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show all sequences of 1.13.11.48

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

Frerichs-Deeken, U.; Fetzner, S.; Curr. Microbiol. 51, 344-352 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; sequence comparisons, overexpression of mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
Paenarthrobacter nitroguajacolicus
Engineering
Amino acid exchange
Commentary
Organism
C69S
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD; stable in its monomeric form
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
Commentary
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
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
0.0095
-
1H-3-Hydroxy-4-oxoquinaldine
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C; mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
0.0257
-
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
0.0399
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196K, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
0.0836
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
0.0995
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
0.1907
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
0.325
-
O2
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
0.357
-
O2
mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
0.711
-
O2
mutant E224A, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
1.233
-
O2
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
1.27
-
O2
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
1.37
-
O2
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
1.382
-
O2
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
1.6
-
O2
mutant Y196K, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
1.646
-
O2
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Paenarthrobacter nitroguajacolicus
Q7WSQ7
; strain R-61a, formerly Arthrobacter ilicis R-61a
-
Paenarthrobacter nitroguajacolicus R-61a
Q7WSQ7
strain R-61a, formerly Arthrobacter ilicis R-61a
-
Paenarthrobacter nitroguajacolicus Rü61a
Q7WSQ7
-
-
Purification (Commentary)
Commentary
Organism
; recombinant mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
Paenarthrobacter nitroguajacolicus
Reaction
Reaction
Commentary
Organism
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus Rü61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus R-61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
Paenarthrobacter nitroguajacolicus
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
Paenarthrobacter nitroguajacolicus Rü61a
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
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
673207
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
673207
Paenarthrobacter nitroguajacolicus R-61a
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Paenarthrobacter nitroguajacolicus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
1
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
1.3
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
2.3
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
3.4
-
O2
mutant Y196K, at 30°C; mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
6.4
-
O2
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
10
-
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
12.2
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
14.8
-
O2
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
18.3
-
O2
mutant S220N, at 30°C; 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; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
22.9
-
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
28.2
-
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
38.8
-
O2
mutant S101A, at 30°C; 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; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
110.9
-
O2
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
113.7
-
O2
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Paenarthrobacter nitroguajacolicus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.1
9.1
pH profile, C59S Hod, overview
Paenarthrobacter nitroguajacolicus
5.5
11
-
Paenarthrobacter nitroguajacolicus
pH Stability
pH Stability
pH Stability Maximum
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; sequence comparisons, overexpression of mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
Paenarthrobacter nitroguajacolicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C69S
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD; stable in its monomeric form
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
0.0095
-
1H-3-Hydroxy-4-oxoquinaldine
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
0.0154
-
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C; mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
0.0257
-
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
0.0399
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196K, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
0.0836
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
0.0995
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
0.1907
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
0.325
-
O2
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
0.357
-
O2
mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
0.711
-
O2
mutant E224A, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
1.233
-
O2
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
1.27
-
O2
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
1.37
-
O2
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
1.382
-
O2
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
1.6
-
O2
mutant Y196K, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
1.646
-
O2
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
; recombinant mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
Paenarthrobacter nitroguajacolicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus Rü61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
Paenarthrobacter nitroguajacolicus R-61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
Paenarthrobacter nitroguajacolicus
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
Paenarthrobacter nitroguajacolicus Rü61a
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
-
673207
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
673207
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
673207
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
673207
Paenarthrobacter nitroguajacolicus R-61a
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Paenarthrobacter nitroguajacolicus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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; pH 8.0, 30°C, recombinant mutant Y196K/C69S
Paenarthrobacter nitroguajacolicus
1
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
1.3
-
1H-3-Hydroxy-4-oxoquinaldine
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
2.3
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S101A, at 30°C; pH 8.0, 30°C, recombinant mutant S101A/C69S
