Information on EC 1.14.13.61 - 2-hydroxyquinoline 8-monooxygenase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
1.14.13.61
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxyquinoline 8-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
quinolin-2-ol + NADH + H+ + O2 = quinolin-2,8-diol + NAD+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
quinolin-2(1H)-one,NADH:oxygen oxidoreductase (8-oxygenating)
Requires iron. Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer.
CAS REGISTRY NUMBER
COMMENTARY hide
166799-89-9
-
191941-72-7
GenBank Y12655-derived protein GI 2072732, 2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoR subunit)
191941-74-9
GenBank Y12655-derived protein GI, 2-oxo-1,2-dihydroquinoline 8-monooxygenase (Pseudomonas putida strain 86 gene oxoO subunit)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Oxo-1,2-dihydroquinoline + NADH + O2
8-Hydroxy-2-oxo-1,2-dihydroquinoline + NAD+ + H2O
show the reaction diagram
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
show the reaction diagram
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-Oxo-1,2-dihydroquinoline + NADH + O2
?
show the reaction diagram
quinolin-2-ol + NADH + O2
quinolin-2,8-diol + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
the reductase component contains 1 FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
4,5-dihydroxy-1,3-benzene disulfonic acid
-
-
iodoacetate
-
-
p-hydroxymercuribenzoate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Polyethylene glycol
-
enhances activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.97
-
oxygenase component
32.5
-
reductase component
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
-
reductase component, gel filtration
51200
-
x * 51200, calculation from nucleotide sequence, oxygenase component + x * 37000, calculation from nucleotide sequence, reductase component
55000
-
the reductase component is a monomer, 1 * 37000, SDS-PAGE. The oxygenase component is a hexamer, 6 * 55000, SDS-PAGE
330000
-
oxygenase component, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme, hanging drop vapour diffusion method, 50 mg/ml protein in 10 mM Tris-HCl, pH 8.0, is mixed with reservoir solution, containing 3335% PEG 400, 200 mM ammonium tartrate, pH 6.5, in a 3:2 ratio with a resulting pH of 7.0, at aerobic conditions, 3 days at 17C, under anaerobic conditions a reservoir solution containing 2930% PEG 400, 200 mM ammonium tartrate, 5 mM Na-dithionite, pH 6.5, is mixed with protein reduced by 5 mM Na-dithionite in a ratio of 2:2 at 15C, X-ray diffraction structure determination and analysis at 2.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ion exchange and hydrophobic interaction chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE