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Literature summary for 1.13.11.48 extracted from

  • Frerichs-Deeken, U.; Fetzner, S.
    Dioxygenases without requirement for cofactors: Identification of amino acid residues involved in substrate binding and catalysis, and testing for rate-limiting steps in the reaction of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (2005), Curr. Microbiol., 51, 344-352.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Paenarthrobacter nitroguajacolicus
sequence comparisons, overexpression of mutant N-terminally His6-tagged HODs in Escherichia coli strain M15 Paenarthrobacter nitroguajacolicus

Protein Variants

Protein Variants Comment Organism
C69S stable in its monomeric form Paenarthrobacter nitroguajacolicus
C69S site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD Paenarthrobacter nitroguajacolicus
E224A decreased Km for O2 Paenarthrobacter nitroguajacolicus
E224A/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
F219Y does not affect the kinetic parameters of the enzyme Paenarthrobacter nitroguajacolicus
F219Y/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
H102Q Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold Paenarthrobacter nitroguajacolicus
H102Q/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
S101A about 21fold increase in the Km for the organic substrate Paenarthrobacter nitroguajacolicus
S101A/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
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 Paenarthrobacter nitroguajacolicus
S220N/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
Y196A increased Km value Paenarthrobacter nitroguajacolicus
Y196A/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
Y196K increased Km value Paenarthrobacter nitroguajacolicus
Y196K/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus
Y196R increased Km value Paenarthrobacter nitroguajacolicus
Y196R/C69S site-directed mutagenesis, mutant apparent kinetic parameters compared to the wild-type enzyme Paenarthrobacter nitroguajacolicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pH/pD dependence of apparent kcatO2/KmO2 of Hod C69S, overview Paenarthrobacter nitroguajacolicus
0.0092
-
1H-3-Hydroxy-4-oxoquinaldine wild type enzyme, at 30°C Paenarthrobacter nitroguajacolicus
0.0092
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant C69S Paenarthrobacter nitroguajacolicus
0.0095
-
1H-3-Hydroxy-4-oxoquinaldine mutant F219Y, at 30°C Paenarthrobacter nitroguajacolicus
0.0095
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant F219Y/C69S Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine mutant E224A, at 30°C Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine mutant S220N, at 30°C Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant E224A/C69S Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant S220N/C69S Paenarthrobacter nitroguajacolicus
0.0257
-
1H-3-Hydroxy-4-oxoquinaldine mutant H102Q, at 30°C Paenarthrobacter nitroguajacolicus
0.0257
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant H102Q/C69S Paenarthrobacter nitroguajacolicus
0.0399
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196K, at 30°C Paenarthrobacter nitroguajacolicus
0.0399
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196K/C69S Paenarthrobacter nitroguajacolicus
0.0836
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196R, at 30°C Paenarthrobacter nitroguajacolicus
0.0836
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196R/C69S Paenarthrobacter nitroguajacolicus
0.0995
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196A, at 30°C Paenarthrobacter nitroguajacolicus
0.0995
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196A/C69S Paenarthrobacter nitroguajacolicus
0.1907
-
1H-3-Hydroxy-4-oxoquinaldine mutant S101A, at 30°C Paenarthrobacter nitroguajacolicus
0.1907
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant S101A/C69S Paenarthrobacter nitroguajacolicus
0.325
-
O2 mutant H102Q, at 30°C Paenarthrobacter nitroguajacolicus
0.325
-
O2 pH 8.0, 30°C, recombinant mutant H102Q/C69S Paenarthrobacter nitroguajacolicus
0.357
-
O2 mutant S220N, at 30°C Paenarthrobacter nitroguajacolicus
0.357
-
O2 pH 8.0, 30°C, recombinant mutant S220N/C69S Paenarthrobacter nitroguajacolicus
0.711
-
O2 mutant E224A, at 30°C Paenarthrobacter nitroguajacolicus
0.711
-
O2 pH 8.0, 30°C, recombinant mutant E224A/C69S Paenarthrobacter nitroguajacolicus
1.233
-
O2 wild type enzyme, at 30°C Paenarthrobacter nitroguajacolicus
1.233
-
O2 pH 8.0, 30°C, recombinant mutant C69S Paenarthrobacter nitroguajacolicus
1.27
-
O2 mutant F219Y, at 30°C Paenarthrobacter nitroguajacolicus
1.27
-
O2 pH 8.0, 30°C, recombinant mutant F219Y/C69S Paenarthrobacter nitroguajacolicus
1.37
-
O2 mutant Y196R, at 30°C Paenarthrobacter nitroguajacolicus
1.37
-
O2 pH 8.0, 30°C, recombinant mutant Y196R/C69S Paenarthrobacter nitroguajacolicus
1.382
-
O2 mutant S101A, at 30°C Paenarthrobacter nitroguajacolicus
1.382
-
O2 pH 8.0, 30°C, recombinant mutant S101A/C69S Paenarthrobacter nitroguajacolicus
1.6
-
O2 mutant Y196K, at 30°C Paenarthrobacter nitroguajacolicus
1.6
-
O2 pH 8.0, 30°C, recombinant mutant Y196K/C69S Paenarthrobacter nitroguajacolicus
1.646
-
O2 mutant Y196A, at 30°C Paenarthrobacter nitroguajacolicus
1.646
-
O2 pH 8.0, 30°C, recombinant mutant Y196A/C69S Paenarthrobacter nitroguajacolicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus
-
N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus Rü61a
-
N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus R-61a
-
N-Acetylanthranilate + CO
-
?

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nitroguajacolicus Q7WSQ7
-
-
Paenarthrobacter nitroguajacolicus Q7WSQ7 formerly Arthrobacter ilicis R-61a
-
Paenarthrobacter nitroguajacolicus R-61a Q7WSQ7 formerly Arthrobacter ilicis R-61a
-
Paenarthrobacter nitroguajacolicus Rü61a Q7WSQ7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Paenarthrobacter nitroguajacolicus
recombinant mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography Paenarthrobacter nitroguajacolicus

Reaction

Reaction Comment Organism Reaction ID
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 Paenarthrobacter nitroguajacolicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction Paenarthrobacter nitroguajacolicus N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rü61a N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction Paenarthrobacter nitroguajacolicus Rü61a N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus R-61a N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2 Hod has adapted active-site residues of the alpha/beta hydrolase fold for the dioxygenolytic reaction Paenarthrobacter nitroguajacolicus R-61a N-Acetylanthranilate + CO
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus N-acetylanthranilic acid + CO
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rü61a N-acetylanthranilic acid + CO
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus R-61a N-acetylanthranilic acid + CO
-
?
additional information 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 Paenarthrobacter nitroguajacolicus ?
-
?
additional information 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 Paenarthrobacter nitroguajacolicus Rü61a ?
-
?
additional information 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 Paenarthrobacter nitroguajacolicus R-61a ?
-
?

