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0.0692 - 0.1473
cumene hydroperoxide
0.0978 - 0.2025
tert-butyl hydroperoxide
0.0692
cumene hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
0.1473
cumene hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
0.00039
H2O2
pH 8.5, 30°C, mutant enzyme T43S
0.00039
H2O2
mutant enzyme T43S, at pH 8.5, temperature not specified in the publication
0.00084
H2O2
pH 8.5, 30°C, wild-type enzyme
0.00084
H2O2
wild type enzyme, at pH 8.5, temperature not specified in the publication
0.0011
H2O2
pH 8.5, 30°C, mutant enzyme T77V
0.0011
H2O2
mutant enzyme T77V, at pH 8.5, temperature not specified in the publication
0.0015
H2O2
pH 8.5, 30°C, mutant enzyme C165S
0.0015
H2O2
mutant enzyme C165S, at pH 8.5, temperature not specified in the publication
0.0027
H2O2
pH 8.0, 30°C, mutant enzyme W81F
0.0027
H2O2
mutant enzyme W81F, at pH 8.0, temperature not specified in the publication
0.014
H2O2
pH 8.5, 30°C, mutant enzyme T77I
0.014
H2O2
mutant enzyme T77I, at pH 8.5, temperature not specified in the publication
0.031
H2O2
pH 8.5, 30°C, mutant enzyme W169F
0.031
H2O2
mutant enzyme W169F, at pH 8.5, temperature not specified in the publication
0.034
H2O2
pH 8.5, 30°C, mutant enzyme T43A
0.034
H2O2
mutant enzyme T43A, at pH 8.5, temperature not specified in the publication
0.1934
H2O2
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
0.3479
H2O2
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
0.74
H2O2
pH 8.5, 30°C, mutant enzyme E49Q
0.74
H2O2
mutant enzyme E49Q, at pH 8.5, temperature not specified in the publication
1.5
H2O2
pH 8.5, 30°C, mutant enzyme R119A
1.5
H2O2
mutant enzyme R119A, at pH 8.5, temperature not specified in the publication
1.6
H2O2
pH 8.5, 30°C, mutant enzyme T43V
1.6
H2O2
mutant enzyme T43V, at pH 8.5, temperature not specified in the publication
0.0978
tert-butyl hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
0.2025
tert-butyl hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
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11.6 - 29.7
cumene hydroperoxide
9.5 - 26.1
tert-butyl hydroperoxide
11.6
cumene hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
29.7
cumene hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
0.4
H2O2
pH 8.5, 30°C, mutant enzyme C165S
0.4
H2O2
mutant enzyme C165S, at pH 8.5, temperature not specified in the publication
0.73
H2O2
pH 8.5, 30°C, mutant enzyme E49Q
0.73
H2O2
mutant enzyme E49Q, at pH 8.5, temperature not specified in the publication
2.8
H2O2
pH 8.5, 30°C, mutant enzyme T43V
2.8
H2O2
mutant enzyme T43V, at pH 8.5, temperature not specified in the publication
3.6
H2O2
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
3.8
H2O2
pH 8.5, 30°C, mutant enzyme T43A
3.8
H2O2
mutant enzyme T43A, at pH 8.5, temperature not specified in the publication
4.8
H2O2
pH 8.5, 30°C, mutant enzyme T77I
4.8
H2O2
mutant enzyme T77I, at pH 8.5, temperature not specified in the publication
7.1
H2O2
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
8.9
H2O2
pH 8.5, 30°C, mutant enzyme T43S
8.9
H2O2
mutant enzyme T43S, at pH 8.5, temperature not specified in the publication
9.6
H2O2
pH 8.5, 30°C, mutant enzyme W169F
9.6
H2O2
mutant enzyme W169F, at pH 8.5, temperature not specified in the publication
11.7
H2O2
pH 8.5, 30°C, mutant enzyme R119A
11.7
H2O2
mutant enzyme R119A, at pH 8.5, temperature not specified in the publication
19
H2O2
pH 8.0, 30°C, mutant enzyme W81F
19
H2O2
mutant enzyme W81F, at pH 8.0, temperature not specified in the publication
40
H2O2
pH 8.5, 30°C, wild-type enzyme
40
H2O2
wild type enzyme, at pH 8.5, temperature not specified in the publication
61
H2O2
pH 8.5, 30°C, mutant enzyme T77V
61
H2O2
mutant enzyme T77V, at pH 8.5, temperature not specified in the publication
9.5
tert-butyl hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
26.1
tert-butyl hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
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79 - 429
