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Information on EC 4.2.2.7 - heparin lyase
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EC Tree
4.2.2.7 heparin lyaseSpecify your search results
Word Map
- 4.2.2.7
- heparan
- proteoglycans
- glycosaminoglycans
- chondroitinase
- endothelial
- chondroitin
- oligosaccharide
- disaccharide
-
anticoagulant
-
coagulation
- flavobacterium
-
heparin-like
-
heparin-binding
- antithrombin
- dermatan
- heparinum
- protamine
- clot
-
depolymerization
-
hyaluronic
-
hspgs
- hyaluronidase
- chlorate
- lyases
-
n-sulfated
- thromboplastin
-
glycocalyx
- heparanase
-
iduronic
- tetrasaccharide
-
thromboelastography
- teg
-
atiii
-
anti-xa
-
6-o-sulfate
-
heparin-derived
-
o-sulfation
- decasaccharide
- analysis
-
thromboelastometry
- lmwhs
-
heptose
- enoxaparin
- syndecan-4
- tinzaparin
- medicine
-
trisulfated
- synthesis
-
heparinoids
- kaolin
- octasaccharide
- polybrene
-
beta-vldl
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
Synonyms
heparinase, heparinase i, hepii, heparinase ii, heparin lyase, heparitinase ii, heparin lyase i, hep iii, heparin lyase ii, heparitinase iii, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heparin degrading enzyme
Heparin eliminase
-
-
-
-
heparin lyase I
heparin lyase II
Heparinase
heparinase I
heparinase II
HepI
HepP
HMPREF1016_02668
Lyase, heparin
-
-
-
-
PA14_23430
Pedsa_1818
PL12a
Heparinase
-
-
-
-
heparinase I
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
additional information
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
Heparin lyase
-
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CAS REGISTRY NUMBER
COMMENTARY
1000607-06-6
-
9025-39-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acharan sulfate
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-D-glucosamine
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
heparin
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-6-O-sulfo-D-glucosamine + ?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin pentasaccharide + unsaturated heparin hexasaccharide
heparin pentasaccharide
heparin oligosaccharides
-
oligosaccharide products give bands between those for the heparin disaccharide and tetrasaccharide standards
-
-
?
N-acetyl-de-O-sulfated heparin
?
-
250% activity compared to heparin
-
?
partially de-N-sulfated forms of heparin
(DELTA4,5-unsaturated hexuronic acid)-(N-unsubstituted glucosamine(6S)) + (DELTA4,5-unsaturated hexuronic acid(2S))-(N-unsubstituted glucosamine) + (DELTA4,5-unsaturated hexuronic acid(2S))-(N-unsubstituted glucosamine(6S))
-
heparinase II
-
-
?
2-O-desulfated heparin
?
-
activity is 26% of the activity with heparin
-
-
?
2-O-desulfated heparin
?
-
activity is 26% of the activity with heparin
-
-
?
acharan sulfate
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-D-glucosamine
uniformly repeating disaccharide structure of alpha-D-N-acetylglucosaminyl-2-O-sulfo-alpha-L-iduronic acid
-
-
?
acharan sulfate
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-D-glucosamine
uniformly repeating disaccharide structure of alpha-D-N-acetylglucosaminyl-2-O-sulfo-alpha-L-iduronic acid
-
-
?
fondaparinux
?
pentasaccharide, cleavage occurs by an eliminative mechanism and leads to the formation of a trisaccharide unit and a double-bond-containing disaccharide unit
-
-
?
fondaparinux
?
pentasaccharide, cleavage occurs by an eliminative mechanism and leads to the formation of a trisaccharide unit and a double-bond-containing disaccharide unit
-
-
?
fondaparinux
?
-
pentasaccharide, cleavage occurs by an eliminative mechanism and leads to the formation of a trisaccharide unit and a double-bond-containing disaccharide unit
-
-
?
heparan sulfate
?
-
5 products found, major product not identified
-
?
heparan sulfate
?
-
enzyme prefers heparin to heparan sulfate. Activity with heparan sulfate from porcine mucosa is 17% of the activity with heparin. Activity with heparan sulfate from bovine kidney is 15% of the activity with heparin
-
-
?
heparan sulfate
?
-
enzyme prefers heparin to heparan sulfate. Activity with heparan sulfate from porcine mucosa is 17% of the activity with heparin. Activity with heparan sulfate from bovine kidney is 15% of the activity with heparin
-
-
?
heparan sulfate
?
-
5 products found, major product not identified
-
?
heparan sulfate
?
-
the enzymatic disruption of heparan sulfate chains on cell surface proteoglycans alters bone morphogenetic protein (BMP) activity and Wnt activity so as to enhance the lineage commitment and osteogenic differentiation of human mesenchymal stem cells
-
-
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
-
-
-
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
-
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
Niallia circulans HpT298
-
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
Niallia circulans HpT298
-
-
-
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
Niallia circulans HpT298
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
?
-
enzyme prefers heparin to heparan sulfate. The enzyme acts preferentially on the trisulfated sequence ->4-alpha-D-GlcNS6S(1->4)-alpha-L-IdoA2S1-> comprising heparin affording the unsaturated trisulfated disaccharid (DELTAUA2S-GlcNS6S)
-
-
?
heparin
?
-
enzyme prefers heparin to heparan sulfate. The enzyme acts preferentially on the trisulfated sequence ->4-alpha-D-GlcNS6S(1->4)-alpha-L-IdoA2S1-> comprising heparin affording the unsaturated trisulfated disaccharid (DELTAUA2S-GlcNS6S)
-
-
?
heparin
?
