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1-naphthyl acetate + H2O
1-naphthol + acetate
1-naphthyl butyrate + H2O
1-naphthol + butyrate
-
-
-
-
?
1-phenylvinyl acetate + H2O
1-phenylethylenol + acetate
-
-
-
?
2,2,2-trifluoroethyl acetate + H2O
2,2,2-trifluoroethanol + acetate
-
-
-
?
2,2-difluoroethyl acetate + H2O
2,2-difluoroethanol + acetate
-
-
-
?
2,3-difluorophenyl acetate + H2O
2,3-difluorophenol + acetate
-
-
-
?
2,4-difluorophenyl acetate + H2O
2,4-difluorophenol + acetate
-
-
-
?
2,6-difluorophenyl acetate + H2O
2,6-difluorophenol + acetate
-
-
-
?
2-carboxythiophenyl acetate + H2O
2-carboxythiophenol + acetate
-
-
-
?
2-fluoroethyl acetate + H2O
2-fluoroethanol + acetate
-
-
-
?
2-fluorophenyl acetate + H2O
2-fluorophenol + acetate
-
-
-
?
2-methoxythiophenyl acetate + H2O
2-methoxythiophenol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
2-naphthyl butanoate + H2O
2-naphthol + butanoate
-
-
-
?
2-naphthyl butyrate + H2O
2-naphthol + butyrate
-
-
-
-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
3,4-dimethyl phenyl acetate + H2O
3,4-dimethylphenol + acetate
-
-
-
?
3-acetoxypyridine + H2O
?
-
-
?
3-cyanophenyl acetate + H2O
3-cyanophenol + acetate
-
-
-
?
3-fluorophenyl acetate + H2O
3-fluorophenol + acetate
-
-
-
?
3-naphthyl acetate + H2O
3-naphthol + acetate
-
-
-
?
3-naphthyl butanoate + H2O
3-naphthol + butanoate
-
-
-
?
3-nitrophenyl acetate + H2O
3-nitrophenol + acetate
-
-
-
?
4-(chloromethyl)phenyl acetate + H2O
4-chloromethyl phenol + acetate
-
-
-
?
4-acetoxyacetophenone + H2O
4-hydroxyacetophenone + acetate
-
-
-
?
4-acetoxybenzaldehyde + H2O
4-hydroxybenzaldehyde + acetate
-
-
-
?
4-acetoxybenzaldehyde + H2O
?
4-carboxyphenyl acetate + H2O
4-carboxyphenol + acetate
-
-
-
?
4-chlorophenyl acetate + H2O
4-chlorophenol + acetate
-
-
-
?
4-cyanophenyl acetate + H2O
4-cyanophenol + acetate
-
-
-
?
4-diethyl phosphate methyl benzoate + H2O
?
-
-
-
?
4-methoxy phenyl acetate + H2O
4-methoxy phenol + acetate
-
-
-
?
4-methylphenyl acetate + H2O
4-methylphenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
4-nitrophenyl diethylphosphate + H2O
diethylphosphate + 4-nitrophenol
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
about 10% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
?
7-aminocephalosporanic acid + H2O
?
-
-
-
-
?
9-(2,4-dimethylphenoxycarbonyl)-10-methylacridinium triflate + H2O
2,4-dimethylphenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
9-(4-chlorophenoxycarbonyl)-10-methylacridinium triflate + H2O
4-chlorophenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate + H2O
9-carboxy-10-methylacridinium triflate + 4-chlorophenol
-
-
-
-
?
9-(4-methylphenoxycarbonyl)-10-methylacridinium triflate + H2O
4-methylphenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
9-(4-tert-butylphenoxycarbonyl)-10-methylacridinium triflate + H2O
4-tert-butylphenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
9-(phenyloxycarbonyl)-10-methylacridinium triflate + H2O
phenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
acetylcholine chloride + H2O
?
-
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
benzyl acetate + H2O
benzyl alcohol + acetate
-
-
-
?
beta-naphthyl acetate + H2O
beta-naphthol + acetate
-
-
-
-
?
bromoxynil octanoate + H2O
?
butyl acetate + H2O
butanol + acetate
-
-
-
?
butyrylcholine iodide + H2O
?
