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Information on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase and Organism(s) Bos taurus and UniProt Accession Q0VCA8

for references in articles please use BRENDA:EC1.13.11.6

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EC Tree

1 Oxidoreductases

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.11 With incorporation of two atoms of oxygen

1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase

Requires Fe2+.

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Bos taurus

UNIPROT: Q0VCA8

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Word Map

1.13.11.6
quinolinic
kynureninase
quin
2,3-dioxygenase
3-monooxygenase
excitotoxin
phosphoribosyltransferase
kynurenine-oxoglutarate
aminocarboxymuconate-semialdehyde
kynurenic
3-hydroxykynurenine
ibotenic
epilepsy-prone
picolinic
drug development
medicine
pharmacology

The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

Reaction Schemes

3-hydroxyanthranilate

+

=

2-amino-3-carboxymuconate semialdehyde

+

=

Synonyms

3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilic acid oxygenase, 3-hao, 3-hydroxyanthranilate oxygenase, 3-had, show all synonyms

show all synonyms

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Go to Synonym Search

3-hydroxyanthranilate 3,4-dioxygenase

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3HAO

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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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3HAO

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oxygenase, 3-hydroxyanthranilate 3,4-di-

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Go to Reaction Type Search

redox reaction

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oxidation

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reduction

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Go to Pathway Search

BRENDA

tryptophan metabolism

KEGG

Tryptophan metabolism

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-, -, -, -

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Go to Systematic Name Search

3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)

Requires Fe2+.

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Go to CAS Registry Number Search

9029-50-9

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Go to Substrate/Product Search

2-amino-3-hydroxybenzoic acid + O2

2,3-pyridinedicarboxylic acid + H2O

show the reaction diagram

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intermediate 2-amino-3-carboxymuconic acid semialdehyde

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?

3-hydroxy-4-methylanthranilic acid + O2

?

show the reaction diagram

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-

-

?

3-hydroxyanthranilate + O2

2-amino-3-carboxymuconate semialdehyde

show the reaction diagram

show

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Go to Natural Substrate Search

2-amino-3-hydroxybenzoic acid + O2

2,3-pyridinedicarboxylic acid + H2O

show the reaction diagram

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intermediate 2-amino-3-carboxymuconic acid semialdehyde

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?

3-hydroxyanthranilate + O2

2-amino-3-carboxymuconate semialdehyde

show the reaction diagram

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?

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Go to Metals and Ions Search

(NH4)2SO4

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the most effective salt, the optimal concentration is 0.035 M

Fe2+

show

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

MgCl2

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NaCl

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-

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Go to Inhibitor Search

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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Go to Activating Compound Search

Triton X-100

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-

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Go to KM Value Search

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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Go to Ki Value Search

12

6-chloro-3-hydroxyanthranilic acid

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2 - 6.5

anthranilic acid

show

1.8

quinolinic acid

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for the pI 5.6 enzyme

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Go to Specific Activity Search

115.7

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last purification step

140

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additional information

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reaches a maximum after 10 min at acid pH

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Go to pH Optimum Search

6.9 - 7.4

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Go to pH Range Search

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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Go to Temperature Range Search

55

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activation by heating at 55°C for 5 min

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Go to Pi Value Search

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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Go to Organism Search

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UniProt

Manually annotated by BRENDA team

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Go to Source Tissue Search

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Manually annotated by BRENDA team

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Manually annotated by BRENDA team

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Manually annotated by BRENDA team

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Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

3HAO_BOVIN

286

0

32493

Swiss-Prot

other Location (Reliability: 4)

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Go to PDB and Structure Links Search

3fe5, download, 3D-view

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Go to Molecular Weight Search

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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Go to Subunit Search

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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Go to Crystallization (commentary) Search

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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Go to pH Stability Search

10

-

4°C, half-life: 3 days

439364

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Go to Temperature Stability Search

0 - 4

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stable for a month, in Tris-maleate buffer, pH 6.5

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Go to Organic Solvent Search

additional information

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drastic change in the Km of the enzyme in the presence of dimethylglutarate buffer

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Go to Storage Stability Search

-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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Go to Purification (commentary) Search

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

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succesive size exclusion and affinity columns

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top print hide References Search

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

Manually annotated by BRENDA team

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

Manually annotated by BRENDA team

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

Manually annotated by BRENDA team

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

Manually annotated by BRENDA team

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Release 2023.1 (January 2023)