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4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcN-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcN
-
-
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc6S-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc6S
-
-
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNS
-
-
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS6S-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNS6S
-
-
-
?
4-nitrophenyl beta-D-GlcA-(1->4>)-alpha-D-GlcNS-(1->4)-beta-IdoA2S-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4>)-alpha-D-GlcNS-(1->4)-beta-IdoA2S-(1->4)-alpha-D-GlcNS
-
-
-
?
beta-D-glucopyranosyluronic acid
?
-
major requirement for enzyme action is reduced sulfation, cannot cleave linkages containing unsulfated GalAP residues
-
-
?
chemically modified heparins
?
-
-
-
-
?
desulfated N-sulfated heparosan
desulfated N-sulfated heparosan disaccharide
heparan sulfate
heparan disaccharide
heparan sulfate
n alpha-deltaUA-glcNAc
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
heparan sulfate
unsaturated heparan disaccharide
-
-
-
-
?
heparin
heparin disaccharide
heparin
unsaturated heparin disaccharide + ?
-
-
-
-
?
heparitin sulfates
?
-
and related compounds
-
-
?
heparosan
heparosan disaccharide
heparosan polysaccharide
heparosan oligosaccharide
-
-
-
-
?
hyaluronate
unsaturated hyaluronate disaccharide
-
no substrate of wild-type, but substrate of mutant K130C. Reaction of EC 4.2.2.1
-
-
?
IdoA2S-containing sulfated heparan hexasaccharide
?
-
-
-
?
IdoA2S-containing sulfated heparan pentasaccharide
?
-
-
-
?
N,6-sulfated glucosaminido-alpha-1,4-glucuronic acid oligosaccharide
N-sulfated glucosaminido-alpha-1,4-glucuronic acid oligosaccharide + 6-sulfated glucosaminido-alpha-1,4-glucuronic acid oligosaccharide + SO42-
-
heparitinase II
heparitinase II
?
N-acetylated heparan-sulfate
N-acetylated disaccharides
-
heparitinase I
hepartitinase I
?
N-acetylated heparan-sulfate
N-sulfated disaccharides
-
heparitinase I
hepartitinase I
?
N-desulfated, N-acetylated heparin
N-desulfated, N-acetylated heparin disaccharide
N-sulfated heparan pentasaccharide
?
-
-
-
?
N-sulfoheparosan
N-sulfoheparosan disaccharide
-
-
-
?
partially de-N-acetylated polysaccharide of Escherichia coli K5 strain
(DELTA4,5-unsaturated hexuronic acid)-(N-unsubstituted glucosamine)-(hexuronic acid)-(N-acetylglucosamine)
-
the polysaccharide consists of the repeating linear sequence -4GlcAbeta1-4GlcNAcalpha1-. Under controlled conditions for partial digestion, lyase III does not act at the GlcN-GlcA linkage, whereas GlcNAc-GlcA is cleaved. Under forced conditions for exhaustive digestion, the GlcN-GlcA linkage is only partially cleaved
-
-
?
partially de-N-sulfated forms of heparin
(DELTA4,5-unsaturated hexuronic acid)-(N-unsubstituted glucosamine)
-
heparinase III
-
-
?
unsulfated alpha-L-idopyranosyluronic acid
?
-
major requirement for enzyme action is reduced sulfation, cannot cleave linkages containing unsulfated GalAP residues
-
-
?
additional information
?
-
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc
-
-
-
?
4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNAc-(1->4)-beta-D-GlcA
4-nitrophenyl 4-deoxy-alpha-L-threo-hex-4-enopyranosiduronic acid + beta-D-GlcA-(1->4)-alpha-D-GlcNAc
about 15fold higher catalytic efficiency than with 4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
-
-
?
desulfated N-sulfated heparosan
desulfated N-sulfated heparosan disaccharide
-
-
-
?
desulfated N-sulfated heparosan
desulfated N-sulfated heparosan disaccharide
-
-
-
?
heparan sulfate
?
-
-
-
-
?
heparan sulfate
?