-
-
-
-
?
cephalosporin C + H2O
?
-
-
-
-
?
ethyl acetate + H2O
ethanol + acetate
-
-
-
?
ethyl hexanoate + H2O
ethanol + hexanoate
-
-
?
isopropyl acetate + H2O
isobutanol + acetate
-
-
-
?
ketoprofen ethyl ester + H2O
?
-
-
-
-
?
methyl 4-(acetyloxy)benzoate + H2O
methyl 4-hydroxybenzoate + acetate
-
-
-
?
mipafox + H2O
?
-
-
-
-
?
naphthalen-2-yl acetate + H2O
2-naphthol + acetate
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propanoate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
phenyl valerate + H2O
phenol + valerate
-
-
-
-
?
phenylacetate + H2O
phenol + acetate
phenylthioacetate + H2O
thiophenol + acetate
propioncholine iodide + H2O
?
-
-
-
-
?
propyl acetate + H2O
propanol + acetate
-
-
-
?
S-(4-carboxyphenyl)-thioacetate + H2O
4-carboxythiophenol + acetate
-
-
-
?
S-methyl thiobutanoate + H2O
methanol + thiobutanoate
thiophenyl acetate + H2O
?
thiophenyl acetate + H2O
thiophenol + acetate
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
[(3-[(3-hydroxypropoxy)carbonyl]-5-[[3-([4-[(3-hydroxypropoxy)carbonyl]benzoyl]oxy)propoxy]carbonyl]phenyl)-lambda4-sulfanetriyl]tris(oxidanide) + H2O
terephthalic acid + 5-sulfoisophthalic acid + 1,3-propanediol
-
-
-
?
additional information
?
-
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
0.1% of the activity with phenyl acetate, A-type enzyme. 0.25% of the activity with phenyl acetate, B-type enzyme
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
0.1% of the activity with phenyl acetate
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
15.4% activity compared to 4-nitrophenyl acetate
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
5.5% of the activity with phenyl acetate, A-type enzyme. 7% of the activity with phenyl acetate, B-type enzyme
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
13.5% of the activity with phenyl acetate
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
-
-
-
-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
-
2.1% of the activity with phenyl acetate, A-type enzyme. 2% of the activity with phenyl acetate, B-type enzyme
-
-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
-
29% of the activity with phenyl acetate
-
-
?
4-acetoxybenzaldehyde + H2O
?
-
-
-
?
4-acetoxybenzaldehyde + H2O
?
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?, ir
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
2.5% of the activity with phenyl acetate, A-type enzyme. 3.5% of the activity with phenyl acetate, B-type enzyme
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
activity is 2.6fold higher than that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
activity is about 40% of the activity with PON3 (Q15166 (UniProt))
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
activity is about 5% of that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
31% of the activity with phenyl acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
inversely proportional relationship between the maximum specific growth rates of rhizobia strains and the activity of the entire alpha-esterase and beta-esterase pattern
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
shows maximum activity (100%) against p-nitrophenyl acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
highest catalytic efficiency (100% activity)
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
about 15% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
highest specific activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
best substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
best substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
activity is similar to that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
19.7% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4.1% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
10% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
about 10% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
low activity
-
-
?
4-nitrophenyl diethylphosphate + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
4-nitrophenyl diethylphosphate + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
about 10% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
about 5% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
activity is 1.5fold higher than that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
activity is 8.7fold higher than that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
activity is about 10% of the activity with PON3 (Q15166 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
activity is about 65% of the activity with PON3 (Q15166 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
activity is about 7% of that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
-
?
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
-
-
-
?
binapacryl + H2O
?
-
-
-
?
binapacryl + H2O
?
-
-
-
?
binapacryl + H2O
?
-
-
-
?
bromoxynil octanoate + H2O
?
-
-
-
?
bromoxynil octanoate + H2O
?
-
-
-
?
bromoxynil octanoate + H2O
?
-
-
-
?
diclofop methyl + H2O
?
-
-
-
?
diclofop methyl + H2O
?
-
-
-
?
diclofop methyl + H2O
?
