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0.000008
-
wild type enzyme, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00015
-
wild type enzyme, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00019
-
mutant enzyme A80V/F132C/K185R/D208G/H257W/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00022
-
mutant enzyme A80V/K185R/D208G/H257W/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00042
-
purified recombinant enzyme, substrate paraoxon
0.00045
-
mutant enzyme A80V/F132D/K185R/D208G/H257W/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00048
-
mutant enzyme A80V/K185R/D208G/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00075
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.0012
wild type enzyme from crude extract, using paraoxon as substrate
0.0013
mutant enzyme Q192R from crude extract, using paraoxon as substrate
0.00151
-
mutant enzyme A80V/K185R/D208G/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.0022
-
purified recombinant enzyme, substrate methyl paraoxon
0.00414
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00429
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00472
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00509
-
mutant enzyme A80V/K185R/D208G/H257W/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.00617
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.007
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using VX as substrate, in 10 mM N-Tris (hydroxymethyl-3-amino propanesulfonic acid), pH 8.0 , at 25°C
0.00711
-
crude enzyme, at pH 8.0, 37°C
0.01159
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.01404
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.01511
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, using malathion as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.0194
-
mutant enzyme A80V/F132D/K185R/D208G/H257W/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.02677
-
mutant enzyme A80V/F132C/K185R/D208G/H257W/I274N/R319S, using demeton-S methyl as substrate, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.0803
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, using VX as substrate, in 10 mM N-Tris (hydroxymethyl-3-amino propanesulfonic acid), pH 8.0 , at 25°C
0.083
substrate O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, pH 8.0, 25°C, enzyme mutant C23 administered in guinea pigs in vivo
0.097
-
wild type enzyme, using VX as substrate, in 10 mM N-Tris (hydroxymethyl-3-amino propanesulfonic acid), pH 8.0 , at 25°C
0.1
about, wild-type enzyme, substrate chlorpyrifos
0.15
purified recombinant PON1 wild-type enzyme, pH 10.5, 25°C, substrate diethyl-paraoxon
0.18
purified recombinant PON1-hFc fusion enzyme, pH 10.5, 25°C, substrate diethyl-paraoxon
0.205
pH 8.5, 25°C, substrate: paraoxon, purified recombinant enzyme
0.344
-
crude enzyme, pH 8.0, 37°C
0.42
purified recombinant enzyme mutant W263F, pH 8.5, 65°C, substrate diethyl-paraoxon
0.567
substrate cyclosarin, pH 8.0, 25°C, enzyme administered in guinea pigs in vivo
0.611
-
using paraoxin as substrate (paraoxonase activity of PON1), at 25°C
0.94
mutant enzyme Q192R after 1018fold purification, using paraoxon as substrate
0.962
-
purified enzyme from phenotype A blood plasma
1
about, genetic variants A1030 and A1467, substrate chlorpyrifos
1.21
wild type enzyme after 1018fold purification, using paraoxon as substrate
1.4
substrate cyclosarin, pH 8.0, 37°C, enzyme administered in guinea pigs in vivo
1.76
-
Q192 isoenzyme, serum, pH 8 at 37°C, in Tris-base buffer
1.88
-
isozyme 192Q, crude enzyme, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
1.94
pH 8.5, 25°C, substrate: paraoxon, purified recombinant enzyme
10.78
-
enzyme of breed Swiss Black, pH 8.0, 25°C
113
pH 8.5, 25°C, substrate: diazoxon, purified recombinant enzyme
1168
-
isozyme 192R, crude enzyme, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
12.03
-
substrate paraoxon, wild-type enzyme, pH and temperature not specified in the publication
12.3
-
substrate: paraoxon, pH 8.5, 70°C, Mn2+-containing enzyme
12.8
purified recombinant enzyme mutant W263F, pH 8.5, 65°C, substrate diethyl-paraoxon
12.84
-
after 37.3fold purification, pH 8.0, 37°C
122.6
substrate paraoxon, enzyme mutant C258L/I261F/W263A, pH and temperature not specified in the publication
123.6
purified recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C, substrate diethyl-paraoxon
14.92
-
after 1690fold purification, at pH 8.0, 37°C
168
recombinant enzyme in presence of Co2+
1730
-
purified serum enzyme
2.5
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, using VX as substrate, in 10 mM N-Tris (hydroxymethyl-3-amino propanesulfonic acid), pH 8.0 , at 25°C
2109
-
