 100178996
SPU: 586838
AME: 725623
BIM: 100745198
BTER: 105666557
SOC: 105193112
AEC: 105154939
ACEP: 105626290
PBAR: 105430094
HST: 105180876
CFO: 105248467
LHU: 105671110
PGC: 109853681
NVI: 100113700
TCA: 659639
NVL: 108564172
BMOR: 100141461(Hepa)
PMAC: 106717291
PRAP: 110998158
PXY: 105384116
API: 107884704
DNX: 107165408
ZNE: 110830469
FCD: 110856956
CRG: 105335864
MYI: 110448663
LAK: 106153669
HMG: 100212115
AQU: 100632989
LJA: Lj0g3v0146829.1(Lj0g3v0146829.1) Lj0g3v0146829.2(Lj0g3v0146829.2) Lj2g3v0609680.1(Lj2g3v0609680.1) Lj4g3v1683270.1(Lj4g3v1683270.1) Lj4g3v1683270.2(Lj4g3v1683270.2) Lj4g3v1946680.1(Lj4g3v1946680.1) Lj4g3v1946680.2(Lj4g3v1946680.2) Lj4g3v2298190.1(Lj4g3v2298190.1) Lj6g3v1093320.1(Lj6g3v1093320.1)
DOSA: Os02t0802200-01(Os02g0802200) Os03t0211700-01(Os03g0211700) Os06t0179000-01(Os06g0179000) Os07t0598400-01(Os07g0598400) Os12t0578400-01(Os12g0578400)
ATS: 109736222(LOC109736222) 109750281(LOC109750281) 109770916(LOC109770916) 109777268(LOC109777268) 109780669(LOC109780669)
 » show all
Taxonomy
Reference
1  [PMID:11445547]
  Authors
Bame KJ
  Title
Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans.
  Journal
Glycobiology 11:91R-98R (2001)
DOI:10.1093/glycob/11.6.91R
Reference
2  [PMID:20181948]
  Authors
Peterson SB, Liu J
  Title
Unraveling the specificity of heparanase utilizing synthetic substrates.
  Journal
J Biol Chem 285:14504-13 (2010)
DOI:10.1074/jbc.M110.104166
  Sequence
[hsa:10855]
Reference
3  [PMID:9668050]
  Authors
Pikas DS, Li JP, Vlodavsky I, Lindahl U
  Title
Substrate specificity of heparanases from human hepatoma and platelets.
  Journal
J Biol Chem 273:18770-7 (1998)
DOI:10.1074/jbc.273.30.18770
Reference
4  [PMID:12213822]
  Authors
Okada Y, Yamada S, Toyoshima M, Dong J, Nakajima M, Sugahara K
  Title
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.
  Journal
J Biol Chem 277:42488-95 (2002)
DOI:10.1074/jbc.M206510200
  Sequence
[hsa:10855]
Reference
5  [PMID:17635638]
  Authors
Vreys V, David G
  Title
Mammalian heparanase: what is the message?
  Journal
J Cell Mol Med 11:427-52 (2007)
DOI:10.1111/j.1582-4934.2007.00039.x
Reference
6  [PMID:12837765]
  Authors
Gong F, Jemth P, Escobar Galvis ML, Vlodavsky I, Horner A, Lindahl U, Li JP
  Title
Processing of macromolecular heparin by heparanase.
  Journal
J Biol Chem 278:35152-8 (2003)
DOI:10.1074/jbc.M300925200
  Sequence
[mmu:15442]
Reference
7  [PMID:10446189]
  Authors
Toyoshima M, Nakajima M
  Title
Human heparanase. Purification, characterization, cloning, and expression.
  Journal
J Biol Chem 274:24153-60 (1999)
DOI:10.1074/jbc.274.34.24153
  Sequence
[hsa:10855]
Reference
8  [PMID:12460766]
  Authors
Miao HQ, Navarro E, Patel S, Sargent D, Koo H, Wan H, Plata A, Zhou Q, Ludwig D, Bohlen P, Kussie P
  Title
Cloning, expression, and purification of mouse heparanase.
  Journal
Protein Expr Purif 26:425-31 (2002)
DOI:10.1016/S1046-5928(02)00558-2
  Sequence
[mmu:15442]
Reference
9  [PMID:19748475]
  Authors
Hammond E, Li CP, Ferro V
  Title
Development of a colorimetric assay for heparanase activity suitable for kinetic  analysis and inhibitor screening.
  Journal
Anal Biochem 396:112-6 (2010)
DOI:10.1016/j.ab.2009.09.007
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.166
IUBMB Enzyme Nomenclature: 3.2.1.166
ExPASy - ENZYME nomenclature database: 3.2.1.166
BRENDA, the Enzyme Database: 3.2.1.166

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