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
ir
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
652704, 665028, 692695, 693321, 702421, 703470, 707155, 707214, 708095, 709261, 709755, 714112, 714759, 714893, 714895, 715735, 715738, 729339, 749628, 749762, 749840, 750340, 750345, 750428, 750482, 750483, 750484, 750511, 750758, 752150, 752173 -
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
activity is less than 1% of that with PON1 (P27169 (UniProt))
-
-
?
phenyl acetate + H2O
phenol + acetate
activity is more than 100fold higher than with PON2 (Q15165 (UniProt)) and PON3 (Q15166 (UniProt))
-
-
?
phenyl acetate + H2O
phenol + acetate
arylesterase activity is independent of the polymorphic form of PON1
-
-
?
phenyl acetate + H2O
phenol + acetate
arylesterase activity of PON1
-
-
?
phenyl acetate + H2O
phenol + acetate
enzyme protein also shows activities of EC 3.1.8.1 and EC 3.1.1.25
-
-
?
phenyl acetate + H2O
phenol + acetate
-
human serum paraoxonase/arylesterase is an esterase with broad substrate specificity. It occurs in two genetically determined allozymic forms, designated types A and B. These allozymes are the products of two allelic genes located at the paraoxonase locus on chromosome 7, which is closely linked to the gene for cystic fibrosis. Paraoxonase activity of the B type isozyme is considerably higher and stimulated more by 1 M NaCl than A-type paraoxonase. The ratio of paraoxonase activity to arylesterase activity of the B-isozyme is about 8, and that of the A isozyme about 1
-
-
?
phenyl acetate + H2O
phenol + acetate
lowest activity with phenyl acetate
-
-
?
phenyl acetate + H2O
phenol + acetate
-
PON1 activity determined towards the synthetic compounds paraoxon and phenyl acetate reflects no association with markers of oxidative stress
-
-
?
phenyl acetate + H2O
phenol + acetate
PON1 activity determined towards the synthetic compounds paraoxon and phenyl acetate reflects no association with markers of oxidative stress
-
-
?
phenyl acetate + H2O
phenol + acetate
shows highest hydrolytic rate towards phenyl acetate
-
-
?
phenyl acetate + H2O
phenol + acetate
-
the enzyme exists in two genetically determined allozymic forms, and these A and B allozymes possess both paraoxonase and arylesterase activities. B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
?
phenyl acetate + H2O
phenol + acetate
best substrate
-
?
phenyl acetate + H2O
phenol + acetate
best substrate
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
166% activity compared to 4-nitrophenyl acetate
-
-
?
phenylacetate + H2O
phenol + acetate
-
-
-
-
?
phenylacetate + H2O
phenol + acetate
-
-
-
?
phenylacetate + H2O
phenol + acetate
-
-
-
-
?
phenylacetate + H2O
phenol + acetate
-
-
-
?
phenylacetate + H2O
phenol + acetate
-
-
-
-
?
phenylthioacetate + H2O
thiophenol + acetate
-
-
?
phenylthioacetate + H2O
thiophenol + acetate
-
-
?
phenylthioacetate + H2O
thiophenol + acetate
-
-
?
S-methyl thiobutanoate + H2O
methanol + thiobutanoate
-
-
-
-
?
S-methyl thiobutanoate + H2O
methanol + thiobutanoate
-
-
-
?
thiophenyl acetate + H2O
?
-
27% of the activity with phenyl acetate, A-type enzyme. 34% of the activity with phenyl acetate, B-type enzyme
-
-
?
thiophenyl acetate + H2O
?
-
30.5% of the activity with phenyl acetate
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
-
-
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
-
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl laurate and 4-nitrophenyl palmitate
-
-
?
additional information
?
-
-
the enzyme is a carboxylesterase and has highest activity with 4-nitrophenyl butyrate, activity decreases with acylglycerols containing longer carbon chains
-
-
?
additional information
?
-
substrate specificity of this arylesterase is higher toward short chain pnitrophenyl esters (C2 to C4) and also toward aromatic esters, such as phenyl acetate. enzyme is a serine esterase, the catalytic triad is composed of residues Ser163, Asp263, and His293 in the active site
-
-
?
additional information
?