-
-
-
?
heparan sulfate
?
-
-
-
-
?
heparan sulfate
heparan disaccharide
-
-
-
?
heparan sulfate
heparan disaccharide
-
-
-
?
heparan sulfate
heparan disaccharide
-
-
-
-
?
heparan sulfate
n alpha-deltaUA-glcNAc
-
major product
-
?
heparan sulfate
n alpha-deltaUA-glcNAc
-
major product
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
-
-
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
-
-
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
-
-
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
-
-
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
-
-
-
?
heparin
?
-
-
-
?
heparin
heparin disaccharide
-
-
-
?
heparin
heparin disaccharide
-
-
-
?
heparosan
heparosan disaccharide
-
-
-
?
heparosan
heparosan disaccharide
-
-
-
?
hyaluronic acid
?
-
-
-
?
hyaluronic acid
?
-
-
-
?
N-desulfated, N-acetylated heparin
N-desulfated, N-acetylated heparin disaccharide
-
-
-
?
N-desulfated, N-acetylated heparin
N-desulfated, N-acetylated heparin disaccharide
-
-
-
?
additional information
?
-
-
cleavage/degradation of heparin forming unsaturated uronic acid
-
-
?
additional information
?
-
-
the enzyme is capable of tolerating heparin sulfate trimers containing single GlcNH2, GlcNAc6S or GlcNS6S residues, but is more than 20 times less reactive towards the secondary cleavage sites compared with the counterpart primary substrates. Hep III hydrolyzes the iduronic acid containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction
-
-
?
additional information
?
-
the enzyme is capable of tolerating heparin sulfate trimers containing single GlcNH2, GlcNAc6S or GlcNS6S residues, but is more than 20 times less reactive towards the secondary cleavage sites compared with the counterpart primary substrates. Hep III hydrolyzes the iduronic acid containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction
-
-
?
additional information
?
-
-
the susceptibility of the oligosaccharide substrates to the enzymatic digestion is size-dependent. Hep III has a preference for cleavage of the internal glycosidic linkages over those near to nonreducing/reducing ends . Hep III hydrolyzes the IdoA-containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction. The IdoA2S residue significantly decreases the reactivity of Hep III towards its adjacent GlcNS-GlcA at reducing end of heparan sulfate oligosaccharides, but shows no obvious influence on its nearby cleavage site at the nonreducing end
-
-
?
additional information
?
-
the susceptibility of the oligosaccharide substrates to the enzymatic digestion is size-dependent. Hep III has a preference for cleavage of the internal glycosidic linkages over those near to nonreducing/reducing ends . Hep III hydrolyzes the IdoA-containing glyosidic linkage (GlcNS-IdoA) at similar catalytic efficiency to GlcNS-GlcA, but has a slight preference toward GlcNS-GlcA linkage over GlcNS-IdoA at the beginning of catalytic reaction. The IdoA2S residue significantly decreases the reactivity of Hep III towards its adjacent GlcNS-GlcA at reducing end of heparan sulfate oligosaccharides, but shows no obvious influence on its nearby cleavage site at the nonreducing end
-
-
?
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Adenocarcinoma
Sialoglycopeptides obtained from a transplantable rat colorectal adenocarcinoma: a comparison with those from normal colonic mucosa.
Albuminuria
Essential role and therapeutic targeting of the glomerular endothelial glycocalyx in lupus nephritis.
Albuminuria
Removal of heparan sulfate from the glomerular basement membrane blocks protein passage.
Alzheimer Disease
Characterization of proteoglycans in Alzheimer's disease fibroblasts.
Arthritis
FGF-2 is bound to perlecan in the pericellular matrix of articular cartilage, where it acts as a chondrocyte mechanotransducer.
Bone Resorption
J774A.1 macrophage cell line produces PDGF-like and non-PDGF-like growth factors for bone cells.
Carcinoma
Ovarian carcinoma cells synthesize both chondroitin sulfate and heparan sulfate cell surface proteoglycans that mediate cell adhesion to interstitial matrix.
