1.13.11.47: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
This is an abbreviated version!
For detailed information about 3-hydroxy-4-oxoquinoline 2,4-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.47
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1.13.11.47
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putida
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dioxygenolytic
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arthrobacter
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alpha/beta
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alpha/beta-hydrolase
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hydrolases
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cofactor-free
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anthranilate
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dioxygenation
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epr
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vapour-diffusion
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his6-tagged
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base-catalyzed
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ilicis
- 1.13.11.47
- putida
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dioxygenolytic
- arthrobacter
- alpha/beta
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alpha/beta-hydrolase
- hydrolases
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cofactor-free
- anthranilate
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dioxygenation
- epr
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vapour-diffusion
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his6-tagged
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base-catalyzed
- ilicis
Reaction
Synonyms
(1H)-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase, 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, 1H-3-Hydroxy-4-oxo-quinoline oxygenase, 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase, 1H-3-Hydroxy-4-oxoquinoline oxygenase, 3,4-dihydroxyquinoline 2,4-dioxygenase, 3-Hydroxy-4(1H)-one, 2,4-dioxygenase, 3-Hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase, EC 1.12.99.5, EC 1.13.99.5, HOD, MeQDO, More, Oxygenase, 1H-3-hydroxy-4-oxoquinoline 2,4-di, QDO, Quinoline-3,4-diol 2,4-dioxygenase, quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)
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Substrates Products
Substrates Products on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
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REACTION DIAGRAM
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism
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1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism
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N-Formylanthranilate + CO
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at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
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1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
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at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
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1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
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N-formylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
QDO possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism
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?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
QDO possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism
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active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview
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additional information
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active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview
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additional information
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substrate deprotonation under transient-state conditions is not rate-limiting and shows a pKa value of 7.2 for wild-type. A large solvent isotope effect is found, and the pKa value is shifted to 8.3 in D2O
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additional information
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active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview
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additional information
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N-heteroaromatic substrate binding and kinetics
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additional information
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N-heteroaromatic substrate binding and kinetics
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additional information
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N-heteroaromatic substrate binding and kinetics
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