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
LITERATURE
3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
(1H)-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
-
-
-
-
MeQDO
-
-
-
-
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)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
144941-44-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrobacter nitroguajacolicus R61a
-
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
COMMENTARY
LITERATURE
physiological function
O33472
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
O31266
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
physiological function
Pseudomonas putida 33/1, Arthrobacter nitroguajacolicus R61a
-
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
O31266
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
O31266
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
?
-
O31266
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
O31266
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
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
O31266
-
-
-
?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
show the reaction diagram
Pseudomonas putida, Pseudomonas putida 33/1
O33472
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no spectral evidence for the presence of a chromophoric cofactor
-
METALS and IONS
ORGANISM
UNIPROT
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
2,2'-dipyridyl
-
-
ascorbate
-
-
Ca2+
-
weak
Co2+
-
weak
Cu2+
-
strong
ethylxanthate
-
-
Fe2+
-
strong
iodoacetamide
-
-
iodoacetate
-
-
Mg2+
-
weak
Mn2+
-
weak
Ni2+
-
strong
p-hydroxymercuribenzoate
-
-
Sodium azide
-
-
Sodium dithionite
-
-
Zn2+
-
strong
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
1H-3-Hydroxy-4-oxoquinaldine
O31266
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
0.0233
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
0.0272
1H-3-Hydroxy-4-oxoquinaldine
O31266
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
O31266
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.1595
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
0.162
1H-3-Hydroxy-4-oxoquinaldine
O31266
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0034
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication
0.027
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication
1.05
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication
3
1H-3-Hydroxy-4-oxoquinaldine
O31266
HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication
38.4
1H-3-Hydroxy-4-oxoquinaldine
O31266
wild-type HOD, pH not specified in the publication, temperature not specified in the publication
46.4
1H-3-Hydroxy-4-oxoquinaldine
O31266
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Arthrobacter sp. Ru61a
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
-
gel filtration
207897
30000
-
gel filtration
207895
32000
-
gel filtration
207895
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
monomer
Pseudomonas putida 33/1
-
1 * 30000, SDS-PAGE
-
monomer
Arthrobacter sp. Ru61a
-
1 * 32000, SDS-PAGE
-
additional information
O31266
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
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
-
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
-
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
O31266
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
labile above
207895
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 3 days
-
4C, 15% loss of activity after 2 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both N-terminally His6-tagged and native QDO were overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C69S/H251A
O31266
inactive mutant
D126A
O31266
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H102L
O31266
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H251A
O31266
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
H38A
O31266
site-directed mutagenesis, the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
S101A
O31266
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
-