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Information on EC 1.13.11.48 - 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
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1.13.11.48 3-hydroxy-2-methylquinolin-4-one 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 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.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
1H-3-hydroxy-4-oxoquinaldine oxygenase
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
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HOD
HodC
additional information
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
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1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
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additional information
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HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
additional information
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HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
additional information
HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
additional information
HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
additional information
HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
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additional information
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HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
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additional information
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HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
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additional information
HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
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3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
catalytic mechanism, overview. H251 acts as a general base to abstract a proton from the organic substrate. Residue S101, which corresponds to the nucleophile of the catalytic triad of alpha/beta-hydrolases, presumably participates in binding the heteroaromatic substrate. H102 and residues located in the topological region of the triad's acidic residue appear to influence O2 binding and reactivity. Role of Y196 of Hod as hydrogen-bondforming residue to oxygen atoms or even proton donor to negative charges of catalytic intermediates
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3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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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.
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CAS REGISTRY NUMBER
COMMENTARY
160995-63-1
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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
1H-3-hydroxy-4-oxoquinaldine + O2
?
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
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?
1H-3-hydroxy-4-oxoquinaldine + O2
?
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cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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-
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
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?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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also 1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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also 1H-3-hydroxy-4-oxoquinaldine oxygenase
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ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
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ir
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
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?
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
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?
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + CO
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?
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + CO
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?
additional information
?
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absence of viscosity effects and kinetic solvent isotope effects suggests that turnover of the ternary complex, rather than substrate binding, product release, or proton movements, involves the rate-determining step in the reaction catalyzed by Hod
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?
additional information
?
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absence of viscosity effects and kinetic solvent isotope effects suggests that turnover of the ternary complex, rather than substrate binding, product release, or proton movements, involves the rate-determining step in the reaction catalyzed by Hod
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?
additional information
?
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absence of viscosity effects and kinetic solvent isotope effects suggests that turnover of the ternary complex, rather than substrate binding, product release, or proton movements, involves the rate-determining step in the reaction catalyzed by Hod
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?
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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-oxoquinaldine + O2
?
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
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?
1H-3-hydroxy-4-oxoquinaldine + O2
?
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cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0092
1H-3-Hydroxy-4-oxoquinaldine
wild type enzyme, at 30°C
0.0092
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant C69S
0.0095
1H-3-Hydroxy-4-oxoquinaldine
mutant F219Y, at 30°C
0.0095
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant F219Y/C69S
0.0154
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C
0.0154
1H-3-Hydroxy-4-oxoquinaldine
mutant S220N, at 30°C
0.0154
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant E224A/C69S
0.0154
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant S220N/C69S
0.0257
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C
0.0257
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant H102Q/C69S
0.0399
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196K, at 30°C
0.0399
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196K/C69S
0.0836
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C
0.0836
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196R/C69S
0.0995
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C
0.0995
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196A/C69S
0.1907
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C
0.1907
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant S101A/C69S
0.325
O2
pH 8.0, 30°C, recombinant mutant H102Q/C69S
0.357
O2
pH 8.0, 30°C, recombinant mutant S220N/C69S
0.711
O2
pH 8.0, 30°C, recombinant mutant E224A/C69S
1.27
O2
pH 8.0, 30°C, recombinant mutant F219Y/C69S
1.37
O2
pH 8.0, 30°C, recombinant mutant Y196R/C69S
1.382
O2
pH 8.0, 30°C, recombinant mutant S101A/C69S
1.646
O2
pH 8.0, 30°C, recombinant mutant Y196A/C69S
additional information
additional information
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comparison of thermodynamic parameters for GdnHCl- and urea-induced unfolding of His6HodC69S in 10 mM sodium phosphate and 10 mM sodium borate, pH 7.5, at 25°C, overview
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additional information
additional information
comparison of thermodynamic parameters for GdnHCl- and urea-induced unfolding of His6HodC69S in 10 mM sodium phosphate and 10 mM sodium borate, pH 7.5, at 25°C, overview
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additional information
additional information
pH/pD dependence of apparent kcatO2/KmO2 of Hod C69S, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196K, at 30°C
0.7
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196K/C69S
1
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C
1
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196R/C69S
1.3
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C
1.3
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant Y196A/C69S
2.3
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C
2.3
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant S101A/C69S
10
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C
10
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant H102Q/C69S
12.2
1H-3-Hydroxy-4-oxoquinaldine
mutant S220N, at 30°C
12.2
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant S220N/C69S
22.8
1H-3-Hydroxy-4-oxoquinaldine
mutant F219Y, at 30°C
22.8
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant F219Y/C69S
22.9
1H-3-Hydroxy-4-oxoquinaldine
wild type enzyme, at 30°C
22.9
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant C69S
28.2
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C
28.2
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant E224A/C69S
35
3-hydroxy-2-methyl-1H-quinolin-4-one
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30°C, pH 8.0, at 0.12 mM O2
145
3-hydroxy-2-methyl-1H-quinolin-4-one
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30°C, pH 8.0, at 0.96 mM O2
14.8
O2
pH 8.0, 30°C, recombinant mutant H102Q/C69S
18.3
O2
pH 8.0, 30°C, recombinant mutant S220N/C69S
38.8
O2
pH 8.0, 30°C, recombinant mutant S101A/C69S
79.1
O2
pH 8.0, 30°C, recombinant mutant E224A/C69S
110.9
O2
pH 8.0, 30°C, recombinant mutant F219Y/C69S
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Arthrobacter ilicis R-61a
TrEMBL
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism
additional information
thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism
additional information
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thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism
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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). A0A1C0U9T7_9GAMM
265
0
30494
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33240