-
removal of heparin, the anticoagulant required in extracorporal devices for patients undergoing open-heart surgery or kidney dialysis
-
-
?
heparin
?
-
presence of Ca+ is required. Heparin-Na+ is not a substrate for heparinase I in the absence of Ca2+ ions. The binding of Ca2+ to the heparin substrate prior to enzymatic action determines the products of digestion, independently of the presence of Ca2+ in the digestion buffer
-
-
?
heparin
?
-
presence of Ca+ is required. Heparin-Na+ is not a substrate for heparinase I in the absence of Ca2+ ions. The binding of Ca2+ to the heparin substrate prior to enzymatic action determines the products of digestion, independently of the presence of Ca2+ in the digestion buffer
-
-
?
heparin
heparin disaccharide + ?
-
substrate is heparin from porcine intestinal mucosa. Cysteine, histidine may be present at the active site
-
-
?
heparin
heparin disaccharide + ?
-
substrate is heparin from porcine intestinal mucosa. Cysteine, histidine may be present at the active site
-
-
?
heparin
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-6-O-sulfo-D-glucosamine + ?
-
2 minor products found
-
?
heparin
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-6-O-sulfo-D-glucosamine + ?
-
2 minor products found
-
?
heparin
unsaturated heparin disaccharide + ?
-
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
unsaturated heparin disaccharide + ?
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
unsaturated heparin disaccharide + ?
Niallia circulans HpT298
-
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
unsaturated heparin disaccharide + ?
Niallia circulans HpT298
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
trisulfated disaccharide, small amounts of tetrasaccharides and hexasaccharides
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin hexasaccharide
-
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin pentasaccharide + unsaturated heparin hexasaccharide
-
-
-
?
heparin
unsaturated heparin disaccharide + unsaturated heparin tetrasaccharide + unsaturated heparin pentasaccharide + unsaturated heparin hexasaccharide
-
-
-
?
heparin, 20-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 6-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 8-mer
unsaturated heparin disaccharides
-
-
-
-
?
additional information
?
-
-
affinity of the enzyme for different glycosaminoglycans varies, with high substrate specificity toward heparin and heparin-derived polysaccharide. Depolymerization of heparin results in heparin disaccharides as main products
-
-
?
additional information
?
-
-
cysteine, histidine may be present at the active site
-
-
?
additional information
?
-
-
affinity of the enzyme for different glycosaminoglycans varies, with high substrate specificity toward heparin and heparin-derived polysaccharide. Depolymerization of heparin results in heparin disaccharides as main products
-
-
?
additional information
?
-
-
cysteine, histidine may be present at the active site
-
-
?
additional information
?
-
enzyme is not able to cleave a variant of fondaparinux which lacks the glucosaminsulfate at the reducing end. Cleavage occurs with low activity in fondaparinux variants having an addtional glucuronic acid or iduronic acid at the reducing end
-
-
?
additional information
?
-
-
enzyme is not able to cleave a variant of fondaparinux which lacks the glucosaminsulfate at the reducing end. Cleavage occurs with low activity in fondaparinux variants having an addtional glucuronic acid or iduronic acid at the reducing end
-
-
?
additional information
?
-
enzyme is not able to cleave a variant of fondaparinux which lacks the glucosaminsulfate at the reducing end. Cleavage occurs with low activity in fondaparinux variants having an addtional glucuronic acid or iduronic acid at the reducing end
-
-
?
additional information
?
-
-
chondroitin sulfate A,B or C, and hyaluronic acid can not act as substrates
-
?
additional information
?
-
-
no activity with acharan sulfate, chondroitin sulfate and N-desulfated heparin
-
-
?
additional information
?
-
-
no activity with acharan sulfate, chondroitin sulfate and N-desulfated heparin
-
-
?
additional information
?
-
-
chondroitin sulfate A,B or C, and hyaluronic acid can not act as substrates
-
?
additional information
?
-
-
no catalytic activity on dermatan sulfate and keratan sulfate as substrates
-
?
additional information
?
-
no catalytic activity on dermatan sulfate and keratan sulfate as substrates
-
?
additional information
?
-
-
no catalytic activity on dermatan sulfate and keratan sulfate as substrates
-
?
additional information
?
-
Niallia circulans HpT298
-
no catalytic activity on dermatan sulfate and keratan sulfate as substrates
-
?
additional information
?
-
Niallia circulans HpT298
no catalytic activity on dermatan sulfate and keratan sulfate as substrates
-
?
additional information
?
-
-
heparinase I does not cleave at GlcNH3+ residues in partially de-N-sulfated forms of heparin
-
-
?
additional information
?
-
-
heparinase 1 shows selectivity for 3,6-di-O-sulfo-2-deoxy-2-sulfamido-alpha-D-glucopyranose (1,4) 2-O-sulfo-alpha-L-idopyranosyluronic acid, GlcNS3S6S-IdoA2S, linkages, overview
-
-
?
additional information
?
-
-
porcine intestinal mucosa heparin is partially depolymerized by recombinant heparinase 1 and then fractionated, leading to the isolation of 22 homogeneous oligosaccharides with sizes ranging from disaccharide to hexadecasaccharide. Product analysis by electrospray ionization-mass spectrometry and structure determination using one- and two-dimensional nuclear magnetic resonance spectroscopy at 600 MHz, detailed overview
-
-
?
additional information
?
-
-
substrates are HepI heparin-derived defined tetrasaccharides, overview
-
-
?
additional information
?