Carcinoma
VEGF release by MMP-9 mediated heparan sulphate cleavage induces colorectal cancer angiogenesis.
Carcinoma, Hepatocellular
Degradative removal of heparan sulfate from the surface of an ascites hepatoma, AH 66, by heparitinase.
Corneal Dystrophies, Hereditary
Abnormal product of corneal explants from patients with macular corneal dystrophy.
Dengue
Internalization and propagation of the dengue virus in human hepatoma (HepG2) cells.
Dengue
Productive dengue virus infection of human endothelial cells is directed by heparan sulfate-containing proteoglycan receptors.
Glaucoma
Flicker defined form perimetry in glaucoma suspects with normal achromatic visual fields.
Infections
Cell membrane bound N-acetylneuraminic acid is involved in the infection of fibroblasts and phorbol-ester differentiated monocyte-like cells with human cytomegalovirus (HCMV).
Infections
Cell-surface heparan sulfate facilitates human immunodeficiency virus Type 1 entry into some cell lines but not primary lymphocytes.
Infections
Cell-surface heparan sulfate proteoglycan mediates HIV-1 infection of T-cell lines.
Infections
Cellular invasion of Orientia tsutsugamushi requires initial interaction with cell surface heparan sulfate.
Infections
Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses.
Infections
Heparin-mediated inhibition of Chlamydia psittaci adherence to HeLa cells.
Infections
Membrane-associated heparan sulfate is not required for rAAV-2 infection of human respiratory epithelia.
Infections
Neisseria meningitidis producing the Opc adhesin binds epithelial cell proteoglycan receptors.
Infections
Primary attachment of murine leukaemia virus vector mediated by particle-associated heparan sulfate proteoglycan.
Infections
Proteoglycans act as cellular hepatitis delta virus attachment receptors.
Infections
Role of cell surface glycosaminoglycans of human T cells in human immunodeficiency virus type-1 (HIV-1) infection.
Infections
Role of heparan sulfate in attachment to and infection of the murine female genital tract by human papillomavirus.
Infections
Shielding of a lipooligosaccharide IgM epitope allows evasion of neutrophil-mediated killing of an invasive strain of nontypeable Haemophilus influenzae.
Infections
The initial steps leading to papillomavirus infection occur on the basement membrane prior to cell surface binding.
Lymphoma
Activation of platelet heparitinase by tumor cell-derived factors.
Measles
Analysis of the molecules involved in human T-cell leukaemia virus type 1 entry by a vesicular stomatitis virus pseudotype bearing its envelope glycoproteins.
Melanoma
A synthetic peptide from the heparin-binding domain III (repeats III4-5) of fibronectin promotes stress-fibre and focal-adhesion formation in melanoma cells.
Melanoma
Activation of platelet heparitinase by vascular cell lysates.
Melanoma
Cell surface phosphatidylinositol-anchored heparan sulfate proteoglycan initiates mouse melanoma cell adhesion to a fibronectin-derived, heparin-binding synthetic peptide.
Melanoma
Glycosaminoglycans of cultured human fetal uveal melanocytes and comparison with those produced by cultured human melanoma cells.
Neoplasm Metastasis
Activation of platelet heparitinase by tumor cell-derived factors.
Neoplasm Metastasis
Decreasing the metastatic potential in cancers--targeting the heparan sulfate proteoglycans.
Neoplasm Metastasis
Partial sequence of human platelet heparitinase and evidence of its ability to polymerize.
Neoplasm Metastasis
Platelet-tumor cell interaction with the subendothelial extracellular matrix: relationship to cancer metastasis.
Neoplasms
Activation of platelet heparitinase by tumor cell-derived factors.
Neoplasms
Activation of platelet heparitinase by vascular cell lysates.
Neoplasms
Decreasing the metastatic potential in cancers--targeting the heparan sulfate proteoglycans.
Neoplasms
Expression of N-CAM by human renal cell carcinomas correlates with growth rate and adhesive properties.