-
substrate specificity of this arylesterase is higher toward short chain pnitrophenyl esters (C2 to C4) and also toward aromatic esters, such as phenyl acetate. enzyme is a serine esterase, the catalytic triad is composed of residues Ser163, Asp263, and His293 in the active site
-
-
?
additional information
?
-
-
the enzyme is one of the HDL-associated antioxidant proteins, overview
-
-
?
additional information
?
-
-
paraoxonase-1 is an enzyme with three activities which are inversely related to cardiovascular diseases, paraoxonase and arylesterase activities are involved in coronary artery disease, overview
-
-
?
additional information
?
-
-
polymorphisms allele frequency in relation to exposure of individuals to organophosphates, overview
-
-
?
additional information
?
-
polymorphisms allele frequency in relation to exposure of individuals to organophosphates, overview
-
-
?
additional information
?
-
PON1 hydrolyses esters, including organophosphates and lactones, and exhibits anti-atherogenic properties, the enzyme is associated to high-density-lipoprotein, bound together with the human phosphate binding protein
-
-
?
additional information
?
-
-
PON1 hydrolyses esters, including organophosphates and lactones, and exhibits anti-atherogenic properties, the enzyme is associated to high-density-lipoprotein, bound together with the human phosphate binding protein
-
-
?
additional information
?
-
-
the enzyme is important in the mechanism of organophosphorous toxicity
-
-
?
additional information
?
-
the enzyme is important in the mechanism of organophosphorous toxicity
-
-
?
additional information
?
-
PON1 hydrolyzes organophosphates, such as paraoxon, aromatic esters, for instance, phenyl acetate, and also lipid peroxidation products, and reduces the accumulation of them, PON1 prevents the acceleration of atherosclerosis, exhibits antioxidant ability, and assumes an antiatherogenic property. Negative correlation between the activity of PON1 and the level of lipid hydroperoxides in the rheumatoid arthritis patient group, overview
-
-
?
additional information
?
-
-
PON1 hydrolyzes organophosphates, such as paraoxon, aromatic esters, for instance, phenyl acetate, and also lipid peroxidation products, and reduces the accumulation of them, PON1 prevents the acceleration of atherosclerosis, exhibits antioxidant ability, and assumes an antiatherogenic property. Negative correlation between the activity of PON1 and the level of lipid hydroperoxides in the rheumatoid arthritis patient group, overview
-
-
?
additional information
?
-
PON1 is not able to prevent macrophage oxidative stress, however, is able to retard macrophage-induced low-density lipoprotein oxidation
-
-
?
additional information
?
-
-
PON1 is not able to prevent macrophage oxidative stress, however, is able to retard macrophage-induced low-density lipoprotein oxidation
-
-
?
additional information
?
-
PON1 plays a key role in the protection of low density lipoproteins and high density lipoproteins from oxidation by hydrolyzing activated phospholipids and lipid peroxide products
-
-
?
additional information
?
-
-
PON1 plays a key role in the protection of low density lipoproteins and high density lipoproteins from oxidation by hydrolyzing activated phospholipids and lipid peroxide products
-
-
?
additional information
?
-
the active site of the enzyme is characterized by two distinct binding regions, the hydrophobic binding site for arylesters/lactones and the paraoxon binding site for phosphotriesters
-
-
?
additional information
?
-
-
the active site of the enzyme is characterized by two distinct binding regions, the hydrophobic binding site for arylesters/lactones and the paraoxon binding site for phosphotriesters
-
-
?
additional information
?
-
the enzyme is located on high-density lipoprotein and prevents low-density-lipoprotein and high-density-lipoprotein oxidation both in vivo and in vitro through hydrolysis of lipid peroxides, the risk of ischemic stroke is related to the genotype of PON1 192RQ polymorphisms, overview
-
-
?
additional information
?
-
-
the enzyme is located on high-density lipoprotein and prevents low-density-lipoprotein and high-density-lipoprotein oxidation both in vivo and in vitro through hydrolysis of lipid peroxides, the risk of ischemic stroke is related to the genotype of PON1 192RQ polymorphisms, overview
-
-
?
additional information
?