-
-
heparinase I specificity and efficiency depend on the cationic form of the substrate. Ca2+-heparin, in which a-L-iduronate-2-O-sulfate residues adopt 1C4 conformation preferentially, is a substrate, while Na+-heparin is an inhibitor. A model based on molecular dynamics and docking proposes that deprotonated residue His203 initiates beta-elimination by abstracting the C5 proton of the alpha-L-iduonate-2-O-sulfate residue in the substrate, and protonated Tyr357 provides the donor to the hexosamine leaving group
-
-
?
additional information
?
-
-
isoforms heparinase I and heparinase II can depolymerize heparin more efficiently than isoform heparinase III, respectively, but heparinase III is the best able to protect the anticoagulant activities of low molecular weight heparins. Heparinase III and heparinase I/II combinations are able to efficiently depolymerize heparin to low molecular weight heparins with higher anticoagulant activity than the low molecular weight heparins produced by the respective heparinase I and heparinase II. HepIII and HepI is the best combination for maintaining high anti-IIa activity at the same molecular weight value
-
-
?
additional information
?
-
-
enzyme is able to cleave variants of fondaparinux which lack the glucosaminsulfate at the reducing end or have an addtional glucuronic acid or iduronic acid at the reducing end
-
-
?
additional information
?
-
-
heparinase I specificity and efficiency depend on the cationic form of the substrate. Ca2+-heparin, in which a-L-iduronate-2-O-sulfate residues adopt 1C4 conformation preferentially, is a substrate, while Na+-heparin is an inhibitor. A model based on molecular dynamics and docking proposes that deprotonated residue His203 initiates beta-elimination by abstracting the C5 proton of the alpha-L-iduonate-2-O-sulfate residue in the substrate, and protonated Tyr357 provides the donor to the hexosamine leaving group
-
-
?
additional information
?
-
-
chondroitin sulfate A,B or C, and hyaluronic acid can not act as substrates
-
?
additional information
additional information
-
-
requirement O-sulfate and sulfamido groups
-
-
?
additional information
additional information
-
-
not: N-acetyl heparin
-
-
?
additional information
additional information
-
-
substrate specificity
-
?
additional information
additional information
-
-
a synthetic pentasaccharide containing an antithrombin III binding site serves as substrate
a trisaccharide and a disaccharide with no antithrombin III binding activity
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
heparan sulfate
?
-
the enzymatic disruption of heparan sulfate chains on cell surface proteoglycans alters bone morphogenetic protein (BMP) activity and Wnt activity so as to enhance the lineage commitment and osteogenic differentiation of human mesenchymal stem cells
-
-
?
heparin
?
-
removal of heparin, the anticoagulant required in extracorporal devices for patients undergoing open-heart surgery or kidney dialysis
-
-
?
additional information
?
-
-
affinity of the enzyme for different glycosaminoglycans varies, with high substrate specificity toward heparin and heparin-derived polysaccharide. Depolymerization of heparin results in heparin disaccharides as main products
-
-
?
additional information
?
-
-
affinity of the enzyme for different glycosaminoglycans varies, with high substrate specificity toward heparin and heparin-derived polysaccharide. Depolymerization of heparin results in heparin disaccharides as main products
-
-
?
additional information
?
-
-
heparinase 1 shows selectivity for 3,6-di-O-sulfo-2-deoxy-2-sulfamido-alpha-D-glucopyranose (1,4) 2-O-sulfo-alpha-L-idopyranosyluronic acid, GlcNS3S6S-IdoA2S, linkages, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
NaCl
Ni2+
Zn2+
Ca2+
-
purified GST fusion enzyme requires Ca2+. Activity of the GST-heparinase I is stimulated 7fold by 1 mM Ca2+. Mg2+ and Mn2+ are much less effective at the same concentrations while Cu2+ and Zn2+ are ineffective
Ca2+
-
essential for activity, two calcium-binding sites with different affinity
Ca2+
-
required. Ca2+ is sequestered from the medium to achieve effective catalysis, and there is only very weak residual catalysis when Ca2+ ions are excluded from the medium
Zn2+
-
bound within the central domain and plays an essential structural role in the stabilization of a loop forming one wall of the substrate-binding site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-Acetylimidazole
-
80% inhibition at 1 mM concentration of inhibitor, indicates the necessity of tyrosine residues in the active site
additional information
-
specific desulfation of the alpha-L-iduronic acid, 2-O-sulfate ring or the desulfation of the acid alpha-L-iduronic, 2-O-sulfate ring, followed by epimerization of its iduronic to galacturonic acid abolishes its degradation by heparinase I, as well as leading to the formation of competitive inhibitors
-
EDTA
-
1 mM EDTA completely inactivates heparinase I in the presence of 2 mM Ca2+. Inhibition is reversible, the reintroduction of calcium ions into the system completely restores the enzymatic activity of heparinase I
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
free sulfohydryl groups of cysteine residues are necessary for catalytic activity of the enzyme
-
additional information
-
catalytic activity of heparinase I requires a reducing environment
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.018
heparin pentasaccharide
-
cleavage of a synthetic pentasaccharide containing an antithrombin III binding site into a trisaccharide and a disaccharide, pH 7.0, 30ºC
additional information
heparin
-
several double and triple mutants of the calcium-coordinating residues
additional information
heparin
kcat/Km value 19.3 ml/mg/s, pH 6.0, 50°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