Neoplasms
Heparanase enhances syndecan-1 shedding: a novel mechanism for stimulation of tumor growth and metastasis.
Neoplasms
Interference with tumor cell-induced degradation of endothelial matrix on the antimetastatic action of nafazatrom.
Neoplasms
Partial characterization of proteoglycans synthesized by human glomerular epithelial cells in culture.
Neoplasms
Partial sequence of human platelet heparitinase and evidence of its ability to polymerize.
Neoplasms
Platelet-tumor cell interaction with the subendothelial extracellular matrix: relationship to cancer metastasis.
Neoplasms
The syndecan-1 heparan sulfate proteoglycan is a viable target for myeloma therapy.
Neuroblastoma
A cell-surface heparan sulfate proteoglycan mediates neural cell adhesion and spreading on a defined sequence from the C-terminal cell and heparin binding domain of fibronectin, FN-C/H II.
Ovarian Neoplasms
[Hypoxia increases the expression of heparitinase and the invasiveness through the hypoxia inducible factor-1alpha dependent pathway in human ovarian cancer cell line SKOV3]
Reperfusion Injury
Heparinase III exerts endothelial and cardioprotective effects in feline myocardial ischemia-reperfusion injury.
Scleroderma, Diffuse
Compositional changes of urinary acidic glycosaminoglycans in progressive systemic sclerosis.
Thrombasthenia
Neutrophil accumulation on activated, surface-adherent platelets in flow is mediated by interaction of Mac-1 with fibrinogen bound to alphaIIbbeta3 and stimulated by platelet-activating factor.
Trachoma
Chlamydia trachomatis glycosaminoglycan-dependent and independent attachment to eukaryotic cells.
Virus Diseases
Sulfated Glycosaminoglycans as Viral Decoy Receptors for Human Adenovirus Type 37.
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0.009 - 0.593
heparan sulfate
0.438
hyaluronate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
additional information
heparan sulfate
0.009
heparan sulfate
-
mutant H110A, pH 7.6, 35°C
0.016
heparan sulfate
-
mutant H241A, pH 7.6, 35°C
0.058
heparan sulfate
-
mutant H152A, pH 7.6, 35°C
0.059
heparan sulfate
-
mutant H424A, pH 7.6, 35°C
0.071
heparan sulfate
-
mutant H469A, pH 7.6, 35°C
0.075
heparan sulfate
-
mutant H234A, pH 7.6, 35°C
0.08
heparan sulfate
-
recombinant wild-type enzyme and mutant H225A, pH 7.6, 35°C
0.08
heparan sulfate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.092
heparan sulfate
-
mutant H539A, pH 7.6, 35°C
0.093
heparan sulfate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
0.098
heparan sulfate
-
mutant H36A, pH 7.6, 35°C
0.143
heparan sulfate
-
native wild-type enzyme, pH 7.6, 35°C
0.191
heparan sulfate
-
mutant H139A, pH 7.6, 35°C
0.593
heparan sulfate
pH 7.5, 23°C
0.326
heparin
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.344
heparin
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
additional information
heparan sulfate
0.08808 mg/ml
additional information
heparan sulfate
-
0.08808 mg/ml
additional information
heparin
0.42275 mg/ml
additional information
heparin
-
0.42275 mg/ml
additional information
additional information
-
kinetic modeling based on inactivation data, overview
-
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1.3
hyaluronate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
5
heparan sulfate
-
mutant H241A, pH 7.6, 35°C
22
heparan sulfate
-
mutant H225A, pH 7.6, 35°C
23
heparan sulfate
-
mutant H234A, pH 7.6, 35°C
24
heparan sulfate
-
mutant H424A, pH 7.6, 35°C
37
heparan sulfate
-
mutant H110A, pH 7.6, 35°C
56
heparan sulfate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
68
heparan sulfate
-
mutant H139A, pH 7.6, 35°C
68
heparan sulfate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
78
heparan sulfate
-
recombinant wild-type enzyme, pH 7.6, 35°C
83
heparan sulfate
-
mutant H152A, pH 7.6, 35°C
86
heparan sulfate
-
mutant H36A, pH 7.6, 35°C
94
heparan sulfate
-
native wild-type enzyme, pH 7.6, 35°C
