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Information on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase and Organism(s) Pseudomonas putida and UniProt Accession O33472
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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
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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
The taxonomic range for the selected organisms is: Pseudomonas putida
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1H)-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
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1H-3-Hydroxy-4-oxo-quinoline oxygenase
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1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
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1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
1H-3-Hydroxy-4-oxoquinoline oxygenase
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3,4-dihydroxyquinoline 2,4-dioxygenase
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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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MeQDO
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Oxygenase, 1H-3-hydroxy-4-oxoquinoline 2,4-di
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QDO
Quinoline-3,4-diol 2,4-dioxygenase
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quinoline-3,4-diol 2,4-dioxygenase (carbon monoxide-forming)
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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
1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase
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QDO
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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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.
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
additional information
?
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N-heteroaromatic substrate binding and kinetics
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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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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-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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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addition of metal ions in the absence and in the presence of the reductant ascorbate does not increase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the cofactor-independent dioxygenase is involved in the breakdown of N-heteroaromatic compounds
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). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D120A
site-directed mutagenesism the mutant shows altered kinetics and reduced catalytic efficiency compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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., Arthrobacter sp. Ru61a, Pseudomonas putida, Pseudomonas putida 33/1
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
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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
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
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, Paenarthrobacter nitroguajacolicus R61a (O31266), Pseudomonas putida (O33472), Pseudomonas putida 33/1 (O33472), Pseudomonas putida 33/1
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