-
does not hydrolyse demeton-S-methyl
-
-
?
additional information
?
-
-
does not hydrolyse demeton-S-methyl
-
-
?
additional information
?
-
exhibits diazoxonase, paraoxonase, and arylesterase activities
-
-
?
additional information
?
-
paraoxonase 1 enzyme with three activities, which are paraoxonase, arylesterase and diazoxonase
-
-
?
additional information
?
-
-
paraoxonase 1 enzyme with three activities, which are paraoxonase, arylesterase and diazoxonase
-
-
?
additional information
?
-
-
PON1 catalyses the hydrolysis of arylesters, toxic organophosphate compounds, carbamates and lactones, shows higher arylesterase than paraoxonase activity
-
-
?
additional information
?
-
PON1 contains paraoxonase and arylesterase activities
-
-
?
additional information
?
-
-
PON1 contains paraoxonase and arylesterase activities
-
-
?
additional information
?
-
PON1 hydrolyzes organophosphates, arylesters and lactones, whereas the lactones activity is assumed as the physio/pathological one
-
-
?
additional information
?
-
PON1 is an high density lipoprotein-associated enzyme with three activities: paraoxonase, arylesterase and dyazoxonase
-
-
?
additional information
?
-
-
PON1 is an high density lipoprotein-associated enzyme with three activities: paraoxonase, arylesterase and dyazoxonase
-
-
?
additional information
?
-
rhPON3 can effectively delay and inhibit oxidation of high density lipoprotein in vitro
-
-
?
additional information
?
-
-
rhPON3 can effectively delay and inhibit oxidation of high density lipoprotein in vitro
-
-
?
additional information
?
-
the enzyme can delay and inhibit low-density lipoprotein oxidation in a dose-dependent manner
-
-
?
additional information
?
-
the enzyme contains arylesterase, paraoxonase, and lactonase activities
-
-
?
additional information
?
-
-
the enzyme contains arylesterase, paraoxonase, and lactonase activities
-
-
?
additional information
?
-
the phenyl acetate esterase activity of paraoxonase-1 shows normal solvent kinetic isotope effects, while proton inventory analysis indicates that two protons contribute to the kinetic isotope effect. Moderate competitive inhibition with the phenyl methylphosphonate anion reveals that the rate-limiting transition state suboptimally resembles the tetrahedral intermediate. Despite the presence of the Ca2+-promoted oxyanion hole, the catalytic power can be mostly rationalized by concerted two-proton exchange reorganisation at the active site
-
-
?
additional information
?
-
-
the phenyl acetate esterase activity of paraoxonase-1 shows normal solvent kinetic isotope effects, while proton inventory analysis indicates that two protons contribute to the kinetic isotope effect. Moderate competitive inhibition with the phenyl methylphosphonate anion reveals that the rate-limiting transition state suboptimally resembles the tetrahedral intermediate. Despite the presence of the Ca2+-promoted oxyanion hole, the catalytic power can be mostly rationalized by concerted two-proton exchange reorganisation at the active site
-
-
?
additional information
?
-
-
the rate-limiting step is the nucleophilic attack of the carbonyl group of the substrate by a water molecule. The active site is preorganized with no induced fit, and the enzyme-bound calcium plays an important role in stabilizing both the substrate and the transition state
-
-
?
additional information
?
-
no activity with ethyl acetate, ethyl propionate, ethyl butanoate, ethyl pentanoate, propyl acetate, butyl acetate, hexanoyl acetate, and 4-nitrophenyl esters of chain length C10-C16
-
?
additional information
?
-
-
no activity with ethyl acetate, ethyl propionate, ethyl butanoate, ethyl pentanoate, propyl acetate, butyl acetate, hexanoyl acetate, and 4-nitrophenyl esters of chain length C10-C16
-
?
additional information
?
-
substrate specificity, no activity with 4-nitrophenyl caprate, 4-nitrophenyl laurate, 4-nitrophenyl phosphate, 4-nitrophenyl sulfate, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl phenylphosphonate, stearoyl-CoA, palmitoyl-CoA, methylacetylsalicylate, ethyl acetate, propyl acetate, isopropyl acetate, butyl acetate, isobutyl acetate, isoamyl acetate, and caproyl acetate
-
?
additional information
?