Synonyms

Synonyms Comment Organism
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
Paenarthrobacter nitroguajacolicus
HOD
-
Paenarthrobacter nitroguajacolicus
HodC
-
Paenarthrobacter nitroguajacolicus
More HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes Paenarthrobacter nitroguajacolicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Paenarthrobacter nitroguajacolicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.037 0.23 O2 mutant E224A, at 30°C Paenarthrobacter nitroguajacolicus
0.7
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196K, at 30°C Paenarthrobacter nitroguajacolicus
0.7
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196K/C69S Paenarthrobacter nitroguajacolicus
1
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196R, at 30°C Paenarthrobacter nitroguajacolicus
1
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196R/C69S Paenarthrobacter nitroguajacolicus
1.3
-
1H-3-Hydroxy-4-oxoquinaldine mutant Y196A, at 30°C Paenarthrobacter nitroguajacolicus
1.3
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant Y196A/C69S Paenarthrobacter nitroguajacolicus
2.3
-
1H-3-Hydroxy-4-oxoquinaldine mutant S101A, at 30°C Paenarthrobacter nitroguajacolicus
2.3
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant S101A/C69S Paenarthrobacter nitroguajacolicus
3.4
-
O2 mutant Y196K, at 30°C Paenarthrobacter nitroguajacolicus
3.4
-
O2 mutant Y196R, at 30°C Paenarthrobacter nitroguajacolicus
3.4
-
O2 pH 8.0, 30°C, recombinant mutant Y196K/C69S Paenarthrobacter nitroguajacolicus
3.4
-
O2 pH 8.0, 30°C, recombinant mutant Y196R/C69S Paenarthrobacter nitroguajacolicus
6.4
-
O2 mutant Y196A, at 30°C Paenarthrobacter nitroguajacolicus
6.4
-
O2 pH 8.0, 30°C, recombinant mutant Y196A/C69S Paenarthrobacter nitroguajacolicus
10
-
1H-3-Hydroxy-4-oxoquinaldine mutant H102Q, at 30°C Paenarthrobacter nitroguajacolicus
10
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant H102Q/C69S Paenarthrobacter nitroguajacolicus
12.2
-
1H-3-Hydroxy-4-oxoquinaldine mutant S220N, at 30°C Paenarthrobacter nitroguajacolicus
12.2
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant S220N/C69S Paenarthrobacter nitroguajacolicus
14.8
-
O2 mutant H102Q, at 30°C Paenarthrobacter nitroguajacolicus
14.8
-
O2 pH 8.0, 30°C, recombinant mutant H102Q/C69S Paenarthrobacter nitroguajacolicus
18.3
-
O2 mutant S220N, at 30°C Paenarthrobacter nitroguajacolicus
18.3
-
O2 pH 8.0, 30°C, recombinant mutant S220N/C69S Paenarthrobacter nitroguajacolicus
21
-
O2 mutant F219Y, at 30°C Paenarthrobacter nitroguajacolicus
22.8
-
1H-3-Hydroxy-4-oxoquinaldine mutant F219Y, at 30°C Paenarthrobacter nitroguajacolicus
22.8
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant F219Y/C69S Paenarthrobacter nitroguajacolicus
22.9
-
1H-3-Hydroxy-4-oxoquinaldine wild type enzyme, at 30°C Paenarthrobacter nitroguajacolicus
22.9
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant C69S Paenarthrobacter nitroguajacolicus
28.2
-
1H-3-Hydroxy-4-oxoquinaldine mutant E224A, at 30°C Paenarthrobacter nitroguajacolicus
28.2
-
1H-3-Hydroxy-4-oxoquinaldine pH 8.0, 30°C, recombinant mutant E224A/C69S Paenarthrobacter nitroguajacolicus
38.8
-
O2 mutant S101A, at 30°C Paenarthrobacter nitroguajacolicus
38.8
-
O2 pH 8.0, 30°C, recombinant mutant S101A/C69S Paenarthrobacter nitroguajacolicus
42
-
O2 wild type enzyme, at 30°C Paenarthrobacter nitroguajacolicus
79.1
-
O2 mutant E224A, at 30°C Paenarthrobacter nitroguajacolicus
79.1
-
O2 pH 8.0, 30°C, recombinant mutant E224A/C69S Paenarthrobacter nitroguajacolicus
110.9
-
O2 mutant F219Y, at 30°C Paenarthrobacter nitroguajacolicus
110.9
-
O2 pH 8.0, 30°C, recombinant mutant F219Y/C69S Paenarthrobacter nitroguajacolicus
113.7
-
O2 wild type enzyme, at 30°C Paenarthrobacter nitroguajacolicus
113.7
-
O2 pH 8.0, 30°C, recombinant mutant C69S Paenarthrobacter nitroguajacolicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Paenarthrobacter nitroguajacolicus

pH Range

pH Minimum pH Maximum Comment Organism
5.1 9.1 pH profile, C59S Hod, overview Paenarthrobacter nitroguajacolicus
5.5 11
-
Paenarthrobacter nitroguajacolicus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 11 incubation for 5 min at pH between 5.5 and 11.0 does not result in significant loss of activity Paenarthrobacter nitroguajacolicus