cumene hydroperoxide
47 - 267
tert-butyl hydroperoxide
79
cumene hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
429
cumene hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
0.99
H2O2
mutant enzyme E49Q, at pH 8.5, temperature not specified in the publication
1.8
H2O2
pH 8.5, 30°C, mutant enzyme T43V
1.8
H2O2
mutant enzyme T43V, at pH 8.5, temperature not specified in the publication
8
H2O2
pH 8.5, 30°C, mutant enzyme R119A
8
H2O2
mutant enzyme R119A, at pH 8.5, temperature not specified in the publication
10
H2O2
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
36
H2O2
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
99
H2O2
pH 8.5, 30°C, mutant enzyme E49Q
110
H2O2
pH 8.5, 30°C, mutant enzyme T43A
110
H2O2
mutant enzyme T43A, at pH 8.5, temperature not specified in the publication
270
H2O2
pH 8.5, 30°C, mutant enzyme C165S
270
H2O2
mutant enzyme C165S, at pH 8.5, temperature not specified in the publication
310
H2O2
pH 8.5, 30°C, mutant enzyme W169F
310
H2O2
mutant enzyme W169F, at pH 8.5, temperature not specified in the publication
340
H2O2
pH 8.5, 30°C, mutant enzyme T77I
340
H2O2
mutant enzyme T77I, at pH 8.5, temperature not specified in the publication
7200
H2O2
pH 8.0, 30°C, mutant enzyme W81F
7200
H2O2
mutant enzyme W81F, at pH 8.0, temperature not specified in the publication
23000
H2O2
pH 8.5, 30°C, mutant enzyme T43S
23000
H2O2
mutant enzyme T43S, at pH 8.5, temperature not specified in the publication
47000
H2O2
pH 8.5, 30°C, wild-type enzyme
47000
H2O2
wild type enzyme, at pH 8.5, temperature not specified in the publication
55000
H2O2
pH 8.5, 30°C, mutant enzyme T77V
55000
H2O2
mutant enzyme T77V, at pH 8.5, temperature not specified in the publication
47
tert-butyl hydroperoxide
in the presence of thioredoxin C as reducing system, at pH 7.4 and 25°C
267
tert-butyl hydroperoxide
in the presence of AhpD as reducing system, at pH 7.4 and 25°C
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malfunction
enzyme deletion affects the survival rate of Burkholderia thailandensis in response to peroxynitrite
malfunction
enzyme deletion leads to a higher sensitivity to hypochlorous acid, hydrogen peroxide and urate hydroperoxide. The enzyme-deficient strain is more sensitive to the killing by isolated neutrophils and less virulent in a mice model of infection
malfunction
-
inactivation of the enzyme gene negatively affects the viability of the SK586 mutant in biofilms, which is most noticeable under nitrogen limitation. Inactivation of the enzyme leads to an increased sensitivity to peroxides and to changes in flagellation, motility, and cell surface properties
malfunction
the enzyme-deficient mutant is attenuated for intramacrophage growth
malfunction
the enzyme-deficient mutant reveals enhanced sensitivities towards superoxide-generating compounds as indicated by significantly larger zones of inhibition around the discs impregnated with menadione, pyrogallol and paraquat as compared to those observed for wild type enzyme. The enzyme-deficient mutant exhibits enhanced sensitivity towards reactive nitrogen species, organic peroxides and H2O2, does not exhibit intramacrophage growth defect but is attenuated for virulence in mice
malfunction
-
the enzyme-deficient mutant reveals enhanced sensitivities towards superoxide-generating compounds as indicated by significantly larger zones of inhibition around the discs impregnated with menadione, pyrogallol and paraquat as compared to those observed for wild type enzyme. The enzyme-deficient mutant exhibits enhanced sensitivity towards reactive nitrogen species, organic peroxides and H2O2, does not exhibit intramacrophage growth defect but is attenuated for virulence in mice
-
malfunction
-
inactivation of the enzyme gene negatively affects the viability of the SK586 mutant in biofilms, which is most noticeable under nitrogen limitation. Inactivation of the enzyme leads to an increased sensitivity to peroxides and to changes in flagellation, motility, and cell surface properties
