Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
1H-3-hydroxy-4-oxoquinaldine oxygenase
3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
-
-
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
-
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
-
-
HOD
-
-
HodC
-
-
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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
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
-
-
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1H-3-hydroxy-4-oxoquinaldine + O2
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + CO
additional information
?
-
1H-3-hydroxy-4-oxoquinaldine + O2
?
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
?
-
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
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
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
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
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
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
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
-
ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
N-acetylanthranilic acid + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
-
-
ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
-
-
ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
also 1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
also 1H-3-hydroxy-4-oxoquinaldine oxygenase
-
ir
1H-3-hydroxy-4-oxoquinoline + O2
N-formylanthranilic acid + CO
-
-
-
ir
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
-
-
-
-
?
3-hydroxy-1H-quinoline-4-one + O2
N-formylanthranilate + CO
-
-
-
-
?
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + CO
-
-
-
-
?
3-hydroxy-2-methyl-1H-quinolin-4-one + O2
N-acetylanthranilate + 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
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1H-3-hydroxy-4-oxoquinaldine + O2
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
1H-3-hydroxy-4-oxoquinaldine + O2
?
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
?
-
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
N-Acetylanthranilate + CO
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0092 - 0.1907
1H-3-Hydroxy-4-oxoquinaldine
0.0017
3-hydroxy-2-methyl-1H-quinolin-4-one
-
30°C, pH 8.0
additional information
additional information
-
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
0.03
1H-3-Hydroxy-4-oxoquinaldine
-
-
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
mutant H102Q, at 30°C
0.325
O2
pH 8.0, 30°C, recombinant mutant H102Q/C69S
0.357
O2
mutant S220N, at 30°C
0.357
O2
pH 8.0, 30°C, recombinant mutant S220N/C69S
0.711
O2
mutant E224A, at 30°C
0.711
O2
pH 8.0, 30°C, recombinant mutant E224A/C69S
0.81
O2
-
30°C, pH 8.0, with 3-hydroxy-2-methyl-1H-quinolin-4-one
1.233
O2
wild type enzyme, at 30°C
1.233
O2
pH 8.0, 30°C, recombinant mutant C69S
1.27
O2
mutant F219Y, at 30°C
1.27
O2
pH 8.0, 30°C, recombinant mutant F219Y/C69S
1.37
O2
mutant Y196R, at 30°C
1.37
O2
pH 8.0, 30°C, recombinant mutant Y196R/C69S
1.382
O2
mutant S101A, at 30°C
1.382
O2
pH 8.0, 30°C, recombinant mutant S101A/C69S
1.6
O2
mutant Y196K, at 30°C
1.6
O2
pH 8.0, 30°C, recombinant mutant Y196K/C69S
1.646
O2
mutant Y196A, at 30°C
1.646
O2
pH 8.0, 30°C, recombinant mutant Y196A/C69S
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
-
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
-
additional information
additional information
pH/pD dependence of apparent kcatO2/KmO2 of Hod C69S, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.7 - 28.2
1H-3-Hydroxy-4-oxoquinaldine
35 - 145
3-hydroxy-2-methyl-1H-quinolin-4-one
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
-
30°C, pH 8.0, at 0.12 mM O2
145
3-hydroxy-2-methyl-1H-quinolin-4-one
-
30°C, pH 8.0, at 0.96 mM O2
0.037 - 0.23
O2
mutant E224A, at 30°C
3.4
O2
mutant Y196K, at 30°C
3.4
O2
mutant Y196R, at 30°C
3.4
O2
pH 8.0, 30°C, recombinant mutant Y196K/C69S
3.4
O2
pH 8.0, 30°C, recombinant mutant Y196R/C69S
6.4
O2
mutant Y196A, at 30°C
6.4
O2
pH 8.0, 30°C, recombinant mutant Y196A/C69S
14.8
O2
mutant H102Q, at 30°C
14.8
O2
pH 8.0, 30°C, recombinant mutant H102Q/C69S
18.3
O2
mutant S220N, at 30°C
18.3
O2
pH 8.0, 30°C, recombinant mutant S220N/C69S
21
O2
mutant F219Y, at 30°C
38.8
O2
mutant S101A, at 30°C
38.8
O2
pH 8.0, 30°C, recombinant mutant S101A/C69S
42
O2
wild type enzyme, at 30°C
79.1
O2
mutant E224A, at 30°C
79.1
O2
pH 8.0, 30°C, recombinant mutant E224A/C69S
110.9
O2
mutant F219Y, at 30°C
110.9
O2
pH 8.0, 30°C, recombinant mutant F219Y/C69S
113.7
O2
wild type enzyme, at 30°C
113.7
O2
pH 8.0, 30°C, recombinant mutant C69S
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
