Information on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.48
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RECOMMENDED NAME
GeneOntology No.
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxy-2-methyl-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 Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
160995-63-1
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
?
show the reaction diagram
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
show the reaction diagram
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
show the reaction diagram
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
show the reaction diagram
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
show the reaction diagram
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + CO
show the reaction diagram
additional information
?
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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
1H-3-hydroxy-4-oxoquinaldine + O2
?
show the reaction diagram
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no cofactors
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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1 mM, weak inhibition
Co2+
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1 mM, weak inhibition
Cu2+
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1 mM, strong inhibition
Fe2+
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1 mM, strong inhibition
guanidine hydrochloride
almost linear decrease of activity up to 1 M where activity vanishes, three-state unfolding of mutant enzyme; causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview
Mg2+
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1 mM, weak inhibition
Mn2+
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1 mM, weak inhibition
Ni2+
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1 mM, strong inhibition
Urea
causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview; nonlinear decrease of activity, activity lost at about 5 M, three-state unfolding of mutant enzyme
Zn2+
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1 mM, strong inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0092 - 0.1907
1H-3-Hydroxy-4-oxoquinaldine
0.0017
3-hydroxy-2-methyl-1H-quinolin-4-one
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30C, pH 8.0
0.325 - 1.646
O2
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 28.2
1H-3-Hydroxy-4-oxoquinaldine
35 - 145
3-hydroxy-2-methyl-1H-quinolin-4-one
0.037 - 113.7
O2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
sodium phosphate buffer, 30C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 9.1
pH profile, C59S Hod, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Arthrobacter nitroguajacolicus
Arthrobacter nitroguajacolicus
Arthrobacter nitroguajacolicus
Arthrobacter nitroguajacolicus
Arthrobacter nitroguajacolicus
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-terminally His6-tagged HOD is crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure is solved by the single anomalous dispersion technique using data collected to 3.5 A resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P43212, with unit-cell parameters a = b = 153.788, c = 120.872 A; purified recombinant wild-type and mutants C69S and C69S/H251A N-terminally His6-tagged HOD, hanging drop vapour diffusion method, 50 mg/ml protein in 20 mM Tris-HCl pH 7.5, 100 mM NaCl, 2 mM EDTA, 1 mM DTT, is mixed with 1.65 M sodium/potassium tartrate, 0.1 M HEPES, pH 7.0, and 30 mM CuCl2, method optimization, X-ray diffraction structure determination and analysis at 3.5 A resolution, single anomalous dispersion technique
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 11
incubation for 5 min at pH between 5.5 and 11.0 does not result in significant loss of activity
673207
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
enzyme in native reduced state (40 mM dithiothreitol) of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 40C
10 - 50
native oxidized state of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 50C
additional information
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recombinant His6HodC exhibits three-state unfolding with an intermediate state I that exhibits at the transition temperature a volume larger than that of the native or denatured state. The intermediate state I is also associated with the highest isothermal expansion coefficient, alphaP, of the three states and exhibits a significantly lower percentage of R-helical structure than the native state. The stability difference between the native and intermediate state is rather small which makes I a potential candidate for reactions with various ligands, particularly those having a preference for the apparently preserved beta-type motifs
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
recombinant wild-type and mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; sequence comparisons, overexpression of mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
expression in Escherichia coli
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expression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
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overexpression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C69S/H251A
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site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
E224A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
F219Y
does not affect the kinetic parameters of the enzyme
F219Y/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
H102Q
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
H102Q/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
S101A
about 21fold increase in the Km for the organic substrate
S101A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
S220N
does not drastically influence the kinetic parameters of the enzyme for the organic substrate, but it causes a 3.5fold decrease in Km for O2 and a 6.2fold decrease in kcat for O2
S220N/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196A/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196K/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
Y196R/C69S
site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme
E224A
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decreased Km for O2
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H102Q
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Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
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S101A
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about 21fold increase in the Km for the organic substrate
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C69S
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site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
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C69S/H251A
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site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
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C69S/H251A
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site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
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E224A
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decreased Km for O2
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H102Q
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Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
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S101A
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about 21fold increase in the Km for the organic substrate
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