Q192 isoenzyme, 901fold purified, pH 8 at 37°C, in Tris-base buffer
22.4
-
enzyme of breed Montofon, pH 8.0, 25°C
3221
-
isozyme 192R, after 742fold purification, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
33
-
substrate ethyl parathion
3333
-
R192 isoenzyme, 453fold purified, pH 8 at 37°C, in Tris-base buffer
34
recombinant enzyme in absence of Co2+
35
about, genetic variant B3561, substrate chlorpyrifos
3840
-
in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C
4.34
-
isozyme 192Q, after 589.7fold purification, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
40.9
pH 8.5, 25°C, substrate: chlorpyrifos oxon, purified recombinant enzyme
438.2
-
515fold purified enzyme, at 37°C
465
recombinant enzyme after 90fold purification
5
about, genetic variant B2136, substrate chlorpyrifos
5.15
recombinant enzyme from crude cell extract
5.21
-
R192 isoenzyme, serum, pH 8 at 37°C, in Tris-base buffer
53.8
purified recombinant His-tagged mature enzyme
6.64
-
purified enzyme from phenotype A blood plasma
76.3
-
purified enzyme, substrate 4-nitrophenyl phosphate at pH 7.0 and 25°C
8310
-
substrate methyl paraoxon, 30°C, pH 8.0
27
-
enzyme of breed Holstein, pH 8.0, 25°C
27
about, genetic variant B1368, substrate chlorpyrifos
additional information
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additional information
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assay method evaluation of analogues with fluorescent leaving groups for screening and selection of the enzyme that efficiently hydrolyzes organophosphorus nerve agents, overview
additional information
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-
additional information
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His6-tagged organophosphate hydrolase fused with alpha-helical leucine zipper domains and unstructured soluble linker domains shows specific activities from 1.6-2.2 units for paraoxon, 0.61-1.3 units for parathion and 0.011-0.036 units for ethyl parathion (one unit is defined as mol of substrate per mol enzyme per second), in 50 mM carbonate buffer (pH 10.5), at 25°C
additional information
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relative rates of hydrolysis for several substrates
additional information
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assay method evaluation of analogues with fluorescent leaving groups for screening and selection of the enzyme that efficiently hydrolyzes organophosphorus nerve agents, overview
additional information
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enzyme activity in individuals of both sexes and different age, overview
additional information
new enzymatic tests are developed that detect total PON1 levels, irrespective of high-density lipoprotein status and R/Q polymorphism, as well as the degree of catalytic stimulation and increased stability that follows tight binding of PON1 to HDLapoA-I. The tests are based on measuring total PON1 levels with a fluorogenic phosphotriester, measuring the lipolactonase activity with a chromogenic lactone, and assaying the chelator-mediated inactivation rate of the enzyme. The latter two are affected by tight binding of high-density lipoprotein and thereby derive the levels of the serum PON1-HDL complex. The new tests are demonstrated with a group of healthy individuals and show that the levels of PON1-HDL vary by a factor of 12
additional information
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new enzymatic tests are developed that detect total PON1 levels, irrespective of high-density lipoprotein status and R/Q polymorphism, as well as the degree of catalytic stimulation and increased stability that follows tight binding of PON1 to HDLapoA-I. The tests are based on measuring total PON1 levels with a fluorogenic phosphotriester, measuring the lipolactonase activity with a chromogenic lactone, and assaying the chelator-mediated inactivation rate of the enzyme. The latter two are affected by tight binding of high-density lipoprotein and thereby derive the levels of the serum PON1-HDL complex. The new tests are demonstrated with a group of healthy individuals and show that the levels of PON1-HDL vary by a factor of 12
additional information
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activity in wild-type strain WCP904 and of purified recombinant enzyme with different organophosphorus pesticides, overview
additional information
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specific activity of five enzyme fractions determined with paraoxon, diazoxon or chlorpyrifos-oxon
additional information
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-
additional information
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