-
malfunction
-
enzyme deletion leads to a higher sensitivity to hypochlorous acid, hydrogen peroxide and urate hydroperoxide. The enzyme-deficient strain is more sensitive to the killing by isolated neutrophils and less virulent in a mice model of infection
-
malfunction
-
the enzyme-deficient mutant is attenuated for intramacrophage growth
-
metabolism
-
the enzyme plays a critical role in aerobic growth and removes the excess H2O2
metabolism
the enzyme plays an important role in peroxides and peroxynitrite damage response
metabolism
-
the enzyme plays a critical role in aerobic growth and removes the excess H2O2
-
physiological function
AhpC of Francisella tularensis LVS confers resistance against a wide range of reactive oxygen and nitrogen species, and serves as a virulence factor
physiological function
-
alkyl hydroperoxide reductase subunit C acquires chaperone activity under heat stress. High-molecular-weight oligomer formation and the chaperone-like activity of oxidized AhpC depend on the incubation temperature and the period of incubation
physiological function
dual function of Pseudomonas aeruginosa AhpF (PaAhpF) as a reductase and a molecular chaperone. The reductase and foldase chaperone function of PaAhpF predominated for its low-molecular-weight form, whereas the holdase chaperone function of PaAhpF is associated with its high-molecular-weight complex. PaAhpF has multiple function in controlling oxidative and heat stresses in Pseudomonas aeruginosa resistance to oxidative and heat stress
physiological function
in highly virulent Francisella tularensis SCHU S4 strain, AhpC serves as a key antioxidant enzyme and contributes to its robust oxidative and nitrosative stress resistance, and intramacrophage survival
physiological function
-
the enzyme activity enables the bacteria to overcome the negative effect of stress factors during the germination of the dried dormant forms
physiological function
-
the enzyme and catalase KatG act together to scavenge endogenous hydrogen peroxide. The enzyme has little effect on protecting cells against toxicity of organic peroxides
physiological function
the enzyme confers resistance against a wide range of reactive oxygen and nitrogen species, and serves as a virulence factor
physiological function
-
the enzyme is a particularly important peroxidase in oxidative stress resistance in Shewanella, not only playing a compensatory role for catalase, but also by itself providing sufficient protection from killing of H2O2 generated abiotically
physiological function
the enzyme is a relevant scavenger of oxidants generated during inflammatory oxidative burst and a mechanism of Pseudomonas aeruginosa escaping from killing
physiological function
the enzyme serves as a key antioxidant enzyme and contributes to its robust oxidative and nitrosative stress resistance, and intramacrophage survival
physiological function
-
the enzyme confers resistance against a wide range of reactive oxygen and nitrogen species, and serves as a virulence factor
-
physiological function
-
AhpC of Francisella tularensis LVS confers resistance against a wide range of reactive oxygen and nitrogen species, and serves as a virulence factor
-
physiological function
-
the enzyme activity enables the bacteria to overcome the negative effect of stress factors during the germination of the dried dormant forms
-
physiological function
-
the enzyme is a particularly important peroxidase in oxidative stress resistance in Shewanella, not only playing a compensatory role for catalase, but also by itself providing sufficient protection from killing of H2O2 generated abiotically
-
physiological function
-
the enzyme and catalase KatG act together to scavenge endogenous hydrogen peroxide. The enzyme has little effect on protecting cells against toxicity of organic peroxides
-
physiological function
-
