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
strain 86
-
-
Manually annotated by BRENDA team
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 33–35% 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 17°C, under anaerobic conditions a reservoir solution containing 29–30% 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 15°C, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ion exchange and hydrophobic interaction chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE