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
Glycosaminoglycan degradation
Metabolic pathways
Orthology
K07964  
heparanase 1
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)
RRO: 
104658833(HPSE)
CJC: 
100402671(HPSE)
MMU: 
15442(Hpse)
RNO: 
64537(Hpse)
CGE: 
100755610(Hpse)
NGI: 
103744984(Hpse)
HGL: 
101721140(Hpse)
OCU: 
100101601(HPSE)
TUP: 
102501533(HPSE)
CFA: 
608707(HPSE)
AML: 
100470911(HPSE)
UMR: 
103665420(HPSE)
FCA: 
101090101(HPSE)
PTG: 
102965445(HPSE)
BTA: 
281230(HPSE)
BOM: 
102265641(HPSE)
PHD: 
102318817(HPSE)
CHX: 
102188207(HPSE)
OAS: 
101118612(HPSE)
SSC: 
100271932(HPSE)
CFR: 
102517816(HPSE)
BACU: 
102999760(HPSE)
LVE: 
103084178(HPSE)
ECB: 
100061267(HPSE)
MYB: 
102245458(HPSE)
MYD: 
102774009(HPSE)
PALE: 
102888805(HPSE)
MDO: 
100026183(HPSE)
SHR: 
100923804(HPSE)
GGA: 
373981(HPSE)
MGP: 
100545679(HPSE)
CJO: 
107313425(HPSE)
APLA: 
101797825(HPSE)
TGU: 
100218163(HPSE)
GFR: 
102040930(HPSE)
FAB: 
101809526(HPSE)
PHI: 
102109966(HPSE)
CCW: 
104697252(HPSE)
FPG: 
101912317(HPSE)
FCH: 
102057366(HPSE)
CLV: 
102085346(HPSE)
AAM: 
106494822(HPSE)
ASN: 
102369021(HPSE)
AMJ: 
102571669(HPSE)
PSS: 
102450514(HPSE)
CMY: 
102946031(HPSE)
ACS: 
100565376(hpse)
PBI: 
103050955(HPSE)
GJA: 
107116059(HPSE)
XTR: 
100145320(hpse)
DRE: 
563020(hpse)
TRU: 
101076415(hpse)
MZE: 
101471023(hpse)
OLA: 
101156941(hpse)
XMA: 
102231016(hpse)
LCM: 
102346905(HPSE)
CMK: 
103187960(hpse)
BFO: 
CIN: 
SPU: 
SKO: 
AME: 
725623(GB13964)
SOC: 
AEC: 
105154939(Heparanase)
HST: 
105180876(Heparanase)
CFO: 
105248467(Heparanase)
NVI: 
TCA: 
BMOR: 
100141461(Hepa)
PXY: 
API: 
PHU: 
ISC: 
HRO: 
LGI: 
CRG: 
105320771(Heparanase) 105335864(Heparanase)
OBI: 
NVE: 
HMG: 
AQU: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
EGR: 
GMX: 
PVU: 
VRA: 
MTR: 
CAM: 
ADU: 
AIP: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
POPTR_0006s06100g POPTR_0010s16820g(POPTRDRAFT_805321) POPTR_0015s03440g(POPTRDRAFT_775808) POPTR_0018s02050g(POPTRDRAFT_261180) POPTR_0025s00410g
VVI: 
SLY: 
SPEN: 
SOT: 
SIND: 
BVG: 
NNU: 
DOSA: 
Os02t0802200-01(Os02g0802200) Os03t0211700-01(Os03g0211700) Os06t0179000-01(Os06g0179000) Os07t0598400-01(Os07g0598400) Os12t0578400-01(Os12g0578400)
OBR: 
BDI: 
SBI: 
SORBI_01g043180(SORBIDRAFT_01g043180) SORBI_08g019250(SORBIDRAFT_08g019250) SORBI_10g005260(SORBIDRAFT_10g005260)
ZMA: 
100192026(cl10629_-1b) 100193781(GRMZM2G148167) 100279495(GRMZM2G107815) 100285720 100501670(GRMZM2G083812) 103640342(GRMZM2G480451)
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPP: 
MBR: 
SRE: 
TPS: 
AAF: 
EHX: 
GTT: 
SPOI: 
SCD: 
 » show all
Taxonomy
Reference
1  [PMID:11445547]
  Authors
Bame KJ
  Title
Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans.
  Journal
Glycobiology. 11 (2001) 91R-98R.
Reference
2  [PMID:20181948]
  Authors
Peterson SB, Liu J
  Title
Unraveling the specificity of heparanase utilizing synthetic substrates.
  Journal
J. Biol. Chem. 285 (2010) 14504-13.
  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 (1998) 18770-7.
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 (2002) 42488-95.
  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 (2007) 427-52.
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 (2003) 35152-8.
  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 (1999) 24153-60.
  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 (2002) 425-31.
  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 (2010) 112-6.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

DBGET integrated database retrieval system