100
heparan sulfate
-
mutant H469A, pH 7.6, 35°C
132
heparan sulfate
-
mutant H539A, pH 7.6, 35°C
1.6
heparin
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
1.9
heparin
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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C352A
87% wild-type activity (heparan sulfate), 72% wild-type activity (heparin)
C474A
32% wild-type activity (heparan sulfate), below 10% wild-type activity (heparin)
C577A
98% wild-type activity (heparan sulfate), 72% wild-type activity (heparin)
C624A
24% wild-type activity (heparan sulfate), below 10% wild-type activity (heparin)
C352A
-
87% wild-type activity (heparan sulfate), 72% wild-type activity (heparin)
-
C474A
-
32% wild-type activity (heparan sulfate), below 10% wild-type activity (heparin)
-
C577A
-
98% wild-type activity (heparan sulfate), 72% wild-type activity (heparin)
-
C624A
-
24% wild-type activity (heparan sulfate), below 10% wild-type activity (heparin)
-
H431A
complete loss of activity
N247A
complete loss of activity
Y301F
complete loss of activity
H431A
-
complete loss of activity
-
N247A
-
complete loss of activity
-
Y301F
-
complete loss of activity
-
C297S
-
site-directed mutagenesis, the mutant suppresses the dimerization and shows 70% reduced activity compared to the wild-type enzyme
E237A
40.8% of wild-type activitiy
F423A
42.4% of wild-type activitiy
H105A
-
PCR overlap extension site-directed mutagenesis, very low expression level, no measurement of activity possible, reduced expression level
H110A
-
PCR overlap extension site-directed mutagenesis, reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes, reduced expression level
H139A
-
PCR overlap extension site-directed mutagenesis, reduced kcat and increased Km compared to both recombinant and native wild-type enzymes, reduced expression level
H152A
-
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
H225A
-
PCR overlap extension site-directed mutagenesis, Km is the same as for the recombinant wild-type, reduced kcat
H234A
-
PCR overlap extension site-directed mutagenesis, Km is similar to the recombinant wild-type, reduced kcat
H295A
-
PCR overlap extension site-directed mutagenesis, inactive mutant
H36A
-
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
H469A
-
PCR overlap extension site-directed mutagenesis, reduced Km and increased kcat compared to both recombinant and native wild-type enzymes
H510A
-
PCR overlap extension site-directed mutagenesis, inactive mutant
H539A
-
PCR overlap extension site-directed mutagenesis, Km between the recombinant and the native wild-type enzyme, kcat is increased compared to both wild-type enzymes
I29V/L657S
42.7% of wild-type activitiy
K130C
-
mutant is able to degrade hyaluronic acid without affecting its native activity toward heparin and heparan sulfate, due to dimerization through a disulfide bond to expand the substrate binding pocket
N240A
3.1% of wild-type activitiy
Q238A
88.5% of wild-type activitiy
W350A
27.7% of wild-type activitiy
Y294F
2.8% of wild-type activitiy
Y450F
5.6% of wild-type activitiy
Y590
7.7% of wild-type activitiy
E237A
-
40.8% of wild-type activitiy
-
F423A
-
42.4% of wild-type activitiy
-
H241A
-
29.7% of wild-type activitiy
-
H424A
-
0.3% of wild-type activitiy
-
N240A
-
3.1% of wild-type activitiy
-
H241A
-
PCR overlap extension site-directed mutagenesis, highly reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes
H241A
29.7% of wild-type activitiy
H424A
-
PCR overlap extension site-directed mutagenesis, reduced Km and kcat
H424A
0.3% of wild-type activitiy
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Hovingh, P.; Linker, A.
The enzymatic degradation of heparin and heparitin sulfate. 3. Purification of a heparitinase and a heparinase from flavobacteria
J. Biol. Chem.
245
6170-6175
1970
Flavobacteriia
brenda
Nader, H.B.; Dietrich, C.P.; Bounassi, V.; Colburn, P.
