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acharan sulfate
n 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranosyl-(1->4)-N-acetyl-D-glucosamine
de-N-sulfated heparin
?
-
8% activity compared to heparin
-
?
deaminated heparin
?
-
54% activity compared to heparin
-
?
heparan sulfate
heparan sulfate disaccharides with 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
heparin
heparin disaccharide + ?
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 + ?
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 disaccharides
heparin pentasaccharide
heparin oligosaccharides
-
oligosaccharide products give bands between those for the heparin disaccharide and tetrasaccharide standards
-
-
?
Heparin sulfate
?
-
heparin-like portion
-
-
?
heparin, 20-mer
unsaturated heparin disaccharides
heparin, 6-mer
unsaturated heparin disaccharides
heparin, 8-mer
unsaturated heparin disaccharides
N-acetyl heparin
?
-
78% activity compared to heparin
-
?
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
-
-
?
additional information
?
-
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
?
-
600% activity compared to 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
?
-
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
?
-
600% activity compared to heparin
-
?
heparan sulfate
?
-
5 products found, major product not identified
-
?
heparan sulfate
?
-
-
-
-
?
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
?
-
bovine or porcine
-
?
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
-
-
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
-
-
-
?
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
?
heparin
?
-
-
-
-
?
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 + ?
-
-
-
?
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 + ?
-
-
several disaccharides formed by 4-deoxy-alpha-L-threo-hex-4-enepyranosyluronic acid and glucosamine, both free and sulfated
?
heparin
unsaturated heparin disaccharide + ?
-
-
-
?
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 + 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
unsaturated heparin disaccharides
-
main product
-
-
?
heparin
unsaturated heparin disaccharides
-
main product
-
-
?
Heparin monosulfate
?
-
-
-
-
?
Heparin monosulfate
?
-
-
-
-
?
heparin, 20-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 20-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 6-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 6-mer
unsaturated heparin disaccharides
-
-
-
-
?
heparin, 8-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
?
-
-
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
?
-
-
heparinase I does not cleave at GlcNH3+ residues in partially de-N-sulfated forms of heparin
-
-
?
additional information
?
-
-
acts on heparin and heparan sulfate
-
-
?
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
?
-
-
HepII has a broad specificity
-
-
?
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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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
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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