-
substrate specificity, no activity with 4-nitrophenyl caprate, 4-nitrophenyl laurate, 4-nitrophenyl phosphate, 4-nitrophenyl sulfate, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl phenylphosphonate, stearoyl-CoA, palmitoyl-CoA, methylacetylsalicylate, ethyl acetate, propyl acetate, isopropyl acetate, butyl acetate, isobutyl acetate, isoamyl acetate, and caproyl acetate
-
?
additional information
?
-
-
substrate specificity, no activity with 4-nitrophenyl caprate, 4-nitrophenyl laurate, 4-nitrophenyl phosphate, 4-nitrophenyl sulfate, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl phenylphosphonate, stearoyl-CoA, palmitoyl-CoA, methylacetylsalicylate, ethyl acetate, propyl acetate, isopropyl acetate, butyl acetate, isobutyl acetate, isoamyl acetate, and caproyl acetate
-
?
additional information
?
-
-
does not use paraoxon as a substrate
-
-
?
additional information
?
-
PON1 is a lipo-lactonase which is associated with high density lipoprotein and possesses antioxidative properties
-
-
?
additional information
?
-
-
PON1 is a lipo-lactonase which is associated with high density lipoprotein and possesses antioxidative properties
-
-
?
additional information
?
-
molecular docking of substrates to wild-type and mutant enzymes using the crystal structure of PON1 (PDB ID 3SRG with resolution 2.19 A), overview. The enzyme is a paraoxonase (EC 3.1.8.1) that also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate
-
-
?
additional information
?
-
-
the enzyme exhibits a substrate preference for short-chain fatty-acid esters such as C2 or C4 with an (R)-preference
-
-
?
additional information
?
-
-
can not hydrolyze organophosphates
-
-
?
additional information
?
-
no activity with 4-nitrophenyl decanoate
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl decanoate
-
-
?
additional information
?
-
no activity with 4-nitrophenyl decanoate
-
-
?
additional information
?
-
no activity with phenyl acetate, 4-nitrophenyl-decanoate or 3-phenyl acetate
-
-
?
additional information
?
-
-
no activity with phenyl acetate, 4-nitrophenyl-decanoate or 3-phenyl acetate
-
-
?
additional information
?
-
no activity with phenyl acetate, 4-nitrophenyl-decanoate or 3-phenyl acetate
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl caprylate and diclofop methyl
-
?
additional information
?
-
the enzyme has no activity towards 4-nitrophenyl esters with acyl chains longer than C8 like 4-nitrophenyl caprylate, 4-nitrophenyl caprate, 4-nitrophenyl palmitate, as well as 4-nitrophenyl phosphate and methyl parathion
-
-
?
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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
-
-
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
-
0.5 mM inhibits by ca. 19%. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 91% inactivation
butylated hydroxytoluene
-
-
CdCl2
-
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
-
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
-
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
-
iodoacetic acid
slight inhibition
lanthanum(III) chloride
-
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
-
decreases specific activity in a concentration-dependent manner
metrifonate
-
50% inhibition at 0.00048 mM, pralidoxime protects
N-ethylmaleimide
-
leads to 24fold reduced enzyme activity at 0.2 mM
organophosphorous compounds
inhibit the enzyme of all genotypes slightly after in vivo exposure
-
phenylmethylsulfonyl fluoride
piperonyl butoxide
-
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
-
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
-
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
-
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
-
inhibits recombinant paraoxonase 1 lactonase or arylesterase activities by up to 20% or 42%, respectively
-
2-hydroxyquinoline
-
70% inhibition
2-hydroxyquinoline
-
specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
-
dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
2-hydroxyquinoline
-
specific inhibitor
2-hydroxyquinoline
-
specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
-
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
-
complete inhibition at 0.2 mM
4-chloromercuribenzoate
-
Ca2+
-
-
Ca2+
88.5% residual activity at 5 mM
Co2+
-
-
Co2+
92.6% residual activity at 5 mM