heparin
Km value 4.6 mg/ml, pH 6.0, 50°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00008
heparin with reduced carboxylate group
-
pH not specified in the publication temperature not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44.6
additional information
additional information
-
heparinase activity is found to be dependent on the rate of utilization of heparin during growth. Heparin is taken up rapidly in the initial exponential phase of the growth at a rate of 0.16 g/cell/h. Enzyme activity increases at a rate of 1.53 units/h with the exhaustion of heparin in the medium
additional information
no activity with chondroitin sulfate or hyaluronic acid
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
additional information
-
effect of blocking agents on pH optimum, immobilized enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 7.9
-
pH 5.8: about 55% of maximal activity, pH 7.9: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 60
-
highly active within the temperature range of 25-35°C, but activity is lost rapidly above 35°C
30 - 56
-
30°C: about 40% of maximal activity, 56°C: about 650% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Niallia circulans HpT298
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
optimization of enzyme production, simple carbon sources, including sucrose, lactose, maltose, and complex carbon sources such as starch and cellulose are able to support growth of the organism, but enzyme can be produced only in the presence of maltose, sorbitol, mannitol, arabinose, and mannose. Phosphate inhibits enzyme production and cell growth, while heparin inhibits cell growth but is required for enzyme induction, overview. Heparinase production in optimized medium is highest, i.e., 75.4 units, when the pH of the medium is kept at pH 6.5, inoculum size of 0.5-1.0% of spore suspension, and for an incubation temperature of 30°C. Growth profile, heparin utilization, and heparinase production in optimized medium, overview
brenda
additional information
-
propagated in bovine lung microvascular endothelial cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the fungus produces heparinase, both extracellularly and intracellularly, in its late log phase of growth
-
brenda
-
the fungus produces heparinase, both extracellularly and intracellularly, in its late log phase of growth
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
-
differential effects of heparitinase I, EC 4.2.2.8, and heparitinase III on endothelial tube formation. The enzymes inhibit tube formation and reduce tumor-derived neovascularization in vivo by reducing bFGF binding and subsequent signaling, HepIII has a stronger effect than Hep I. Heparitinases, isolated from Flavobacterium heparinum, cleave heparan sulfate chains at defined locations, Hep III cleaves near sulfated iduronic acid residues and at highly sulfated regions. Hep III therefore may disrupt the growth factor binding domains that are important for angiogenesis
physiological function
-
heparin and heparan sulfate contain a rare 3-O-sulfoglucosamine residue critical for anticoagulation and virus recognition, respectively. The glycosidic linkage proximate to this 3-O-sulfoglucosamine is resistant to cleavage by all heparin lyases
physiological function
HepP plays a crucial role in the pathogenesis of Pseudomonas aeruginosa PA14 during burn wound infection
physiological function
mutation of hepP results in delay of pellicle formation at the air-liquid interface under static growth conditions. Biofilm formation by the mutant is also significantly reduced. In the Caenorhabditis elegans model of slow killing, mutation of hepP results in a significantly lower rate of killing than that of the parent wild-type strain
physiological function
-
mutation of hepP results in delay of pellicle formation at the air-liquid interface under static growth conditions. Biofilm formation by the mutant is also significantly reduced. In the Caenorhabditis elegans model of slow killing, mutation of hepP results in a significantly lower rate of killing than that of the parent wild-type strain
-
physiological function
-
HepP plays a crucial role in the pathogenesis of Pseudomonas aeruginosa PA14 during burn wound infection
-
additional information
-
free sulfohydryl groups of cysteine residues are necessary for catalytic activity of the enzyme
additional information
-
free sulfohydryl groups of cysteine residues are necessary for catalytic activity of the enzyme
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HEPB_PEDHD
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
772
0
87626
Swiss-Prot
-
A0A1V6G754_9BACT
682
0
75072
TrEMBL
-
A0A645GHI1_9ZZZZ
242
0
27086
TrEMBL
other Location (Reliability: 5)
E6SWQ9_BACT6
Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108)
386
0
44162
TrEMBL
-
A0A1V5XTH4_9DELT
644
0
72471
TrEMBL
-
C6Y001_PEDHD
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
384
0
43832
TrEMBL
-
A0A1V5UXT2_9BACT
1028
0
116680
TrEMBL
-
A0A644VGT5_9ZZZZ
772
0
87953
TrEMBL
Secretory Pathway (Reliability: 1)
A7M5V1_BACO1
Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
392
0
44342
TrEMBL
-
A0A2N9N5B1_9BACT
735
0
82673
TrEMBL
-
A0A5C6CY00_9BACT
847
1
95313
TrEMBL
-
A0A1V6FG37_9BACT
748
0
84483
TrEMBL
-
C6Y1P2_PEDHD
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
362
0
40862
TrEMBL
-
A0A1V6H1V3_9BACT
896
1
99718
TrEMBL
-
A0A1V6FSI9_9BACT
1167
0
128619
TrEMBL
-
A0A078RWF0_BACUN
373
0
43051
TrEMBL
-
A0A0M2WUR3_9BURK
937
0
101589
TrEMBL
-
A0A1V6FNZ8_9BACT
631
0
68832
TrEMBL
-
A0A1V6D7U5_9BACT
760
0
84471
TrEMBL
-
E2N935_9BACE
389
0
44402
TrEMBL
-
A0A7R6P7K5_9GAMM
605
0
68808
TrEMBL
-
A0A0H2ZDM9_PSEAB
Pseudomonas aeruginosa (strain UCBPP-PA14)
550
0
61874
TrEMBL
-
F0S8P2_PSESL
Pseudopedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / CCUG 39354 / LMG 10337 / NBRC 100064 / NCIMB 13643)
