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Information on EC 4.2.2.8 - heparin-sulfate lyase and Organism(s) Pedobacter heparinus and UniProt Accession Q05819
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EC Tree
4.2.2.8 heparin-sulfate lyaseIUBMB Comments
Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages.
Specify your search results
Word Map
- 4.2.2.8
- proteoglycans
- glycosaminoglycans
- chondroitinase
- chondroitin
- endothelial
- oligosaccharide
-
basement
- dermatan
-
heparin-binding
-
hspgs
- bfgf
- disaccharide
- hyaluronidase
- heparinum
-
hyaluronic
-
nitrous
- perlecan
- flavobacterium
- chlorate
- neuraminidase
-
3hglucosamine
- fgf-2
- antithrombin
-
n-sulfated
-
iduronic
- lyases
-
glycocalyx
-
35ssulfate
- keratanase
-
heparin-like
-
proteoheparan
-
inner-core
- analysis
-
heptose
-
cetylpyridinium
-
beta-d-xyloside
-
trifluoromethanesulfonic
- synthesis
-
sulfate-containing
- heparanase
-
glycosaminoglycan-degrading
-
densa
-
35so4-labeled
- hno2
-
cuprolinic
-
6-o-sulfate
-
sulfate-binding
- glypican-1
The taxonomic range for the selected organisms is: Pedobacter heparinus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
heparitinase, heparinase iii, heparitinase i, hep i, hepiii, heparin lyase iii, heparan sulfate lyase, heparitin-sulfate lyase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
heparan sulfate lyase
-
-
-
-
heparin lyase III
-
-
-
-
heparin sulfate eliminase
-
-
-
-
heparin-sulfate eliminase
-
-
-
-
heparitin sulfate lyase
-
-
-
-
heparitin-sulfate lyase
-
-
-
-
heparitinase I
heparitinase II
-
-
-
-
lyase, heparin sulfate
-
-
-
-
heparitinase I
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
His295 and His510 are essential for catalytic activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
-
-
elimination of sulfate
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
heparin-sulfate lyase
Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages.
CAS REGISTRY NUMBER
COMMENTARY
37290-86-1
-
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
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
-
-
-
?
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
about 15fold higher catalytic efficiency than with 4-nitrophenyl beta-D-GlcA-(1->4)-alpha-D-GlcNS-(1->4)-beta-D-GlcA
-
-
?
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
-
-
-
?
beta-D-glucopyranosyluronic acid
?
-
major requirement for enzyme action is reduced sulfation, cannot cleave linkages containing unsulfated GalAP residues
-
-
?
heparan sulfate
non-sulfated di- and tetrasaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends + SO42-
hyaluronate
unsaturated hyaluronate disaccharide
-
no substrate of wild-type, but substrate of mutant K130C. Reaction of EC 4.2.2.1
-
-
?
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
?
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
-
-
?
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-
-
-
-
?
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
?
-
-
cleavage/degradation of heparin forming unsaturated uronic acid
-
-
?
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
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
inactivation, 80% reversible by hydroxylamine within 6 h, mapping of modified histidine residues
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.438
hyaluronate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
kinetic modeling based on inactivation data, overview
-
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
0.093
heparan sulfate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
hyaluronate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
56
heparan sulfate
-
mutant K130C, pH not specified in the publication, temperature not specified in the publication
68
heparan sulfate
-
wild-type, pH not specified in the publication, temperature not specified in the publication
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
propagated in bovine lung microvascular endothelial cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
differential effects of heparitinase I and heparitinase III, EC 4.2.2.7, 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 I cleaves heparin sulfate chains containing glucuronic acid residues adjacent to glucosamine residues containing either N-acetyl or N-sulfate groups. Hep I generates fragments that retain their growth factor binding capability and therefore still potentiate tube formation
additional information
-
intermolecular disulfide bond formation in HepI important for catalysis, overview
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). HEP1_PEDHE
384
0
43807
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
three-dimensional model structure, modelling based on the known crystal structure of Bacteroides thetaiotaomicron HepI, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform Hep III, to 2.2 A resolution. The enzyme comprises an N-terminal alpha/alpha-barrel domain and a C-terminal antiparallel beta-sheet domain as its basic scaffold. Isoform Hep III exhibits an open form compared with the closed form of Hep II. An active site of Hep III is located in the deep cleft at the interface between its two domains
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C297S
-
site-directed mutagenesis, the mutant suppresses the dimerization and shows 70% reduced activity compared to the wild-type enzyme
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
H241A
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
H424A
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
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
H241A
-
PCR overlap extension site-directed mutagenesis, highly reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes
H424A
-
PCR overlap extension site-directed mutagenesis, reduced Km and kcat
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39.4
melting temperature, presence of 1 mM heparin tetrasaccharide
40.5
melting temperature, presence of 0.1 mM heparin tetrasaccharide
43.9
melting temperature, presence of 0.1 mM heparin disaccharide
44.3
melting temperature, presence of 0.1 mM N-acetyl glucosamine
45.2
melting temperature, presence of 0.1 mM gellan tetrasaccharide
additional information
-
the inactivation shows strong concentration dependence. Acceleration of the inactivation with the increase of enzyme concentration implies multi-molecular interactions in the thermal inactivation. Strong reversibility of the unfolding of MBP-HepI, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant maltose-binding protein fusion HepI, MBP-HepI, from Escherichia coli by affinity and anion exchange chromatography, followed by gel filtration to apparent homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of maltose-binding protein fusion HepI, MBP-HepI, in Escherichia coli
-
expression of N-terminally His-tagged wild-type and mutant enzymes in Escherichia coli, recombinant wild-type enzyme shows a lower activity than the native one
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
temperature-induced reactivation of MBP-HepI, when the temperature is lowered from 35°C to 4°C, the rate constant of unfolding decreases by 6000times while that of refolding decreases by only 600times, MBP-HepI undergoes reactivation during the cooling treatment at 4°C after incubation at 35°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
analysis of heparitinase induced changes in Xenopus laevis embryos
synthesis
construcution of a photoswitchable biocatalyst consisating of a heparinase III mutant K130C-N,N-dimethylacrylamide-co-4-phenyl azophenyl acrylate copolymer. Upon photoswitch, the enzymatic degradation of heparin can be artificially controlled to produce low molecular weight heparin with more uniform molecular weight and an increase in anticoagulant activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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)
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
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