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2-propanol
55% residual activity in the presence of 90% (v/v) 2-propanol, after 60 min at 70°C
6-palmityl-ascorbic acid
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acetonitrile
43% residual activity in the presence of 90% (v/v) acetonitrile, after 60 min at 70°C
Ag+
9.7% residual activity at 5 mM
ascorbate
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0.5 mM inhibits by ca. 19%. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 91% inactivation
butylated hydroxytoluene
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CdCl2
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83% residual activity after 24 h in the presence of 0.02 mg/ml CdCl2
Cr3+
39.8% residual activity at 5 mM
D-penicillamine
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40.5% residual activity after 24 h in the presence of 0.2 mg/ml D-penicillamine
diethyldicarbonate
0.5 mM, complete loss of activity
diisopropyl fluorophosphate
diisopropylfluorophosphate
dimethyl sulfoxide
71% residual activity in the presence of 90% (v/v) dimethyl sulfoxide, after 60 min at 70°C
dimyristoylphosphatidic acid
0.4 mM, 81% inhibition of arylesterase activity, 64% inhibition of paraoxonase activity
dimyristoylphosphatidylserine
no significant inhibition of both paraoxonase and arylesterase activity up to 0.030 mM, remarkable inhibition of both activities at 0.10.4 mM, with a greater inhibition of arylesterase activity
dithiothreitol
19.4% residual activity at 5 mM
Fe3+
13.7% residual activity at 5 mM
high density lipoprotein
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incubation of serum or high density lipoprotein from healthy subjects with very low density lipoprotein significantly decreases serum paraoxonase 1 lactonase or arylesterase activities by up to 11% or 24%, and HDL-associated paraoxonase 1 lactonase or arylesterase activities by up to 32% or 46%, respectively
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iodoacetic acid
slight inhibition
lanthanum(III) chloride
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about 50% inhibition at 0.05 mM
methanol
48% residual activity in the presence of 90% (v/v) methanol, after 60 min at 70°C
methylglyoxal
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decreases specific activity in a concentration-dependent manner
metrifonate
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50% inhibition at 0.00048 mM, pralidoxime protects
N-ethylmaleimide
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leads to 24fold reduced enzyme activity at 0.2 mM
organophosphorous compounds
inhibit the enzyme of all genotypes slightly after in vivo exposure
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phenylmethylsulfonyl fluoride
piperonyl butoxide
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50% inhibition at 0.6 mM. Enzyme inhibition in vivo reaches a maximum after 4 h and enzyme subsequently recovers over a 24 h period
pyridoxal 5'-phosphate
0.5 mM, 62% residual activity
sodium dodecylsulfate
1 mM, 32% of initial activity
sodium hypochlorite
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at 1 mM causes approximately 15% decrease in activity, at 1 mM and in the presence of PBS buffer causes approximately 76% decrease in activity
tenoxicam
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tenoxicam decreases the arylesterase activity of the enzyme during the use of 12 h, in 0.74 mM and 1.48 mM dose
Tween 20
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51% residual activity at 10% (v/v)
Tween 80
21% residual activity in the presence of 5% (v/v) Tween 80, after 60 min at 70°C
Valproic acid
arylesterase activity is decreased after 60 days of valproic acid treatment
very low density lipoprotein
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inhibits recombinant paraoxonase 1 lactonase or arylesterase activities by up to 20% or 42%, respectively
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2-hydroxyquinoline
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70% inhibition
2-hydroxyquinoline
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specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
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dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
2-hydroxyquinoline
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specific inhibitor
2-hydroxyquinoline
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specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
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dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
2-mercaptoethanol
1 mM, 16% of initial activity
2-mercaptoethanol
73.5% residual activity at 5 mM
4-chloromercuribenzoate
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complete inhibition at 0.2 mM
4-chloromercuribenzoate
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Ca2+
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Ca2+
88.5% residual activity at 5 mM
Co2+
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Co2+
92.6% residual activity at 5 mM
Cu2+
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Cu2+
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oxidizes HDL and inactivates HDL-associated paraoxonase1, relationship, overview, the inactivation is enhanced catecholamines, such as 3,4-dihydroxyphenylalanine, dopamine, or norepinephrine, but not by uric acid or homocysteine, low enhancement of Cu2+-mediated enzyme inactivation by catecholamines caffeic acid and pyrocatechol, and by ascorbate, effects on activity of purified enzyme and HDL-complexed enzyme, overview, the inactivation in prevented by several compounds, e.g. by catalase, ethanol, oleic acid, substrate paraoxon, phenylacetate, and slightly by quercetin, mannitol, and DMSO in presence of 1 mM Ca2+
Cu2+
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0.001 mM inhibits by ca. 13%. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 91% inactivation. Ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 51% inactivation after 30 min
Cu2+
1 mM, 13% of initial activity
Cu2+
28.9% residual activity at 5 mM
diethyl dicarbonate
6% residual activity in the presence of 5 mM diethyl dicarbonate, after 30 min at 30°C
diethyl dicarbonate
5.5% residual activity at 5 mM
diisopropyl fluorophosphate
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diisopropyl fluorophosphate
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diisopropylfluorophosphate
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competitive inhibition
diisopropylfluorophosphate
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diisopropylfluorophosphate
complete inactivation at 5 mM diisopropylfluorophosphate, after 30 min at 30°C
EDTA
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EDTA
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1 mM, completely and irreversibly inhibits activity with phenyl acetate