the enzyme is a relevant scavenger of oxidants generated during inflammatory oxidative burst and a mechanism of Pseudomonas aeruginosa escaping from killing
-
physiological function
-
the enzyme serves as a key antioxidant enzyme and contributes to its robust oxidative and nitrosative stress resistance, and intramacrophage survival
-
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C13N
-
the mutant shows reduced activity compared to the wild type enzyme
C13N/C66V
-
the mutant shows reduced activity compared to the wild type enzyme
C66V
-
the mutant shows reduced activity compared to the wild type enzyme
C165S
-
kcat/Km for H2O2 is 192fold lower than wild-type value
-
E49Q
-
kcat/Km for H2O2 is 47619fold lower than wild-type value. Mutations destabilizes decamers in the reduced form
-
R119A
-
kcat/Km for H2O2 is 5882fold lower than wild-type value. Mutations destabilizes decamers in the reduced form
-
T77I
-
kcat/Km for H2O2 is 139fold lower than wild-type value
-
W169F
-
kcat/Km for H2O2 is 151fold lower than wild-type value
-
C168S
-
the mutant retains a significant share of H2O2-reducing activity
C165S
kcat/Km for H2O2 is 192fold lower than wild-type value
C165S
the mutant shows 0.52% activity with H2O2 compared to the wild type enzyme
E49Q
kcat/Km for H2O2 is 47619fold lower than wild-type value. Mutations destabilizes decamers in the reduced form
E49Q
the mutation lowers catalytic efficiency with hydrogen peroxide by 4-5 orders of magnitude, but does not affect reactivity toward their reductant, AhpF. The mutant shows 0.0021% activity with H2O2 compared to the wild type enzyme
R119A
kcat/Km for H2O2 is 5882fold lower than wild-type value. Mutations destabilizes decamers in the reduced form
R119A
the mutation lowers catalytic efficiency with hydrogen peroxide by 4-5 orders of magnitude, but does not affect reactivity toward their reductant, AhpF. The mutant shows 0.017% activity with H2O2 compared to the wild type enzyme
T43A
kcat/Km for H2O2 is 434fold lower than wild-type value
T43A
the mutant exhibits stabilized decamers and is more efficiently reduced by AhpF than wild type enzyme. The mutant shows 0.23% activity with H2O2 compared to the wild type enzyme
T43S
kcat/Km for H2O2 is 2fold lower than wild-type value. Mutation stabilizes oxidized decameric form
T43S
the mutant exhibits stabilized decamers and is more efficiently reduced by AhpF than wild type enzyme. The mutant shows 48% activity with H2O2 compared to the wild type enzyme
T43V
kcat/Km for H2O2 is 26315fold lower than wild-type value. Mutations destabilizes decamers in the reduced form. Mutation stabilizes oxidized decameric form
T43V
the mutation lowers catalytic efficiency with hydrogen peroxide by 4-5 orders of magnitude, but does not affect reactivity toward their reductant, AhpF. The mutant shows 0.0038% activity with H2O2 compared to the wild type enzyme
T77I
kcat/Km for H2O2 is 139fold lower than wild-type value
T77I
the mutant shows 0.72% activity with H2O2 compared to the wild type enzyme
T77V
kcat/Km for H2O2 is 83% comared to wild-type value. Mutation stabilizes reduced and oxidized decameric form
T77V
the mutant exhibits stabilized decamers and is more efficiently reduced by AhpF than wild type enzyme. The mutant shows 120% activity with H2O2 compared to the wild type enzyme
W169F
kcat/Km for H2O2 is 151fold lower than wild-type value
W169F
the mutant shows 0.66% activity with H2O2 compared to the wild type enzyme
W81F
kcat/Km for H2O2 is 6.7fold lower than wild-type value
W81F
the mutant shows 15% activity with H2O2 compared to the wild type enzyme
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Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus
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30019-30028
2000
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Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli
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Pseudomonas aeruginosa (Q9I6Z2), Pseudomonas aeruginosa
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