random-acceleration molecular dynamics study on 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in complex with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one, in aqueous solution. Gates for expulsion of O2 from the protein, which can also be taken as gates for O2 uptake, are found throughout almost the whole external surface of the protein, alongside a variety of binding pockets for O2 . The most exploited gates and binding pockets do not correspond to the single gate and binding pocket proposed from the examination of the static model from X-ray diffraction analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
E224A
decreased Km for O2
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
-
decreased Km for O2
-
H102Q
-
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
-
S101A
-
about 21fold increase in the Km for the organic substrate
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
-
C69S/H251A
-
site-directed mutagenesis, the mutant is catalytically inactive owing to the Ala substitution of the essential residue His251
-
E224A
-
decreased Km for O2
-
H102Q
-
Km for the heteroaromatic substrate is increased only 2.8fold, and kcat is reduced 2.3fold
-
S101A
-
about 21fold increase in the Km for the organic substrate
-
H251A
-
2258fold lower specific activity than wild-type
H251A
-
2258fold lower specific activity than wild-type
-
C69S
stable in its monomeric form
C69S
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184
C69S
-
an oxidatively stable mutant variant
C69S
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
C69S
site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
C69S
-
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184
-
C69S
-
stable in its monomeric form
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S
-
site-directed mutagenesis, the mutant has catalytic properties that are identical to those of wild-type HOD
-
C69S
-
an oxidatively stable mutant variant
-
C69S
-
stable in its monomeric form
-
C69S
-
site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bauer, I.; Max, N.; Fetzner, S.; Lingens, F.
2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Rii61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
Eur. J. Biochem.
240
576-583
1996
Arthrobacter sp., Arthrobacter sp. Ru61a
brenda
Bauer, I.; de Beyer, A.; Tshisuaka, B.; Fetzner, S.; Lingens, F.
A novel type of oxygenolytic ring cleavage: 2,4-oxygenation and decarboxylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline
FEMS Microbiol. Lett.
117
299-304
1994
Arthrobacter sp., Arthrobacter sp. Ru61a
-
brenda
Fischer, F.; Kunne, S.; Fetzner, S.
Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases
J. Bacteriol.
181
5725-5733
1999
Arthrobacter sp.
brenda
Frerichs-Deeken, U.; Ranguelova, K.; Kappl, R.; Huettermann, J.; Fetzner, S.
Dioxygenases without requirement for cofactors and their chemical model reaction: compulsory order ternary complex mechanism of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase involving general base catalysis by histidine 251 and single-electron oxidation of the substrate dianion
Biochemistry
43
14485-14499
2004
Paenarthrobacter ilicis, Paenarthrobacter ilicis Ru61a
brenda
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
Curr. Microbiol.
51
344-352
2005
Paenarthrobacter nitroguajacolicus (Q7WSQ7), Paenarthrobacter nitroguajacolicus R61a (Q7WSQ7), Paenarthrobacter nitroguajacolicus R-61a (Q7WSQ7)
brenda
Steiner, R.A.; Frerichs-Deeken, U.; Fetzner, S.
Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rue61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily
Acta Crystallogr. Sect. F
63
382-385
2007
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R61a, Paenarthrobacter nitroguajacolicus Rue61a
brenda
Boehm, K.; Guddorf, J.; Albers, A.; Kamiyama, T.; Fetzner, S.; Hinz, H.
Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism
Biochemistry
47
7116-7126
2008
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus (Q7WSQ7), Paenarthrobacter nitroguajacolicus R61a (Q7WSQ7), Paenarthrobacter nitroguajacolicus R-61a
brenda
Beermann, B; Guddorf, J.; Boehm, K.; Albers, A.; Kolkenbrock, S.; Fetzner, S.; Hinz, H.-J.
Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Biochemistry
46
4241-4249
2007
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R61a
brenda
Pietra, F.
Binding pockets and permeation channels for dioxygen through cofactorless 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase in association with its natural substrate, 3-hydroxy-2-methylquinolin-4(1H)-one. A perspective from molecular dynamics simulations
Chem. Biodivers.
11
861-871
2014
Paenarthrobacter nitroguajacolicus (O31266)
brenda