1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase
This is an abbreviated version!
For detailed information about 3-hydroxyanthranilate 3,4-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.6
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1.13.11.6
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quinolinic
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kynureninase
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quin
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2,3-dioxygenase
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3-monooxygenase
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excitotoxin
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phosphoribosyltransferase
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kynurenine-oxoglutarate
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aminocarboxymuconate-semialdehyde
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kynurenic
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3-hydroxykynurenine
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ibotenic
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epilepsy-prone
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picolinic
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drug development
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medicine
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pharmacology
- 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
Reaction
Synonyms
3-HAD, 3-HAO, 3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-hydroxyanthranilic acid oxidase, 3-hydroxyanthranilic acid oxygenase, 3-hydroxyanthranilic oxygenase, 3HAO, EC 1.13.1.6, HAD, HAO, oxygenase, 3-hydroxyanthranilate 3,4-di-
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase
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Fe
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each monomer contains two iron binding sites. The catalytic iron is buried deep inside the beta-barrel with His51, Glu57, and His95 serving as ligands. The other iron site forms an FeS4 center close to the solvent surface in which the sulfur atoms are provided by Cys125, Cys128, Cys162, and Cys165. The two iron sites are separated by 24 A
Fe2+
Iron
Ni2+
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two nickel binding sites per molecule. One of the bound nickel atoms occupies the proposed ferrous-coordinated active site
additional information
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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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required, the active site of HAD contains an iron(II) center that is coordinated by the 2-His-1-Glu facial triad
enhanced hydrophobicity at the iron center results from the concerted loop movements after the binding of the primary substrate
comparison of the active sites of Fe(III)-h3HAO and Zn(II)-h3HAO enzymes, overview
additional information
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comparison of the active sites of Fe(III)-h3HAO and Zn(II)-h3HAO enzymes, overview