655
0
76350
TrEMBL
-
Q89YQ6_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
376
0
42514
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
43000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, space group: P2(1)2(1)2(1), unit-cell parameters: a = 70.0 A, b = 119.3 A, c = 200.7 A, alpha = beta = gamma = 90°. Two molecules in the asymmetric unit
-
structure of the enzyme in ligand-free state at 2.15 A resolution and in complex with a disaccharide product of heparin degradation at 2.3 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D210A
-
mutation does not affect the product profile compared to the wild type anzyme
D212A
-
mutation does not affect the product profile compared to the wild type anzyme
E207A
-
mutation does not affect the product profile compared to the wild type anzyme
E381A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
G213A
-
mutation does not affect the product profile compared to the wild type anzyme
G378A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
H202A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
H202A/Y257A
-
His-tagged version expressed in Escherichia coli BL21(DE3)
H406A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
I133T/P316T
mutant displays about 7fold increase in catalytic efficiency
N375A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
N405A
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue
N405G
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant shows broadened substrate specificity and cleaves the resistant linkage proximate to the 3-O-sulfoglucosamine residue
S377A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
T216A
-
mutation does not affect the product profile compared to the wild type anzyme
T373A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
T382A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
Y257A
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
Y257A/H406A
-
His-tagged version expressed in Escherichia coli BL21(DE3)
Y257F
-
no activity in a real time assay, His-tagged version expressed in Escherichia coli BL21(DE3)
Y379A
-
produces lower amounts of disaccharides and tetrasaccharides and a greater fraction of larger digestion fragments
additional information
-
construction of several double and triple mutants of the calcium-coordinating residues
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
-
purified native enzyme, catalytic activity after about 72 h shows a loss of 40.4% in activity
40
-
rapid loss of activity above, more than 25% loss of activity after 20 min
45
50
55
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CaCl2 is a good stabilizer of the purified enzyme in liquid form toward either storaging at 4°C or freezing-thawing
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, without any additives, 15 days, retains its activity, more stable at 4°C than at -20°C, activity decreases after a few cycles of freezing and thawing
Frozen or lyophilized at -20°C, protein concentration: 0.2-0.4 mg/ml, more stable in presence of 7.5% glycerol or 5% sucrose
-
unstable if stored at 4ºC, stability is increased with bovine serum albumin addition
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation followed by DEAE-Sephacel and Sephacryl S-200 column chromatography
-
by several chromatographic steps, including QAE-cellulose, DEAE-cellulose, Sephadex and hydroxyapatite
-
enhancement of enzyme production by 92% is achieved by manipulation of the fermentation conditions (pH: 6.5, inoculum size of 0.5-1.0%, incubation temperature 30°C) and medium ingredients (replacement of dextrose by mannitol, soy peptone by chitin and ammonium sulfate by ammonium nitrate and supplementation of pyridoxine hydrochloride and glutaric acid)
-
enzyme expressed in Escherichia coli as a fusion protein with GST at the N-terminus, one-step affinity purification
-
immobilized metal ion affinity chromatography, ion exchange chromatography, gel filtration
-
ion-exchange chromatography (SP-Sepharose), hydroxylapatite chromatography, mutant proteins by immobilized metal-chelate chromatography, His-tag is removed, further purification by ion-exchange chromatography
-
native enzyme 40.5fold by anion and cation exchange chromatography, and gel filtration
-
native enzyme 40.5fold by anion exchange and hydrophobic interaction chromatography, and gel filtration
-
purification of a recombinant enzyme by ammonium sulfate precipitation followed by DEAE-Sephacel and Sephacryl S-200 column chromatography
three steps osmotic shock procedure, followed by chromatography on SP-Sepharose and Source 30S resin
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein at high yield
-
expression as fusion protein, fused to the C-terminus of soluble partners
-
expression in Escherichia coli
expression in Escherichia coli as a fusion protein with GST at the N-terminus
-
expression of the recombinant wild type and several mutants in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
heparin induces the enzyme in cells, enzyme production is also upleveled by addition of N-acetyl D-glucosamine, glutaric acid, mannitol, arabinose, pyridoxine, diammonium biphosphate, ammonium nitrate, and especially by chitin, slight enhancement by L-leucine, L-glutamine, and L-histidine, overview
-
inducible heparinase
phosphate suppresses the enzyme production in cells, enzyme production is also reduced by potassium nitrate, maltose, mannose, and especially by sucrose, overview
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
synthesis
analysis
-
development of a simple and rapid colorimetric method, which can detect heparinase activity and thus help to identify likely candidates for future anti-metastatic and anti-inflammatory drugs
analysis
-
