BRENDA - Enzyme Database show
show all sequences of 4.2.2.8

Histidine 295 and histidine 510 are crucial for the enzymatic degradation of heparan sulfate by heparinase III

Pojasek, K.; Shriver, Z.; Hu, Y.; Sasisekharan, R.; Biochemistry 39, 4012-4019 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Pedobacter heparinus
Engineering
Amino acid exchange
Commentary
Organism
H105A
PCR overlap extension site-directed mutagenesis, very low expression level, no measurement of activity possible, reduced expression level
Pedobacter heparinus
H110A
PCR overlap extension site-directed mutagenesis, reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes, reduced expression level
Pedobacter heparinus
H139A
PCR overlap extension site-directed mutagenesis, reduced kcat and increased Km compared to both recombinant and native wild-type enzymes, reduced expression level
Pedobacter heparinus
H152A
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
Pedobacter heparinus
H225A
PCR overlap extension site-directed mutagenesis, Km is the same as for the recombinant wild-type, reduced kcat
Pedobacter heparinus
H234A
PCR overlap extension site-directed mutagenesis, Km is similar to the recombinant wild-type, reduced kcat
Pedobacter heparinus
H241A
PCR overlap extension site-directed mutagenesis, highly reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes
Pedobacter heparinus
H295A
PCR overlap extension site-directed mutagenesis, inactive mutant
Pedobacter heparinus
H36A
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
Pedobacter heparinus
H424A
PCR overlap extension site-directed mutagenesis, reduced Km and kcat
Pedobacter heparinus
H469A
PCR overlap extension site-directed mutagenesis, reduced Km and increased kcat compared to both recombinant and native wild-type enzymes
Pedobacter heparinus
H510A
PCR overlap extension site-directed mutagenesis, inactive mutant
Pedobacter heparinus
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
Pedobacter heparinus
Inhibitors
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
inactivation, 80% reversible by hydroxylamine within 6 h, mapping of modified histidine residues
Pedobacter heparinus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
heparan sulfate
mutant H110A, pH 7.6, 35°C
Pedobacter heparinus
0.016
-
heparan sulfate
mutant H241A, pH 7.6, 35°C
Pedobacter heparinus
0.058
-
heparan sulfate
mutant H152A, pH 7.6, 35°C
Pedobacter heparinus
0.059
-
heparan sulfate
mutant H424A, pH 7.6, 35°C
Pedobacter heparinus
0.071
-
heparan sulfate
mutant H469A, pH 7.6, 35°C
Pedobacter heparinus
0.075
-
heparan sulfate
mutant H234A, pH 7.6, 35°C
Pedobacter heparinus
0.08
-
heparan sulfate
recombinant wild-type enzyme and mutant H225A, pH 7.6, 35°C
Pedobacter heparinus
0.092
-
heparan sulfate
mutant H539A, pH 7.6, 35°C
Pedobacter heparinus
0.098
-
heparan sulfate
mutant H36A, pH 7.6, 35°C
Pedobacter heparinus
0.143
-
heparan sulfate
native wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
0.191
-
heparan sulfate
mutant H139A, pH 7.6, 35°C
Pedobacter heparinus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pedobacter heparinus
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutants from Escherichia coli
Pedobacter heparinus
Reaction
Reaction
Commentary
Organism
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
Pedobacter heparinus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
heparan sulfate
-
649969
Pedobacter heparinus
?
-
649969
Pedobacter heparinus
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at
Pedobacter heparinus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5
-
heparan sulfate
mutant H241A, pH 7.6, 35°C
Pedobacter heparinus
22
-
heparan sulfate
mutant H225A, pH 7.6, 35°C
Pedobacter heparinus
23
-
heparan sulfate
mutant H234A, pH 7.6, 35°C
Pedobacter heparinus
24
-
heparan sulfate
mutant H424A, pH 7.6, 35°C
Pedobacter heparinus
37
-
heparan sulfate
mutant H110A, pH 7.6, 35°C
Pedobacter heparinus
68
-
heparan sulfate
mutant H139A, pH 7.6, 35°C
Pedobacter heparinus
78
-
heparan sulfate
recombinant wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
83
-
heparan sulfate
mutant H152A, pH 7.6, 35°C
Pedobacter heparinus
86
-
heparan sulfate
mutant H36A, pH 7.6, 35°C
Pedobacter heparinus
94
-
heparan sulfate
native wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
100
-
heparan sulfate
mutant H469A, pH 7.6, 35°C
Pedobacter heparinus
132
-
heparan sulfate
mutant H539A, pH 7.6, 35°C
Pedobacter heparinus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Pedobacter heparinus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inactivation kinetics
Pedobacter heparinus
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Pedobacter heparinus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H105A
PCR overlap extension site-directed mutagenesis, very low expression level, no measurement of activity possible, reduced expression level
Pedobacter heparinus
H110A
