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Information on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
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1.13.11.47 3-hydroxy-4-oxoquinoline 2,4-dioxygenaseIUBMB Comments
Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate.
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Word Map
- 1.13.11.47
- putida
-
dioxygenolytic
- arthrobacter
- alpha/beta
-
alpha/beta-hydrolase
- hydrolases
-
cofactor-free
- anthranilate
-
dioxygenation
- epr
-
vapour-diffusion
-
his6-tagged
-
base-catalyzed
- ilicis
The enzyme appears in viruses and cellular organisms
Synonyms
1h-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase, 1h-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, meqdo, 1h-3-hydroxy-4-oxoquinoline oxygenase, 1-h-3-hydroxy-4-oxoquinoline 2,4-dioxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1H)-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
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-
-
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1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
1H-3-Hydroxy-4-oxo-quinoline oxygenase
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-
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1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
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-
-
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1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
1H-3-Hydroxy-4-oxoquinoline oxygenase
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-
-
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3,4-dihydroxyquinoline 2,4-dioxygenase
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-
-
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3-Hydroxy-4(1H)-one, 2,4-dioxygenase
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3-Hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase
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EC 1.12.99.5
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formerly
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EC 1.13.99.5
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formerly
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HOD
MeQDO
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Oxygenase, 1H-3-hydroxy-4-oxoquinoline 2,4-di
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-
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QDO
Quinoline-3,4-diol 2,4-dioxygenase
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-
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quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)
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additional information
1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
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-
-
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QDO
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-
-
-
additional information
the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold
additional information
the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold
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additional information
the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold
additional information
the dioxygenase belongs to the alpha/beta-hydrolase fold superfamily. Members of this family typically catalyze hydrolytic processes rather than oxygenation reactions, but the enzyme's crystal structure shows a typical alpha/beta fold
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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reduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate.
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CAS REGISTRY NUMBER
COMMENTARY
144941-44-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
?
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
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
?
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
-
-
?
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
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at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
-
-
?
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
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at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
-
-
?
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
-
-
?
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
-
-
?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
-
-
?
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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-
?
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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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
?
-
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
?
-
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
?
-
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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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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
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no spectral evidence for the presence of a chromophoric cofactor
-
additional information
-
no spectral evidence for the presence of a chromophoric cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Nickel
additional information
additional information
-
addition of metal ions in the absence and in the presence of the reductant ascorbate does not increase activity
additional information
-
addition of metal ions in the absence and in the presence of the reductant ascorbate does not increase activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
1H-3-Hydroxy-4-oxoquinaldine
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
0.0032
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 6.5, 5°C
0.0048
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 10.5, 5°C
0.0209
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 6.5, 5°C
0.0233
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
0.0272
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication
0.0301
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 10.5, 5°C
0.0589
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 6.5, 5°C
0.059
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.0868
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 10.5, 5°C
0.1595
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
0.162
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication
0.0104
1H-3-Hydroxy-4-oxoquinoline
wild-type QDO, pH not specified in the publication, temperature not specified in the publication
0.1809
1H-3-Hydroxy-4-oxoquinoline
QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0006
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 6.5, 5°C
0.0034
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.027
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
0.097
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 10.5, 5°C
0.19
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 6.5, 5°C
1.05
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication
3
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
16.3
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 6.5, 5°C
20.5
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 10.5, 5°C
29.5
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 10.5, 5°C
38.4
1H-3-Hydroxy-4-oxoquinaldine
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
46.4
1H-3-Hydroxy-4-oxoquinaldine
HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication
2.55
1H-3-Hydroxy-4-oxoquinoline
QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication
20.6
1H-3-Hydroxy-4-oxoquinoline
wild-type QDO, pH not specified in the publication, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 6.5, 5°C
1.12
1H-3-Hydroxy-4-oxoquinaldine
mutant H251A, pH 10.5, 5°C
9
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 6.5, 5°C
681
1H-3-Hydroxy-4-oxoquinaldine
mutant D126A, pH 10.5, 5°C
5100
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 6.5, 5°C
6100
1H-3-Hydroxy-4-oxoquinaldine
wild-type, pH 10.5, 5°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
-
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
-
physiological function
-
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8XWM4_RALSO
Ralstonia solanacearum (strain GMI1000)
398
2
45997
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
the enzyme shows an alpha/beta forld, residues Ser101/His251/Asp126 in HOD located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily
additional information
-
the enzyme shows an alpha/beta forld, residues Ser101/His251/Asp126 in HOD located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily
additional information
-
the enzyme shows an alpha/beta forld, residues Ser101/His251/Asp126 in HOD located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily
-
additional information
the enzyme shows an alpha/beta forld, residues Ser95/His244/Asp120 in QDO located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily
additional information
-
the enzyme shows an alpha/beta forld, residues Ser95/His244/Asp120 in QDO located at the interface between the core domain and the cap domain, correspond to the nucleophile/histidine/acidic residue triad required for activity by members of the alpha/beta-hydrolase fold superfamily
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HOD mutant C69S/H251A in complex with its natural 1-H-3-hydroxy-4-oxoquinaldine substrate, its N-acetylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.1 A resolution
mutations H251A and D126A have a minor effect on substrate positioning. Both His-251 and Asp-126 are essential for the proton transfer driving force of the initial reaction
random-acceleration molecular dynamics study. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis
crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6122. Selenomethionine-containing native QDO is prepared and crystallized under identical conditions
-
QDO in complex with its natural 1-H-3-hydroxy-4-oxoquinoline substrate, its N-formylanthranilate reaction product, and chloride as dioxygen mimic, X-ray diffraction structure determination and analysis at 2.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D126A
H102L
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H251A
H38A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
S101A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
D126A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H102L
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H251A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H38A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
S101A
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
D120A
D126A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
D126A
mutation in the active site His-251/Asp-126 dyad, 9fold decrease in kcat/Km
H251A
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H251A
mutation in the active site His-251/Asp-126 dyad, 5500fold decrease in kcat/Km
D120A
site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
D120A
-
site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
both N-terminally His6-tagged and native QDO were overexpressed in Escherichia coli
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bauer, I.; Max, N.; Fetzner, S.; Lingens, F.
2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
Eur. J. Biochem.
240
576-583
1996
Arthrobacter sp., Pseudomonas putida, Pseudomonas putida 33/1, Arthrobacter sp. Ru61a
brenda
Bauer, I.; de Beyer, A.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarboxylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline
FEMS Microbiol. Lett.
117
299-304
1994
Pseudomonas putida
-
brenda
Block, D.W.; Lingens, F.
Microbial metabolism of quinoline and related compounds. XIV. Purification and properties of 1H-3-hydroxy-4-oxoquinoline oxygenase, a new extradiol cleavage enzyme from Pseudomonas putida strain 33/1
Biol. Chem. Hoppe-Seyler
373
343-349
1992
Pseudomonas putida
brenda
Qi, R.; Fetzner, S.; Oakley, A.J.
Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family
Acta Crystallogr. Sect. F
63
378-381
2007
Pseudomonas putida, Pseudomonas putida 33/1
brenda
Steiner, R.A.; Janssen, H.J.; Roversi, P.; Oakley, A.J.; Fetzner, S.
Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
Proc. Natl. Acad. Sci. USA
107
657-662
2010
Paenarthrobacter nitroguajacolicus (O31266), Paenarthrobacter nitroguajacolicus, Pseudomonas putida (O33472), Pseudomonas putida 33/1 (O33472), Pseudomonas putida 33/1, Paenarthrobacter nitroguajacolicus R61a (O31266)