the GSTfused enzyme with high purity and specific activity may be useful in solid phase clinical applications and sequence characterizations of structurally specific heparin and heparan sulfate motifs
analysis
-
detection of heparin and heparinase using a ratiometric fluorescence method based on benzoperylene derivative, 6-(benzo [ghi]perylene-1,2-dicarboxylic imide-yl)hexanoic acid excimer in an aequeous buffer solution. The assay is simple, rapid, inexpensive, sensitive and selective and can be used for assay of heparin and heparinase in complex sample mixtures
analysis
-
in heparinized blood plasma samples of cancer patients, heparinase addition removes the heparin inhibition. Treatment significantly improves PCR efficacy, enabling quantification of circulating tumor DNA
medicine
in a murine model of thermal injury, mutation of HepP reduces the rate of mortality from 100% for mice infected with wild-type to 7% for mice infected with the mutant strain. Upon intraperitoneal inoculation of the thermally injured mice, the rate of mortality for mice infected the mutant was 0%, whereas it was 66% for mice infected with wild-type. Only wild-type PA14 is recovered from the livers and spleens of infected mice
medicine
-
in a murine model of thermal injury, mutation of HepP reduces the rate of mortality from 100% for mice infected with wild-type to 7% for mice infected with the mutant strain. Upon intraperitoneal inoculation of the thermally injured mice, the rate of mortality for mice infected the mutant was 0%, whereas it was 66% for mice infected with wild-type. Only wild-type PA14 is recovered from the livers and spleens of infected mice
-
synthesis
-
expression as fusion protein, fused to the C-terminus of soluble partners translation initiation factor 2 domain I, glutathione S-transferase, maltose-binding protein, small ubiquitin modifying protein and N-utilization substance A, and purification of hybrid proteins. Except for NusA, the fusion partners dramatically improve the soluble expression of recombinant HepA, with translation initiation factor 2 domain I-HepA and small ubiquitin modifying protein-HepA creating almost completely soluble HepA where 98% and 94% of expressed HepA fusions are soluble, respectively
synthesis
-
expression in Escherichia coli using a hexahistidine-tagged small ubiquitin-like modifier. The fusion protein exhibits high enzyme activity without requirements of in vitro refolding and SUMO-tag releasing process, and the optimum enzyme activity is obtained at 30°C, pH 7.0 and 10 mmol/l Ca2+ in the reaction buffer
synthesis
expression of HepI with the chitin binding domain of Bacillus circulans chitinase A1 as a chitin-affinity tag, and the small ubiquitin-like modifier (SUMO) linker as a solvation enhancer in different fusion sequence. The constructs chitin binding domain-HepI, chitin binding domain-SUMO-HepI, SUMO-chitin binding domain-HepI and chitin binding domain-HepI-SUMO show specific enzyme activities of 1.88, 3.69, 3.44, and 2.73 IU/mg total proteins, respectively, with unfractionated heparin as substrate. Chitin binding domain-SUMO-HepI exhibits the maximum half-life (48 min) at 30°C and best thermostability under 15-50°C. All the fusion enzymes show broad pH-stability in the range of 5.4-9.0
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, V.C.; Linhard, R.J.; Bernstein, H.; Cooney, Ch.L.; Langer, R.
Purification and characterization of heparinase from Flavobacterium heparinum
J. Biol. Chem.
260
1849-1857
1985
Pedobacter heparinus
brenda
Nakamura, T.; Shibata, Y.; Fujimura, S.
Purification and properties of Bacteroides heparinolyticus heparinase (heparin lyase, EC 4.2.2.7)
J. Clin. Microbiol.
26
1070-1071
1988
Bacteroides heparinolyticus
brenda
Silverberg, I.; Havsmark, B.; Fransson, L.A.
The substrate specificity of heparan sulphate lyase and heparin lyase from Flavobacterium heparinum
Carbohydr. Res.
137
227-238
1985
Pedobacter heparinus
-
brenda
Arbogast, B.; Hopwood, J.J.; Dorfman, A.
Heparinase activity in rat liver
Biochem. Biophys. Res. Commun.
75
610-617
1977
Rattus norvegicus
brenda
Silva, M.E.; Dietrich, C.P.
Structure of heparin. Characterization of the products formed from heparin by the action of a heparinase and a heparitinase from Flavobacterium heparinum
J. Biol. Chem.
250
6841-6846
1975
Pedobacter heparinus
brenda
Dietrich, C.P.; Silva, M.E.; Michelacci, Y.M.
Sequential degradation of heparin in Flavobacterium heparinum. Purification and properties of five enzymes involved in heparin degradation
J. Biol. Chem.
248
6408-6415
1973
Pedobacter heparinus
brenda
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
Yang, V.C.; Bernstein, H.; Langer, R.
Large scale production of heparinase
Biotechnol. Prog.
3
27-30
1987
Pedobacter heparinus
-
brenda
Linhardt, R.J.; Fitzgerald, G.L.; Cooney, Ch.L.
Mode of action of heparin lyase on heparin
Biochim. Biophys. Acta
702
197-203
1982
Pedobacter heparinus
brenda
Bernstein, H.; Yang, V.C.; Langer, R.
An investigation of heparinase immobilization
Appl. Biochem. Biotechnol.
16
129-143
1987
Pedobacter heparinus
brenda
Linhardt, R.J.; Cooney, C.L.; Tapper, D.; Zannetos, C.A.; Larsen, A.K.; Langer, R.
An immobilized microbial heparinase for blood deheparinization
Appl. Biochem. Biotechnol.
9
41-55
1984
Pedobacter heparinus
brenda
Joubert, J.J.; Pitout, M.J.
A constitutive heparinase in a Flavobacterium sp.
Experientia
41
1541
1985
Flavobacterium sp.
-
brenda
Cerbelaud, E.C.; Conway, L.J.; Galliher, P.M.; Langer, R.S.; Cooney, C.L.
Sulfur regulation of heparinase and sulfatases in Flavobacterium heparinum
Appl. Environ. Microbiol.
51
640-646
1986
Pedobacter heparinus
brenda
Bernstein, H.; Yang, V.C.; Langer, R.
Distribution of heparinase covalently immobilized to agarose: Experimental and theoretical studies
Biotechnol. Bioeng.
30
196-207
1987
Pedobacter heparinus
brenda
Yang, V.C.; Bernstein, H.; Cooney, Ch.L.; Langer, R.