EDTA
complete inhibition of phenyl acetate hydrolyzing activity
EDTA
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74% residual activity after 24 h in the presence of 0.05 mg/ml EDTA
EDTA
92% residual activity in the presence of 10 mM EDTA, after 30 min at 75°C
EDTA
94.2% residual activity at 5 mM
EDTA
0.05-10 mM, nearly complete loss of activity
eserine
0.5 mM, 42% residual activity
eserine
92% residual activity in the presence of 5 mM eserine, after 30 min at 30°C
ethanol
63% residual activity in the presence of 90% (v/v) ethanol, after 60 min at 70°C
ethanol
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with 20% ethanol and 5-10% sodium dodecyl sulfate, whereas no significant changes in presence of 10% ethanol. Mg2+ and Ca2+ have no effect
Fe2+
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Fe2+
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ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 51% inactivation after 30 min
Hg2+
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Hg2+
1 mM, 14% of initial activity
Hg2+
complete inactivation at 5 mM Hg2+, after 30 min at 30°C
Hg2+
7.2% residual activity at 5 mM
Mg2+
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Mg2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
Mg2+
89.2% residual activity at 5 mM
Mn2+
-
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Mn2+
85.4% residual activity at 5 mM
NaCl
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1.0 mM NaCl decreases the serum arylesterase activity of the enzyme
NaCl
76% residual activity in the presence of 2 M NaCl, after 60 min at 70°C
NaCl
43.7% residual activity at 4 M
Ni2+
1 mM, 23% of initial activity
Ni2+
86.3% residual activity at 5 mM
p-chloromercuribenzoate
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p-chloromercuribenzoate
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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p-hydroxymercuribenzoate
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paraoxon
0.5 mM, complete loss of activity
paraoxon
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mixed type inhibition
Pb2+
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Pb2+
45.7% residual activity at 5 mM
pepstatin A
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phenyl acetate
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phenyl acetate
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inhibits hydrolysis of 4-nitrophenyl acetate
Phenylglyoxal
0.5 mM, 77% residual activity
Phenylglyoxal
97% residual activity in the presence of 5 mM phenylglyoxal, after 30 min at 30°C
phenylmethylsulfonyl fluoride
23% residual activity in the presence of 5 mM phenylmethylsulfonyl fluoride, after 30 min at 30°C
phenylmethylsulfonyl fluoride
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phenylmethylsulfonyl fluoride
complete inhibition at 5 mM
PMSF
1 mM
SDS
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complete inhibition at 5 and 10% (w/v)
SDS
about half of the activity is retained at 1% SDS after incubation for 60 min at 70°C, the addition of 5% SDS completely eliminates the enzyme activity at 70°C
SDS
complete inhibition at 5% (w/v)
Triton X-100
-
61% residual activity at 10% (v/v)
Triton X-100
11% residual activity in the presence of 5% (v/v) Tween 80, after 60 min at 70°C
Urea
88% residual activity in the presence of 8 M urea, after 60 min at 70°C
Urea
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leads to complete unfolding at 2.0 M
Urea
64.7% residual activity at 8 M
Zn2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
Zn2+
76.4% residual activity at 5 mM
additional information
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not: Cd2+
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additional information
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additional information
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no inhibition by diisopropyl fluorophosphate and sodium fluoride
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additional information
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the enzyme is sensitive to oxidative stress
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additional information
0.2 mM dimyristoylphosphatidylethanol inhibits paraoxonase activity but has no effect on arylesterase activity
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additional information
the arylesterase activity of PON1 is not correlated with plasma concentrations of total cholesterol, low density lipoprotein-cholesterol, high density lipoprotein-cholesterol, or triacylglycerol in atherosclerosis obliterans patients
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additional information
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the arylesterase activity of PON1 is not correlated with plasma concentrations of total cholesterol, low density lipoprotein-cholesterol, high density lipoprotein-cholesterol, or triacylglycerol in atherosclerosis obliterans patients
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additional information
high plasma C-reactive protein is related to low paraoxonase-I activity
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additional information
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1 mM 3-morpholinosydnoimine, 0.002 mM Fe2+ or 0.01 mM Mn2+, Co2+, Zn2+ cause no significant loss of activity
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additional information
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crystalline particles Min-U-Sil 5 reduce activity due to decreased protein concentrations
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additional information
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not inhibited by diclofenac sodium
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additional information
no inhibition by EDTA and iodoacetic acid
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additional information
infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
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additional information
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infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
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additional information
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ethanol consumption causes a decrease in liver arylesterase activity, which is not significant. Gallic acid treatment restores the loss of this activity due to ethanol exposure. Ethanol consumption causes a significant decrease in liver paraoxonase activity, gallic acid treatment partly restores this decreased paraoxonase activity
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additional information
addition of glycerin has no effect on the enzyme activity
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