PCR overlap extension site-directed mutagenesis, reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes, reduced expression level
Pedobacter heparinus
H139A
PCR overlap extension site-directed mutagenesis, reduced kcat and increased Km compared to both recombinant and native wild-type enzymes, reduced expression level
Pedobacter heparinus
H152A
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
Pedobacter heparinus
H225A
PCR overlap extension site-directed mutagenesis, Km is the same as for the recombinant wild-type, reduced kcat
Pedobacter heparinus
H234A
PCR overlap extension site-directed mutagenesis, Km is similar to the recombinant wild-type, reduced kcat
Pedobacter heparinus
H241A
PCR overlap extension site-directed mutagenesis, highly reduced kcat, highly reduced Km compared to both recombinant and native wild-type enzymes
Pedobacter heparinus
H295A
PCR overlap extension site-directed mutagenesis, inactive mutant
Pedobacter heparinus
H36A
PCR overlap extension site-directed mutagenesis, reduced Km and a kcat value between the recombinant and the native wild-type enzyme
Pedobacter heparinus
H424A
PCR overlap extension site-directed mutagenesis, reduced Km and kcat
Pedobacter heparinus
H469A
PCR overlap extension site-directed mutagenesis, reduced Km and increased kcat compared to both recombinant and native wild-type enzymes
Pedobacter heparinus
H510A
PCR overlap extension site-directed mutagenesis, inactive mutant
Pedobacter heparinus
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
Pedobacter heparinus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
diethyl dicarbonate
inactivation, 80% reversible by hydroxylamine within 6 h, mapping of modified histidine residues
Pedobacter heparinus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
additional information
-
additional information
inactivation kinetics
Pedobacter heparinus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.009
-
heparan sulfate
mutant H110A, pH 7.6, 35°C
Pedobacter heparinus
0.016
-
heparan sulfate
mutant H241A, pH 7.6, 35°C
Pedobacter heparinus
0.058
-
heparan sulfate
mutant H152A, pH 7.6, 35°C
Pedobacter heparinus
0.059
-
heparan sulfate
mutant H424A, pH 7.6, 35°C
Pedobacter heparinus
0.071
-
heparan sulfate
mutant H469A, pH 7.6, 35°C
Pedobacter heparinus
0.075
-
heparan sulfate
mutant H234A, pH 7.6, 35°C
Pedobacter heparinus
0.08
-
heparan sulfate
recombinant wild-type enzyme and mutant H225A, pH 7.6, 35°C
Pedobacter heparinus
0.092
-
heparan sulfate
mutant H539A, pH 7.6, 35°C
Pedobacter heparinus
0.098
-
heparan sulfate
mutant H36A, pH 7.6, 35°C
Pedobacter heparinus
0.143
-
heparan sulfate
native wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
0.191
-
heparan sulfate
mutant H139A, pH 7.6, 35°C
Pedobacter heparinus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutants from Escherichia coli
Pedobacter heparinus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
heparan sulfate
-
649969
Pedobacter heparinus
?
-
649969
Pedobacter heparinus
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
assay at
Pedobacter heparinus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5
-
heparan sulfate
mutant H241A, pH 7.6, 35°C
Pedobacter heparinus
22
-
heparan sulfate
mutant H225A, pH 7.6, 35°C
Pedobacter heparinus
23
-
heparan sulfate
mutant H234A, pH 7.6, 35°C
Pedobacter heparinus
24
-
heparan sulfate
mutant H424A, pH 7.6, 35°C
Pedobacter heparinus
37
-
heparan sulfate
mutant H110A, pH 7.6, 35°C
Pedobacter heparinus
68
-
heparan sulfate
mutant H139A, pH 7.6, 35°C
Pedobacter heparinus
78
-
heparan sulfate
recombinant wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
83
-
heparan sulfate
mutant H152A, pH 7.6, 35°C
Pedobacter heparinus
86
-
heparan sulfate
mutant H36A, pH 7.6, 35°C
Pedobacter heparinus
94
-
heparan sulfate
native wild-type enzyme, pH 7.6, 35°C
Pedobacter heparinus
100
-
heparan sulfate
mutant H469A, pH 7.6, 35°C
Pedobacter heparinus
132
-
heparan sulfate
mutant H539A, pH 7.6, 35°C
Pedobacter heparinus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Pedobacter heparinus
Other publictions for EC 4.2.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748820
Gu
Photoswitchable heparinase II ...
Pedobacter heparinus
Org. Lett.
20
48-51
2018
-
1
-
-
-
-
-
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-
-
-
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1
-
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747456
Hu
Probing cleavage promiscuity ...
Pedobacter heparinus
Carbohydr. Polym.
173
276-285
2017
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
16
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747570
Gu
Expanding the catalytic promi ...
Pedobacter heparinus
Chemistry
23
2548-2551
2017
-
-
-
-
3
-
-
5
-
-
2
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
5
-
-
2
-
-
-
-
-
-
-
-
-
3
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
747916
Ulaganathan
Conformational flexibility of ...
