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
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quinolinic
- kynureninase
-
quin
-
2,3-dioxygenase
-
3-monooxygenase
-
excitotoxin
-
phosphoribosyltransferase
-
kynurenine-oxoglutarate
- aminocarboxymuconate-semialdehyde
-
kynurenic
- 3-hydroxykynurenine
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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-
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General Information
General Information on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase
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evolution
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HAD belongs to the class of nonheme iron(II) enzymes and shares functional similarity with extradiol-cleaving catechol dioxygenases
metabolism
3-hydroxyanthranilate 3,4-dioxygenase (3HAO) is an enzyme in the microglial branch of the kynurenine pathway of tryptophan degradation
physiological function
additional information
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the enzyme catalyzes the degradation of 3-hydroxyanthranilate to quinolinate in the presence of dioxygen
physiological function
enzyme 3HAO is a non-heme iron-containing, ring-cleaving extradiol dioxygenase that catalyzes the addition of both atoms of O2 to the kynurenine pathway metabolite 3-hydroxyanthranilic acid (3-HANA) to form quinolinic acid. Quinolinic acid is a highly potent excitotoxin that is implicated in a number of neurodegenerative conditions
physiological function
the enzyme catalyses the cleavage of the benzene ring of 3-hydroxyanthranilic acid (3-Ohaa), an intermediate in the kynurenine pathway
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oxidative CC bond cleavage of 2-amino-4-tert-butylphenolate on complex nonheme iron(II) complex, [(6-Me3-TPA)FeII(4-tBu-HAP)](ClO4) is mimicking the enzyme function. The iron(II)-aminophenolate complex reacts with molecular oxygen in acetonitrile under ambient conditions, overview
additional information
enzyme molecular modeling, the water population of the active site, and the protein flexibility as well as the amino acid residues interaction networks are relevant for the enzyme activity, hybrid quantum-mechanics/molecular-mechanics (QM/MM) calculations
additional information
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enzyme molecular modeling, the water population of the active site, and the protein flexibility as well as the amino acid residues interaction networks are relevant for the enzyme activity, hybrid quantum-mechanics/molecular-mechanics (QM/MM) calculations
additional information
residue Met35 is involved in interactions with substrates and inhibitors
additional information
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residue Met35 is involved in interactions with substrates and inhibitors