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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Engineering
Engineering on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase
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I142A
the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
I142P
the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
N27A
the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
R47A
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kcat/Km is 7440fold lower than wild-type enzyme. Mutant enzyme shows substrate inhibition
I142A
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the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
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I142P
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the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
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N27A
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the variant cannot form a closed conformation and has a substantially higher Km for O2 than wild-type enzyme
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Q105A
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding
R43A
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding
R95A
site-directed mutagenesis, the mutation affects the enzyme activity, the protein structure, particularly the active site architecture and the metal ion environment, and the substrate binding