Heparin sequences in the heparan sulfate chains of an endothelial cell proteoglycan
Proc. Natl. Acad. Sci. USA
84
3565-3569
1987
Pedobacter heparinus
brenda
Prinz, R.; Klein, U.; Sudhakaran, P.R.; Sinn, W.; Ullrich, K.; von Figura, K.
Metabolism of sulfated glycosaminoglycans in rat hepatocytes. Synthesis of heparan sulfate and distribution into cellular and extracellular pools
Biochim. Biophys. Acta
630
402-413
1980
Rattus norvegicus
brenda
Nader H.B.; Porcionatto M.A.; Tersariol, L.S.; Pinhal, M.A.S.; Oliveira, F.W.; Moraes, C.T.; Dietrich, C.P.
Purification and substrate specificity of heparitinase I and heparitinase II from Flavobacterium heparinum. Analyses of the heparin and heparan sulfate degradation products by 13C NMR spectroscopy
J. Biol. Chem.
265
16807-16813
1990
Pedobacter heparinus
brenda
Desai, U.R.; Wang, H.W.; Linhardt, R.J.
Specificity studies on the heparin lyases from Flavobacterium heparinum
Biochemistry
32
8140-8145
1993
Pedobacter heparinus
brenda
Linhardt, R.J.; Turnbull, J.E.; Wang, H.M.; Lofanathan, D.; Gallagher, J.T.
Examination of the substrate specificity of heparin and heparan sulfate lyases
Biochemistry
29
2611-2617
1990
Pedobacter heparinus
brenda
Yamada, S.; Sakamoto, K.; Tsuda, H.; Yoshida, K.; Sugahara, K.; Khoo, K.H.; Morris, H.R.; Dell, A.
Structural studies on the tri- and tetrasaccharides isolated from porcine intestinal heparin and characterization of heparinase/heparitinases using them as substrates
Glycobiology
4
69-78
1994
Pedobacter heparinus
brenda
Suhahara, K.; Tohno-oka, R.; Yamada, S.; Khoo, K.H.; Morris, H.R.; Dell, A.
Structural studies on the oligosaccharides isolated from bovine kidney heparan sulphate and characterization of bacterial heparitinases used as substrates
Glycobiology
4
535-544
1994
Pedobacter heparinus
brenda
Graham, L.D.; Mitchell, S.M.; Underwood, P.A.
Inhibition of platelet heparitinase by phosphorothioate DNA oligonucleotides
Biochem. Mol. Biol. Int.
37
239-246
1995
Homo sapiens
brenda
Brickman, M.C.; Gerhart, J.C.
Heparitinase inhibition of mesoderm induction and gastrulation in Xenopus laevis embryos
Dev. Biol.
164
484-501
1994
Pedobacter heparinus
brenda
Pojasek, K.; Shriver, Z.; Hu, Y.; Sasisekharan, R.
Histidine 295 and histidine 510 are crucial for the enzymatic degradation of heparan sulfate by heparinase III
Biochemistry
39
4012-4019
2000
Pedobacter heparinus
brenda
Chai, W.; Leteux, C.; Westling, C.; Lindahl, U.; Feizi, T.
Relative susceptibilities of the glucosamine-glucuronic acid and N-acetylglucosamine-glucuronic acid linkages to heparin lyase III
Biochemistry
43
8590-8599
2004
Pedobacter heparinus
brenda
Wei, Z.; Lyon, M.; Gallagher, J.T.
Distinct substrate specificities of bacterial heparinases against N-unsubstituted glucosamine residues in heparan sulfate
J. Biol. Chem.
280
15742-15748
2005
Pedobacter heparinus
brenda
Rops, A.L.; Jacobs, C.W.; Linssen, P.C.; Boezeman, J.B.; Lensen, J.F.; Wijnhoven, T.J.; van den Heuvel, L.P.; van Kuppevelt, T.H.; van der Vlag, J.; Berden, J.H.