Large scale preparation and characterization of mucopolysaccharase contamination free heparinase
Appl. Biochem. Biotechnol.
16
35-50
1987
Pedobacter heparinus
brenda
Yoshida, E.; Sakai, K.; Tokuyama, S.; Miyazono, H.; Maruyama, H.; Morikawa, K.; Yoshida, K.; Tahara, Y.
Purification and characterization of heparinase that degrades both heparin and heparan sulfate from Bacillus circulans
Biosci. Biotechnol. Biochem.
66
1181-1184
2002
Niallia circulans, Niallia circulans HpT298
brenda
Yoshida, E.; Arakawa, S.; Matsunaga, T.; Toriumi, S.; Tokuyama, S.; Morikawa, K.; Tahara, Y.
Cloning, sequencing, and expression of the gene from Bacillus circulans that codes for a heparinase that degrades both heparin and heparan sulfate
Biosci. Biotechnol. Biochem.
66
1873-1879
2002
Niallia circulans (Q8KKH9), Niallia circulans, Niallia circulans HpT298 (Q8KKH9)
brenda
Kim, B.T.; Kim, W.S.; Kim, Y.S.; Linhardt, R.J.; Kim, D.H.
Purification and characterization of a novel heparinase from Bacteroides stercoris HJ-15
J. Biochem.
128
323-328
2000
Bacteroides stercoris, Bacteroides stercoris HJ-15
brenda
Yapeng, C.; Ningguo, G.; Xiulan, C.; Jing, Y.; Shijun, Q.; Shuzheng, Z.
Rapid purification, characterization and substrate specificity of heparinase from a novel species of Sphingobacterium
J. Biochem.
134
365-371
2003
Sphingobacterium sp.
brenda
Liu, D.; Shriver, Z.; Godavarti, R.; Venkataraman, G.; Sasisekharan, R.
The calcium-binding sites of heparinase I from Flavobacterium heparinum are essential for enzymic activity
J. Biol. Chem.
274
4089-4095
1999
Pedobacter heparinus
brenda
Yu, G.; LeBrun, L.; Gunay, N.S.; Hoppensteadt, D.; Walenga, J.M.; Fareed, J.; Linhardt, R.J.
Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site
Thromb. Res.
100
549-556
2000
Pedobacter heparinus
brenda
Shaya, D.; Li, Y.; Cygler, M.
Crystallization and preliminary X-ray analysis of heparinase II from Pedobacter heparinus
Acta Crystallogr. Sect. D
60
1644-1646
2004
Pedobacter heparinus
brenda
Chem, Y.; Xing, X.H.; Lou, K.
Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein
Biochem. Eng. J.
23
155-159
2005
Pedobacter heparinus
-
brenda
Kim, W.S.; Kim, B.T.; et.al.
Purification of heparin lyase I from Bacteroides stercoris HJ-15
J. Biochem. Mol. Biol.
37
684-690
2004
Bacteroides stercoris, Bacteroides stercoris HJ-15
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
Shaya, D.; Tocilj, A.; et.al.
Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product
J. Biol. Chem.
281
15525-15535
2006
Pedobacter heparinus
brenda
Luo, Y.; Huang, X.; McKeehan, W.L.
High yield, purity and activity of soluble recombinant Bacteroides thetaiotaomicron GST-heparinase I from Escherichia coli
Arch. Biochem. Biophys.
460
17-24
2007
Bacteroides thetaiotaomicron
brenda
Ma, X.; Wang, Z.; Li, S.; Shen, Q.; Yuan, Q.
Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum
J. Chromatogr. B
843
209-215
2006
Pedobacter heparinus
brenda
Ahn, S.C.; Kim, B.Y.; Oh, W.K.; Park, Y.M.; Kim, H.M.; Ahn, J.S.
Colorimetric heparinase assay for alternative anti-metastatic activity
Life Sci.
79
1661-1665
2006
Pedobacter heparinus
brenda
Manton, K.J.; Leong, D.F.; Cool, S.M.; Nurcombe, V.
Disruption of heparan and chondroitin sulfate signaling enhances mesenchymal stem cell-derived osteogenic differentiation via bone morphogenetic protein signaling pathways
Stem Cells
25
2845-2854
2007
Homo sapiens
brenda
Banga, J.; Tripathi, C.K.; Bihari, V.
Growth and enzyme production kinetics of a heparinase-producing fungal isolate
Med. Chem. Res.
17
85-93
2008
Aspergillus oryzae, Pedobacter heparinus
-
brenda
Hyun, Y.J.; Lee, K.S.; Kim, D.H.
Cloning, expression and characterization of acharan sulfate-degrading heparin lyase II from Bacteroides stercoris HJ-15
J. Appl. Microbiol.
108
226-235
2010
Bacteroides stercoris (C0JBW5), Bacteroides stercoris HJ-15 (C0JBW5), Bacteroides stercoris HJ-15
brenda
Han, Y.H.; Garron, M.L.; Kim, H.Y.; Kim, W.S.; Zhang, Z.; Ryu, K.S.; Shaya, D.; Xiao, Z.; Cheong, C.; Kim, Y.S.; Linhardt, R.J.; Jeon, Y.H.; Cygler, M.
Structural snapshots of heparin depolymerization by heparin lyase I
J. Biol. Chem.
284
34019-34027
2009
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron WAL2926
brenda
Shaya, D.; Zhao, W.; Garron, M.L.; Xiao, Z.; Cui, Q.; Zhang, Z.; Sulea, T.; Linhardt, R.J.; Cygler, M.
Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate
J. Biol. Chem.
285
20051-20061
2010
Pedobacter heparinus
brenda
Banga, J.; Tripathi, C.K.M.
Purification and characterization of a novel heparin degrading enzyme from Aspergillus flavus (MTCC-8654)
Appl. Biochem. Biotechnol.
160
1004-1016
2010
Aspergillus flavus, Aspergillus flavus MTCC-8654
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
Zhao, W.; Garron, M.L.; Yang, B.; Xiao, Z.; Esko, J.D.; Cygler, M.; Linhardt, R.J.
Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue
FEBS Lett.
585
2461-2466
2011
Pedobacter heparinus
brenda
Xiao, Z.; Zhao, W.; Yang, B.; Zhang, Z.; Guan, H.; Linhardt, R.J.
Heparinase 1 selectivity for the 3,6-di-O-sulfo-2-deoxy-2-sulfamido-alpha-D-glucopyranose (1,4) 2-O-sulfo-alpha-L-idopyranosyluronic acid (GlcNS3S6S-IdoA2S) linkages
Glycobiology
21
13-22
2011
Pedobacter heparinus
brenda
Wu, J.; Zhang, C.; Mei, X.; Li, Y.; Xing, X.H.
Controllable production of low molecular weight heparins by combinations of heparinase I/II/III
Carbohydr. Polym.
101
484-492
2014
Pedobacter heparinus
brenda
Cordula, C.R.; Lima, M.A.; Shinjo, S.K.; Gesteira, T.F.; Pol-Fachin, L.; Coulson-Thomas, V.J.; Verli, H.; Yates, E.A.; Rudd, T.R.; Pinhal, M.A.; Toma, L.; Dietrich, C.P.; Nader, H.B.; Tersariol, I.L.
On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+
Mol. Biosyst.
10
54-64
2014
Pedobacter heparinus, Pedobacter heparinus ATCC 13125
brenda
Huang, J.; Cao, L.; Guo, W.; Yuan, R.; Jia, Z.; Huang, K.
Enhanced soluble expression of recombinant Flavobacterium heparinum heparinase I in Escherichia coli by fusing it with various soluble partners
Protein Expr. Purif.
83
169-176
2012
Pedobacter heparinus
brenda
Balasubramaniam, K.; Sharma, K.; Rani, A.; Rajulapati, V.; Goyal, A.
Deciphering the mode of action, structural and biochemical analysis of heparinase II/III (PsPL12a) a new member of family 12 polysaccharide lyase from Pseudopedobacter saltans
Ann. Microbiol.
68
409-418
2018
Pseudopedobacter saltans (F0S8P2), Pseudopedobacter saltans DSM 12145 (F0S8P2)
-
brenda
Yu, P.; Jia, T.; Chen, Y.; Wu, Y.; Zhang, Y.
Improving the activity of heparinase I by the directed evolution, its enzymatic properties and optimal conditions for heparin degrading by recombinant cells
Biochem. Eng. J.
114
237-243
2016
Pedobacter heparinus (B3U3D9)
-
brenda
Yang, M.; Chen, J.; Zhou, H.; Li, W.; Wang, Y.; Li, J.; Zhang, C.; Zhou, C.; Yu, C.
Polycation-induced benzoperylene probe excimer formation and the ratiometric detection of heparin and heparinase
Biosens. Bioelectron.
75
404-410
2016
Pedobacter heparinus
brenda
Yang, B.; Zhang, C.; Wang, C.; Zhou, H.; Li, Z.; Song, Y.; Zhang, T.; Luo, X.
Soluble expression and purification of heparinase I in Escherichia coli using a hexahistidine-tagged small ubiquitin-like modifier as a fusion partner
Biotechnol. Biotechnol. Equip.
31
1040-1045
2017
Pedobacter heparinus
-
brenda
Dzvova, N.; Colmer-Hamood, J.A.; Griswold, J.A.; Hamood, A.N.
Isolation and characterization of HepP a virulence-related Pseudomonas aeruginosa heparinase
BMC Microbiol.
17
233
2017
Pseudomonas aeruginosa (A0A0H2ZDM9), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZDM9)
brenda
Bohlmann, L.; Chang, C.W.; Beacham, I.; von Itzstein, M.
Exploring bacterial heparinase II activities with defined substrates
ChemBioChem
16
1205-1211
2015
Pedobacter heparinus, Bacteroides eggerthii (E5X103), Bacteroides eggerthii, Bacteroides eggerthii 1_2_48FAA (E5X103)
brenda
Sefrioui, D.; Beaussire, L.; Clatot, F.; Delacour, J.; Perdrix, A.; Frebourg, T.; Michel, P.; Di Fiore, F.; Sarafan-Vasseur, N.
Heparinase enables reliable quantification of circulating tumor DNA from heparinized plasma samples by droplet digital PCR
Clin. Chim. Acta
472
75-79
2017
Bacteroides eggerthii
brenda
Dzvova, N.; Colmer-Hamood, J.A.; Griswold, J.A.; Hamood, A.N.
Heparinase is essential for Pseudomonas aeruginosa virulence during thermal injury and infection
Infect. Immun.
86
e00755
2018
Pseudomonas aeruginosa (A0A0H2ZDM9), Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZDM9)
brenda
Xu, S.; Qiu, M.; Zhang, X.; Chen, J.
Expression and characterization of an enhanced recombinant heparinase I with chitin binding domain
Int. J. Biol. Macromol.
105
1250-1258
2017
Pedobacter heparinus (B3U3D9)
brenda
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