Cu2+
-
-
Cu2+
-
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+
-
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
-
diisopropyl fluorophosphate
-
diisopropylfluorophosphate
-
competitive inhibition
diisopropylfluorophosphate
-
diisopropylfluorophosphate
complete inactivation at 5 mM diisopropylfluorophosphate, after 30 min at 30°C
EDTA
-
-
EDTA
-
1 mM, completely and irreversibly inhibits activity with phenyl acetate
EDTA
complete inhibition of phenyl acetate hydrolyzing activity
EDTA
-
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
-
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+
-
-
Fe2+
-
ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 51% inactivation after 30 min
Hg2+
-
-
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+
-
-
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+
-
-
Mn2+
85.4% residual activity at 5 mM
NaCl
-
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
-
-
p-chloromercuribenzoate
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
paraoxon
0.5 mM, complete loss of activity
paraoxon
-
mixed type inhibition
Pb2+
-
-
Pb2+
45.7% residual activity at 5 mM
pepstatin A
-
phenyl acetate
-
-
phenyl acetate
-
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
-
-
phenylmethylsulfonyl fluoride
complete inhibition at 5 mM
PMSF
1 mM
SDS
-
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
-
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
-
not: Cd2+
-
additional information
-
-
-
additional information
-
no inhibition by diisopropyl fluorophosphate and sodium fluoride
-
additional information
-
the enzyme is sensitive to oxidative stress
-
additional information
0.2 mM dimyristoylphosphatidylethanol inhibits paraoxonase activity but has no effect on arylesterase activity
-
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
-
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
-
additional information
high plasma C-reactive protein is related to low paraoxonase-I activity
-
additional information
-
1 mM 3-morpholinosydnoimine, 0.002 mM Fe2+ or 0.01 mM Mn2+, Co2+, Zn2+ cause no significant loss of activity
-
additional information
-
crystalline particles Min-U-Sil 5 reduce activity due to decreased protein concentrations
-
additional information
-
not inhibited by diclofenac sodium
-
additional information
no inhibition by EDTA and iodoacetic acid
-
additional information
infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
-
additional information
-
infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
-
additional information
-
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
-
additional information
addition of glycerin has no effect on the enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-dilauroyl-phosphatidylcholine
-
stimulation
1-palmitoyl-2-arachidonoylphosphatidylcholine
stimulates arylesterase activity
1-palmitoyl-2-linoleoylphosphatidylcholine
stimulates arylesterase activity
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
the enzyme is activated by 87% by incubation with 1% (w/v) 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, at 30°C
aspirin
induces enzyme expression in the liver and stimulates enzymatic activity in blood plasma
cyclophosphamide
22% increase in the activity of PON1 in the liver and 23% increase in PON1 activity in the serum is observed 24 h after treatment with a single dose of 150 mg/kg cyclophosphamide
cysteine
1 mM, 117% of initial activity
di-oleoyl phosphatidylcholine
2.6 mM di-oleoyl phosphatidylcholine stimulates arylesterase activity of PON1 3.5fold
didecanoylphosphatidylcholine
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
dilauroyl phosphatidylcholine
dilauroylphosphatidylcholine
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
dilinoleoylphosphatidylcholine
stimulates arylesterase activity
dimethyl sulfoxide
21% increase of activity at 50% (v/v) dimethyl sulfoxide, at 30°C
dimyristoyl phosphatidylcholine
dimyristoylphosphatidylcholine
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
dimyristoylphosphatidylglycerol
activates the arylesterase activity and inhibits paraoxonase activity
dioleoyl phosphatidylcholine
dipalmitoylphosphatidylcholine
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
high-density lipoprotein
