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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Crystallization
Crystallization on EC 1.13.11.6 - 3-hydroxyanthranilate 3,4-dioxygenase
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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
seven catalytic intermediates are kinetically and structurally resolved in the crystalline state, and each accompanies protein conformational changes at the active site. Among them, a monooxygenated, seven-membered lactone intermediate as a monodentate ligand of the iron center at 1.59 A resolution is captured, which presumably corresponds to a substrate-based radical species observed by EPR using a slurry of small-sized single crystals. Other structural snapshots determined at around 2.0 A resolution include monodentate and subsequently bidentate coordinated substrate, superoxo, alkylperoxo, and two metal-bound enol tautomers of the unstable dioxygenase product
purified recombinant detagged enzyme in complex with Zn2+ or Fe2+, protein with zinc sulfate or iron sulfate best from 0.1 M HEPES, pH 7.5, 2% PEG 400, and 2.0 M ammonium sulfate., in 2-7 days, X-ray diffraction structure determination and analysis at 1.75-1.88 A resolution, modeling