Paenarthrobacter nitroguajacolicus
3.4
-
O2
mutant Y196K, at 30°C; mutant Y196R, at 30°C; pH 8.0, 30°C, recombinant mutant Y196K/C69S; pH 8.0, 30°C, recombinant mutant Y196R/C69S
Paenarthrobacter nitroguajacolicus
6.4
-
O2
mutant Y196A, at 30°C; pH 8.0, 30°C, recombinant mutant Y196A/C69S
Paenarthrobacter nitroguajacolicus
10
-
1H-3-Hydroxy-4-oxoquinaldine
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
12.2
-
1H-3-Hydroxy-4-oxoquinaldine
mutant S220N, at 30°C; pH 8.0, 30°C, recombinant mutant S220N/C69S
Paenarthrobacter nitroguajacolicus
14.8
-
O2
mutant H102Q, at 30°C; pH 8.0, 30°C, recombinant mutant H102Q/C69S
Paenarthrobacter nitroguajacolicus
18.3
-
O2
mutant S220N, at 30°C; 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; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
22.9
-
1H-3-Hydroxy-4-oxoquinaldine
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
28.2
-
1H-3-Hydroxy-4-oxoquinaldine
mutant E224A, at 30°C; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
38.8
-
O2
mutant S101A, at 30°C; 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; pH 8.0, 30°C, recombinant mutant E224A/C69S
Paenarthrobacter nitroguajacolicus
110.9
-
O2
mutant F219Y, at 30°C; pH 8.0, 30°C, recombinant mutant F219Y/C69S
Paenarthrobacter nitroguajacolicus
113.7
-
O2
pH 8.0, 30°C, recombinant mutant C69S; wild type enzyme, at 30°C
Paenarthrobacter nitroguajacolicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Paenarthrobacter nitroguajacolicus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.1
9.1
pH profile, C59S Hod, overview
Paenarthrobacter nitroguajacolicus
5.5
11
-
Paenarthrobacter nitroguajacolicus
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
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
Other publictions for EC 1.13.11.48
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
696277
Boehm
Thermodynamic analysis of dena ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R-61a, Paenarthrobacter nitroguajacolicus Rü61a
Biochemistry
47
7116-7126
2008
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1
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1
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1
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1
4
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5
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1
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1
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4
1
1
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2
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1
1
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-
684175
Steiner
Crystallization and preliminar ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus Rü61a, Paenarthrobacter nitroguajacolicus Rue61a
Acta Crystallogr. Sect. F
63
382-385
2007
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1
2
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4
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1
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3
1
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714163
Beermann
Stability, unfolding, and stru ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus Rü61a
Biochemistry
46
4241-4249
2007
-
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1
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1
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3
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1
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1
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1
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1
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1
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1
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1
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1
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-
-
-
-
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673207
Frerichs-Deeken
Dioxygenases without requireme ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R-61a, Paenarthrobacter nitroguajacolicus Rü61a
Curr. Microbiol.
51
344-352
2005
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1
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17
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18
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3
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4
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1
1
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12
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1
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20
1
2
1
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1
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17
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18
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3
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1
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12
-
1
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20
1
2
1
-
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-
-
-
-
658042
Frerichs-Deeken
Dioxygenases without requireme ...
Paenarthrobacter ilicis, Paenarthrobacter ilicis Ru61a
Biochemistry
43
14485-14499
2004
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1
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1
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2
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2
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1
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1
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4
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2
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285259
Fischer
Bacterial 2,4-dioxygenases: ne ...
Arthrobacter sp.
J. Bacteriol.
181
5725-5733
1999
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2
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207895
Bauer
2,4-Dioxygenases catalyzing N- ...
Arthrobacter sp., Arthrobacter sp. Ru61a
Eur. J. Biochem.
240
576-583
1996
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8
1
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1
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1
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1
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1
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8
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1
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1
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1
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1
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4
1
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-
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207896
Bauer
-
A novel type of oxygenolytic r ...
Arthrobacter sp., Arthrobacter sp. Ru61a
FEMS Microbiol. Lett.
117
299-304
1994
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