Information on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
1.13.11.47
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxy-4-oxoquinoline 2,4-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1H)-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
-
-
-
-
1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
O33472
-
1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Pseudomonas putida 33/1
O33472
-
-
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 2,4-dioxygenase
-
-
1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
Pseudomonas putida 33/1
-
-
-
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
-
-
formerly
-
EC 1.13.99.5
-
-
formerly
-
HOD
Arthrobacter nitroguajacolicus R61a
A4V8M9
-
-
Oxygenase, 1H-3-hydroxy-4-oxoquinoline 2,4-di
-
-
-
-
QDO
-
-
-
-
QDO
O33472
-
QDO
Pseudomonas putida 33/1
-, O33472
-
-
Quinoline-3,4-diol 2,4-dioxygenase
-
-
-
-
quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)
-
-
-
-
MeQDO
-
-
-
-
additional information
A4V8M9
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
Arthrobacter nitroguajacolicus R61a
A4V8M9
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
O33472
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
Pseudomonas putida 33/1
O33472
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
-
CAS REGISTRY NUMBER
COMMENTARY
144941-44-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Arthrobacter nitroguajacolicus R61a
-
A4V8M9
UniProt
Manually annotated by BRENDA team
strain R61a
-
-
Manually annotated by BRENDA team
Arthrobacter sp. Ru61a
strain R61a
-
-
Manually annotated by BRENDA team
Pseudomonas putida 33/1
-
UniProt
Manually annotated by BRENDA team
Pseudomonas putida 33/1
strain 33/1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
A4V8M9
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
O33472
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
Arthrobacter nitroguajacolicus R61a, Pseudomonas putida 33/1
-
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
show the reaction diagram
Arthrobacter sp., Arthrobacter sp. Ru61a
-
-
-
-
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
show the reaction diagram
A4V8M9
-, 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
show the reaction diagram
Arthrobacter nitroguajacolicus R61a
A4V8M9
-, 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
show the reaction diagram
-
-
-
-
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
show the reaction diagram
-
-
-
-
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
show the reaction diagram
-
-
-
-
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
show the reaction diagram
-
at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
-
-
-
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
show the reaction diagram
Pseudomonas putida 33/1
-
-
-
-
1H-3-Hydroxy-4-oxoquinoline + O2
N-Formylanthranilate + CO
show the reaction diagram
Arthrobacter sp. Ru61a
-
at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine
-
-
-
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
show the reaction diagram
O33472
-, 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
show the reaction diagram
Pseudomonas putida 33/1
O33472
-, 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
-
-
?
additional information
?
-
A4V8M9
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
-
-
-
additional information
?
-
Pseudomonas putida, Pseudomonas putida 33/1
O33472
N-heteroaromatic substrate binding and kinetics
-
-
-
additional information
?
-
Arthrobacter nitroguajacolicus R61a
A4V8M9
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
show the reaction diagram
Arthrobacter nitroguajacolicus, Arthrobacter nitroguajacolicus R61a
A4V8M9
-
-
-
?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 33/1
O33472
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no spectral evidence for the presence of a chromophoric cofactor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Nickel
-
contains 0.02 mol of Ni per mol of enzyme
Nickel
-
contains 0.038 mol of Ni per mol of enzyme
Zinc
-
contains 0.045 mol of zinc per mol of enzyme
copper
-
contains 0.048 mol of Cu per mol of enzyme
additional information
-
addition of metal ions in the absence and in the presence of the reductant ascorbate does not increase activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0027
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
0.0233
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
0.0272
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication
0.03
-
1H-3-Hydroxy-4-oxoquinaldine
-
-
0.059
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.1595
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
0.162
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication
0.0104
-
1H-3-Hydroxy-4-oxoquinoline
O33472
wild-type QDO, pH not specified in the publication, temperature not specified in the publication
0.024
-
1H-3-Hydroxy-4-oxoquinoline
-
-
0.1809
-
1H-3-Hydroxy-4-oxoquinoline
O33472
QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0034
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.027
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
1.05
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication
3
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
38.4
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
46.4
-
1H-3-Hydroxy-4-oxoquinaldine
A4V8M9
HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication
2.55
-
1H-3-Hydroxy-4-oxoquinoline
O33472
QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication
20.6
-
1H-3-Hydroxy-4-oxoquinoline
O33472
wild-type QDO, pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Arthrobacter sp. Ru61a
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26000
-
-
gel filtration
30000
-
-
gel filtration
32000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
Arthrobacter sp. Ru61a
-
1 * 32000, SDS-PAGE
-
monomer
Pseudomonas putida 33/1
-
1 * 30000, SDS-PAGE
-
additional information
A4V8M9
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
O33472
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
Arthrobacter nitroguajacolicus R61a
-
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
Pseudomonas putida 33/1
-
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
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
A4V8M9
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
O33472
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
labile above
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for 3 days
-
4C, 15% loss of activity after 2 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
both N-terminally His6-tagged and native QDO were overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C69S/H251A
A4V8M9
inactive mutant
D126A
A4V8M9
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H102L
A4V8M9
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H251A
A4V8M9
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H38A
A4V8M9
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
S101A
A4V8M9
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
D126A
Arthrobacter nitroguajacolicus R61a
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H102L
Arthrobacter nitroguajacolicus R61a
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H251A
Arthrobacter nitroguajacolicus R61a
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
H38A
Arthrobacter nitroguajacolicus R61a
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
S101A
Arthrobacter nitroguajacolicus R61a
-
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-
D120A
O33472
site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
D120A
Pseudomonas putida 33/1
-
site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
-