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Information on EC 1.13.11.47 - 3-hydroxy-4-oxoquinoline 2,4-dioxygenase and Organism(s) Paenarthrobacter nitroguajacolicus and UniProt Accession O31266

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IUBMB 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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This record set is specific for:
Paenarthrobacter nitroguajacolicus
UNIPROT: O31266
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The taxonomic range for the selected organisms is: Paenarthrobacter nitroguajacolicus
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
144941-44-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0027 - 0.162
1H-3-Hydroxy-4-oxoquinaldine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006 - 46.4
1H-3-Hydroxy-4-oxoquinaldine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 6100
1H-3-Hydroxy-4-oxoquinaldine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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?
HOD_PAENT
276
0
31858
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C69S/H251A
inactive mutant
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Pietra, F.
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations
Chem. Biodivers.
11
861-871
2014
Paenarthrobacter nitroguajacolicus (O31266)
Manually annotated by BRENDA team
Hernandez-Ortega, A.; Quesne, M.G.; Bui, S.; Heuts, D.P.; Steiner, R.A.; Heyes, D.J.; de Visser, S.P.; Scrutton, N.S.
Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase effect of the basicity of an active site His residue
J. Biol. Chem.
289
8620-8632
2014
Paenarthrobacter nitroguajacolicus (O31266)
Manually annotated by BRENDA team