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079
Glycobiology
27
176-187
2017
-
-
1
1
3
-
-
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747454
Carnachan
Determining the extent of hep ...
Pedobacter heparinus
Carbohydr. Polym.
152
592-597
2016
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
729269
Hashimoto
Crystal structure of Pedobacte ...
Pedobacter heparinus, Pedobacter heparinus DSM 2366
Biochemistry
53
777-786
2014
-
-
-
1
11
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
1
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
730858
Dong
Structural basis of heparan su ...
Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079
Protein Cell
3
950-961
2012
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714553
Chen
Biochemical analysis and kinet ...
Pedobacter heparinus
Biotechnol. Bioeng.
108
1841-1851
2011
-
-
1
-
1
1
11
1
-
1
-
-
-
1
-
-
1
-
1
-
1
1
1
1
1
-
3
-
1
-
-
-
-
-
-
-
-
1
-
-
1
1
-
11
-
1
-
1
-
-
-
-
-
1
1
-
1
1
1
1
1
-
3
-
1
-
-
-
-
1
1
-
-
-
701676
Babu
Fluorescent-tagged heparan sul ...
Pedobacter heparinus
Anal. Biochem.
396
124-132
2010
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
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-
-
-
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-
-
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1
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-
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1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701885
Hyun
Cloning, overexpression, and c ...
Bacteroides stercoris, Bacteroides stercoris HJ-15
Appl. Microbiol. Biotechnol.
86
879-890
2010
-
-
1
-
4
-
3
2
-
3
1
-
-
5
-
-
1
-
-
-
5
-
6
1
1
1
1
-
1
1
-
-
-
1
-
-
-
1
-
-
4
-
-
3
-
2
-
3
1
-
-
-
-
1
-
-
5
-
6
1
1
1
1
-
1
1
-
1
-
-
-
-
-
-
714027
Raman
Differential effects of hepari ...
Pedobacter heparinus
Biochem. Biophys. Res. Commun.
398
191-193
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
682098
Rops
Heparan sulfate on activated g ...
Pedobacter heparinus
Nephrol. Dial. Transplant.
22
1070-1077
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
665613
Wei
Distinct substrate specificiti ...
Pedobacter heparinus
J. Biol. Chem.
280
15742-15748
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
664047
Chai
Relative susceptibilities of t ...
Pedobacter heparinus
Biochemistry
43
8590-8599
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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1
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-
649969
Pojasek
Histidine 295 and histidine 51 ...
Pedobacter heparinus
Biochemistry
39
4012-4019
2000
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1
-
13
-
1
11
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2
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1
1
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1
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1
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12
1
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1
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1
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13
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1
1
11
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1
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-
1
-
1
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-
12
1
-
-
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-
37411
Graham
Inhibition of platelet heparit ...
Homo sapiens
Biochem. Mol. Biol. Int.
37
239-246
1995
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-
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2
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1
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1
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2
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1
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37409
Yamada
Structural studies on the tri- ...
Pedobacter heparinus
Glycobiology
4
69-78
1994
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-
-
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1
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1
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-
1
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37410
Suhahara
Structural studies on the olig ...
Pedobacter heparinus
Glycobiology
4
535-544
1994
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-
-
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4
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2
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1
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1
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2
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-
1
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1
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37412
Brickman
Heparitinase inhibition of mes ...
Pedobacter heparinus
Dev. Biol.
164
484-501
1994
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1
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4
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1
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1
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1
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37407
Desai
Specificity studies on the hep ...
Pedobacter heparinus
Biochemistry
32
8140-8145
1993
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1
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2
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1
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5
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1
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1
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1
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5
-
1
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37406
Nader H.B.; Porcionatto M.A.; Tersariol
Purification and substrate spe ...
Pedobacter heparinus
J. Biol. Chem.
265
16807-16813
1990
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1
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2
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1
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6
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1
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1
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1
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6
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1
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37408
Linhardt
Examination of the substrate s ...
Pedobacter heparinus
Biochemistry
29
2611-2617
1990
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1
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2
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1
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2
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1
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1
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1
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1
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-
2
-
1
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1
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37404
Nader
Heparin sequences in the hepar ...
Pedobacter heparinus
Proc. Natl. Acad. Sci. USA
84
3565-3569
1987
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1
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2
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2
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2
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37405
Prinz
Metabolism of sulfated glycosa ...
Rattus norvegicus
Biochim. Biophys. Acta
630
402-413
1980
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-
-
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1
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1
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1
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1
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1
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1
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2
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1
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5978
Hovingh
The enzymatic degradation of h ...
Flavobacteriia
J. Biol. Chem.
245
6170-6175
1970
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-
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5
-
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3
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2
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1
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1
1
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1
1
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1
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-
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5
-
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3
-
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1
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1
1
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1
1
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1
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