Heparan sulfate on activated glomerular endothelial cells and exogenous heparinoids influence the rolling and adhesion of leucocytes
Nephrol. Dial. Transplant.
22
1070-1077
2007
Pedobacter heparinus
brenda
Babu, P.; Kuberan, B.
Fluorescent-tagged heparan sulfate precursor oligosaccharides to probe the enzymatic action of heparitinase I
Anal. Biochem.
396
124-132
2010
Pedobacter heparinus
brenda
Hyun, Y.J.; Lee, J.H.; Kim, D.H.
Cloning, overexpression, and characterization of recombinant heparinase III from Bacteroides stercoris HJ-15
Appl. Microbiol. Biotechnol.
86
879-890
2010
Bacteroides stercoris (C7EXL6), Bacteroides stercoris, Bacteroides stercoris HJ-15 (C7EXL6), Bacteroides stercoris HJ-15
brenda
Raman, K.; Kuberan, B.
Differential effects of heparitinase I and heparitinase III on endothelial tube formation in vitro
Biochem. Biophys. Res. Commun.
398
191-193
2010
Pedobacter heparinus
brenda
Chen, S.; Ye, F.; Chen, Y.; Chen, Y.; Zhao, H.; Yatsunami, R.; Nakamura, S.; Arisaka, F.; Xing, X.H.
Biochemical analysis and kinetic modeling of the thermal inactivation of MBP-fused heparinase I: implications for a comprehensive thermostabilization strategy
Biotechnol. Bioeng.
108
1841-1851
2011
Pedobacter heparinus
brenda
Hashimoto, W.; Maruyama, Y.; Nakamichi, Y.; Mikami, B.; Murata, K.
Crystal structure of Pedobacter heparinus heparin lyase Hep III with the active site in a deep cleft
Biochemistry
53
777-786
2014
Pedobacter heparinus (Q59289), Pedobacter heparinus, Pedobacter heparinus DSM 2366 (Q59289)
brenda
Dong, W.; Lu, W.; McKeehan, W.L.; Luo, Y.; Ye, S.
Structural basis of heparan sulfate-specific degradation by heparinase III
Protein Cell
3
950-961
2012
Bacteroides thetaiotaomicron (Q89YR9), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079 (Q89YR9)
brenda
Carnachan, S.M.; Bell, T.J.; Sims, I.M.; Smith, R.A.A.; Nurcombe, V.; Cool, S.M.; Hinkley, S.F.R.
Determining the extent of heparan sulfate depolymerisation following heparin lyase treatment
Carbohydr. Polym.
152
592-597
2016
Pedobacter heparinus
brenda
Hu, G.; Shao, M.; Gao, X.; Wang, F.; Liu, C.
Probing cleavage promiscuity of heparinase III towards chemoenzymatically synthetic heparan sulfate oligosaccharides
Carbohydr. Polym.
173
276-285
2017
Pedobacter heparinus, Pedobacter heparinus (Q05819)
brenda
Gu, Y.; Lu, M.; Wang, Z.; Wu, X.; Chen, Y.
Expanding the catalytic promiscuity of heparinase III from Pedobacter heparinus
Chemistry
23
2548-2551
2017
Pedobacter heparinus
brenda
Ulaganathan, T.; Shi, R.; Yao, D.; Gu, R.X.; Garron, M.L.; Cherney, M.; Tieleman, D.P.; Sterner, E.; Li, G.; Li, L.; Linhardt, R.J.; Cygler, M.
Conformational flexibility of PL12 family heparinases structure and substrate specificity of heparinase III from Bacteroides thetaiotaomicron (BT4657)
Glycobiology
27
176-187
2017
Bacteroides thetaiotaomicron (Q89YS4), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079 (Q89YS4)
brenda
Gu, Y.; Wu, X.; Liu, H.; Pan, Q.; Chen, Y.
Photoswitchable heparinase III for enzymatic preparation of low molecular weight heparin
Org. Lett.
20
48-51
2018
Pedobacter heparinus (Q59289)
brenda