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show all sequences of 4.2.2.19

Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum

Li, Y.; Matte, A.; Su, H.; Cygler, M.; Acta Crystallogr. Sect. D 55, 1055-1057 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression of enzyme, residues 25-506, in Flavobacterium heparinum cells
Pedobacter heparinus
Crystallization (Commentary)
Crystallization
Organism
6-8 mg/ml purified recombinant enzyme, residues 25-506, in 20 mM Tris-HCl, pH 8.0, 1 mM sodium phosphate, pH 7.0, 3 mM NaCl, 0.5 mM phenylmethylsulfonyl fluoride, 0.001 mg/ml aprotinin, 0.001 mg/ml leupeptin, 0.001 mg/ml E64, hanging drop vapour diffusion method, 292 K, mixed with a double volume of reservoir solution containing 19% w/v PEG 8000, 100 mM bicine buffer, pH 9.0, or 100 mM Tris-HCl, pH 8.8, 0.15 M ammonium acetate, 15% v/v 2-methyl-2,4-pentanediol, drops are suspended over 1 ml of resevroir solution, crystals appear overnight, seeds are introduced into drops conisting of 0.002 ml protein solution, 6.1 mg/ml protein, and 0.004 ml reservoir solution containing 16.5% w/v PEG 8000, 0.1 M Tris-HCl, pH 8.8, 15% v/v 2-methyl-2,4-pentanediol, 0.25 M ammonium acetate, 292 K, 2-3 weeks, X-ray diffraction structure determination and analysis at 2.20-2.28 A resolution
Pedobacter heparinus
General Stability
General Stability
Organism
protease inhibitors like aprotinin, leupeptin or E64 are required for stability of the enzyme during storage at 277 K
Pedobacter heparinus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pedobacter heparinus
Q46079
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme comprising residues 25-506 overexpressed in Flavobacterium heparinum cells, to homogeneity
Pedobacter heparinus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dermatan sulfate
-
649099
Pedobacter heparinus
unsaturated dermatan sulfate oligosaccharide
-
649099
Pedobacter heparinus
?
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of enzyme, residues 25-506, in Flavobacterium heparinum cells
Pedobacter heparinus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
6-8 mg/ml purified recombinant enzyme, residues 25-506, in 20 mM Tris-HCl, pH 8.0, 1 mM sodium phosphate, pH 7.0, 3 mM NaCl, 0.5 mM phenylmethylsulfonyl fluoride, 0.001 mg/ml aprotinin, 0.001 mg/ml leupeptin, 0.001 mg/ml E64, hanging drop vapour diffusion method, 292 K, mixed with a double volume of reservoir solution containing 19% w/v PEG 8000, 100 mM bicine buffer, pH 9.0, or 100 mM Tris-HCl, pH 8.8, 0.15 M ammonium acetate, 15% v/v 2-methyl-2,4-pentanediol, drops are suspended over 1 ml of resevroir solution, crystals appear overnight, seeds are introduced into drops conisting of 0.002 ml protein solution, 6.1 mg/ml protein, and 0.004 ml reservoir solution containing 16.5% w/v PEG 8000, 0.1 M Tris-HCl, pH 8.8, 15% v/v 2-methyl-2,4-pentanediol, 0.25 M ammonium acetate, 292 K, 2-3 weeks, X-ray diffraction structure determination and analysis at 2.20-2.28 A resolution
Pedobacter heparinus
General Stability (protein specific)
General Stability
Organism
protease inhibitors like aprotinin, leupeptin or E64 are required for stability of the enzyme during storage at 277 K
Pedobacter heparinus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme comprising residues 25-506 overexpressed in Flavobacterium heparinum cells, to homogeneity
Pedobacter heparinus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dermatan sulfate
-
649099
Pedobacter heparinus
unsaturated dermatan sulfate oligosaccharide
-
649099
Pedobacter heparinus
?
Other publictions for EC 4.2.2.19
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)
747452
Wu
Establishment of chondroitin ...
Pedobacter heparinus, Pedobacter heparinus DSM 2366
Carbohydr. Polym.
144
338-345
2016
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692532
Volpi
Structural characterization an ...
Pedobacter heparinus
Glycobiology
19
356-367
2008
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677536
Oguma
Analytical method for the dete ...
Pedobacter heparinus
Anal. Biochem.
368
79-86
2007
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677405
Makovitzky
Topooptical investigations and ...
Pedobacter heparinus
Acta Histochem.
108
193-196
2006
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680938
Nakamura
Glycosaminoglycan degradation ...
Pedobacter heparinus
J. Biomed. Mater. Res. A
77
478-486
2006
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652553
Michel
The structure of chondroitin B ...
Pedobacter heparinus
J. Biol. Chem.
279
32882-32896
2004
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652290
Pojasek
Biochemical characterization o ...
Pedobacter heparinus
J. Biol. Chem.
277
31179-31186
2002
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652640
Suzuki
Inhibition of hyaluronidases a ...
Pedobacter heparinus
J. Enzyme Inhib. Med. Chem.
17
183-186
2002
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25
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649575
Pojasek
Recombinant expression, purifi ...
Pedobacter heparinus
Biochem. Biophys. Res. Commun.
286
343-351
2001
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651192
Denholm
Anti-tumor activities of chond ...
Homo sapiens
Eur. J. Pharmacol.
416
213-221
2001
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649356
Tkalec
Isolation and expression in Es ...
Pedobacter heparinus
Appl. Environ. Microbiol.
66
29-35
2000
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649099
Li
Crystallization and preliminar ...
Pedobacter heparinus
Acta Crystallogr. Sect. D
55
1055-1057
1999
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652806
Huang
Crystal structure of chondroit ...
Pedobacter heparinus
J. Mol. Biol.
294
1257-1269
1999
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34100
Gu
Purification, characterization ...
Pedobacter heparinus
Biochem. J.
312
569-577
1995
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650773
Ototani
Purification of chondroitinase ...
Pedobacter heparinus
Carbohydr. Res.
70
295-306
1979
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