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EC Tree
The taxonomic range for the selected organisms is: Bos taurus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hao, 3-hydroxyanthranilate oxygenase, 3-had,
more
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3-hydroxyanthranilate 3,4-dioxygenase
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3-hydroxyanthranilate oxygenase
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3-hydroxyanthranilic acid oxidase
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3-hydroxyanthranilic acid oxygenase
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3-hydroxyanthranilic oxygenase
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oxygenase, 3-hydroxyanthranilate 3,4-di-
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3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)
Requires Fe2+.
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2-amino-3-hydroxybenzoic acid + O2
2,3-pyridinedicarboxylic acid + H2O
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intermediate 2-amino-3-carboxymuconic acid semialdehyde
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?
3-hydroxy-4-methylanthranilic acid + O2
?
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-
-
?
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
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?
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
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?
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
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?
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2-amino-3-hydroxybenzoic acid + O2
2,3-pyridinedicarboxylic acid + H2O
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intermediate 2-amino-3-carboxymuconic acid semialdehyde
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?
3-hydroxyanthranilate + O2
2-amino-3-carboxymuconate semialdehyde
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?
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(NH4)2SO4
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the most effective salt, the optimal concentration is 0.035 M
Fe3+
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does not seem to bind to the enzyme
HCl
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during purification of enzyme treatment with acid was used
Fe2+
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solvent, acid and heat function to modify the protein configuration so that ferrous ions can be bound to the enzyme to generate the most active form
Fe2+
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one Fe2+ per active site
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6-chloro-3-hydroxyanthranilic acid
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5-20 mM, loss of enzymatic activity as a function of the inhibitor concentration
anthranilic acid
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competitive inhibition
p-chloromercuribenzoate
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quinolinic acid
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competitive inhibition
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36 - 57
3-hydroxy-4-methylanthranilic acid
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16 - 19
3-Hydroxyanthranilate
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0.021
3-hydroxyanthranilic acid
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12
6-chloro-3-hydroxyanthranilic acid
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1.8
quinolinic acid
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for the pI 5.6 enzyme
2
anthranilic acid
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for the pI 4.98 enzyme
4.9
anthranilic acid
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for the pI 4.98 enzyme
6.5
anthranilic acid
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for the pI 5.6 enzyme
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115.7
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last purification step
additional information
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reaches a maximum after 10 min at acid pH
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additional information
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at pH 3.4: the enzyme is in a form which can bind substrate but is enzymatically inactive, at pH 6.5: active form of enzyme
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55
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activation by heating at 55°C for 5 min
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4.98
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chromatofocusing in PBE 94 gel exchanger and polybuffer 74, pH 4-7.4
5.6
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chromatofocusing in PBE 94 gel exchanger and polybuffer 74, pH 4-7.4
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UniProt
brenda
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brenda
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brenda
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brenda
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3HAO_BOVIN
286
0
32493
Swiss-Prot
other Location (Reliability: 4 )
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33000
SDS-PAGE, nondenaturating PAGE resolves two components, purified by FPLC on protein PakGlass DEAE-4 PW column, one component is N-terminally truncated annexin IV
32520
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PAGE in nondenaturing conditions, pI 4.98 enzyme
32570
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PAGE in nondenaturing conditions, pI 5.6 enzyme
33000
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SDS-PAGE, for the two active enzyme solutions obtained from hydroxyapatite column
33000 - 34000
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gel filtration
34000
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gel filtration, readily aggregates to form inactive higher molecular weight oligomers
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monomer
1 * 33000, SDS-PAGE, 286 amino acids, 2 domains that represent the dimers of the prokaryote enzyme structure which is also conserved in simple eukaryotes
monomer
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1 * 33000-34000, gel filtration
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first vapor diffusion with sitting drop method starting from protein concentration of 10 mg/ml in 32% (NH4)2SO4, 0.1 M sodium acetate, 10 mM 2-mercaptoethanol, pH 5, subsequently, crystals can be obtained by seeding starting from fragments of first crystallization experiments using 40% (NH4)2SO4, Tris-HCl, 40 mM MgCl2, 3% MPD, pH 8 as precipitant
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10
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4°C, half-life: 3 days
439364
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0 - 4
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stable for a month, in Tris-maleate buffer, pH 6.5
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additional information
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drastic change in the Km of the enzyme in the presence of dimethylglutarate buffer
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-15°C, in 0.01 M Tris buffer, pH 7.0, 4 days, no loss of activity
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-90°C, frozen in dry ice-ethanol bath, partially purified enzyme is stable for at least 1 month, purified enzyme is unstable
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0°C, 0.01 M collidine chloride, 0.01 M potassium chloride, pH 6.5, about 15% loss of activity after 1 month, purified enzyme
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4°C, overnight, about 75% loss of activity
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bovine kidney homogenized in 0.1 M potassium dihydrogen phosphate buffer with 20% glycerol and 3 mM 2-mercaptoethanol, pH 7.4, centrifuged, protein fraction of supernatant that precipitates from 34-62% saturated (NH4)2SO4 is resuspended in 5 mM potassium dihydrogen phosphate buffer with 20% glycerol and 3 mM 2-mercaptoethanol, pH 7.4, dialyzed against same buffer containing protease inhibitor PMSF (0.1 mM), applied to DEAE Sephadex A-50 column, fractions with enzyme activity pooled and concentrated by precipitation with 80%-saturated (NH4)2SO4, dialyzed against 10 mM Tris-HCl with 20% glycerol and 3 mM 2-mercaptoethanol, pH 7.4, applied to Blue-Sepharose CL-4B column, concentration of active fractions by ultrafiltration through YM-10 membrane
succesive size exclusion and affinity columns
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Decker, R.H.; Kang, H.H.; Leach, F.R.; Henderson, L.M.
Purification and properties of 3-hydroxyanthranilic acid oxidase
J. Biol. Chem.
236
3076-3082
1961
Bos taurus
brenda
Koontz, W.A.; Shiman, R.
Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay
J. Biol. Chem.
251
368-377
1976
Bos taurus
brenda
Nandi, D.; Lightcap, E.S.; Koo, Y.K.; Lu, X.; Quancard, J.; Silverman, R.B.
Purification and inactivation of 3-hydroxyanthranilic acid 3,4-dioxygenase from beef liver
Int. J. Biochem. Cell Biol.
35
1085-1097
2003
Bos taurus
brenda
Dilovic, I.; Gliubich, F.; Malpeli, G.; Zanotti, G.; Matkovic-Calogovic, D.
Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase
Biopolymers
91
1189-1195
2009
Bos taurus (Q0VCA8), Bos taurus
brenda