paraoxonase and arylesterase activities are stimulated by high-density lipoprotein by 2-5fold, almost independently of the apoliporotein content
-
Lubrol
the enzyme is activated by 14% by incubation with 1% Lubrol, at 30°C
-
lysophosphatidylinositol
0.01 mM, 10% stimulation of arylesterase activity
Mg2+
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activity
Mn2+
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activity
monooleoyl-lysophosphatidylserine
0.01 mM, 8% stimulation of arylesterase activity
Nonidet P-40
8.2% activation at 5% (v/v)
palmitoyl-lysophosphatidylglycerol
0.01 mM, 47% stimulation of arylesterase activity
paraoxon
115 increase of activita in the presence of 0.5 mM paraoxon, after 30 min at 30°C
phosphatidylcholine
-
purified A or B-type esterases are stimulated
phosphatidylinositol
enhances arylesterase activity, but slightly decreases paraoxonase activity
phosphatidylsenine
-
stimulates
-
pyridoxal 5'-phosphate
110% activity in the presence of 5 mM pyridoxal 5'-phosphate, after 30 min at 30°C
salicylic acid
induces enzyme expression in the liver and stimulates enzymatic activity in blood plasma
sphingomyelin
-
stimulates
Tween 40
16.4% activation at 5% (v/v)
dilauroyl phosphatidylcholine
-
stimulates
dilauroyl phosphatidylcholine
stimulates activity of enzyme variants Q192 and R192
dimyristoyl phosphatidylcholine
-
stimulates
dimyristoyl phosphatidylcholine
-
stimulates
dioleoyl phosphatidylcholine
-
stimulates
dioleoyl phosphatidylcholine
-
stimulation
dioleoyl phosphatidylcholine
-
stimulates
ethanol
4%, 150% of initial activity, 12%, 120% of intial activity
ethanol
15% increase of activity at 50% (v/v) ethanol, at 30°C
lecithin
-
stimulates
lysolecithin
-
stimulates
lysolecithin
-
stimulation
lysolecithin
-
stimulates
NaCl
-
-
NaCl
maximal activity at 35°C at 15%
NaCl
optimal concentration is 3.5% at 35°C
phosphate
-
preserves activity with considerable fluctuations, modulates oligomeric state
phosphatidylethanolamine
-
stimulates
phosphatidylethanolamine
-
stimulation
phosphatidylethanolamine
-
stimulates
phosphatidylglycerol
-
stimulation
phosphatidylglycerol
-
stimulates
Triton X-100
1 mM, 122% of initial activity
Triton X-100
11.2% activation at 5% (v/v)
Tween 20
1 mM, 116% of initial activity
Tween 20
the enzyme is activated by 67% by incubation for 60 min with 1% (v/v) Tween 20 at 30°C
Tween 20
4.8% activation at 5% (v/v)
Tween 80
1 mM, 115% of initial activity
Tween 80
19.6% activation at 5% (v/v)
additional information
arylesterase activity is independently correlated with high density lipoprotein cholesterol and lipid hydroperoxide levels
-
additional information
-
arylesterase activity is independently correlated with high density lipoprotein cholesterol and lipid hydroperoxide levels
-
additional information
pomegranate juice and pomegranate polyphenol extract (from variety Wonderful) consumption contributes to PON1 stabilization, increased association with high density lipoprotein, and enhanced catalytic activity
-
additional information
-
pomegranate juice and pomegranate polyphenol extract (from variety Wonderful) consumption contributes to PON1 stabilization, increased association with high density lipoprotein, and enhanced catalytic activity
-
additional information
-
after anti-tumour necrosis factor therapy, arylesterase significantly increases after 2 weeks from the first infusion and also remains high after 6 months
-
additional information
-
binding of human phosphate binding protein amends the size of the oligomeric states and exerts a stabilizing effect on the activity
-
additional information
serum arylesterase activity is positively correlated with serum total cholesterol and low density lipoprotein and very low density lipoprotein-cholesterol concentrations
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.039 - 0.041
1-naphthyl acetate
0.369
1-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
5
1-phenylvinyl acetate
-
19
2,2,2-trifluoroethyl acetate
-
24.8
2,2-difluoroethyl acetate
-
1.19
2,3-difluorophenyl acetate
-
2.23
2,4-difluorophenyl acetate
-
2
2,6-difluorophenyl acetate
-
54
2-fluoroethyl acetate
-
1.5
2-fluorophenyl acetate
-
0.0079 - 0.65
2-naphthyl acetate
0.0128
2-naphthyl butanoate
pH 7.0, 25°
0.1
2-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
2.1
3,4-dimethyl phenyl acetate
-
1.9
3-cyanophenyl acetate
-
1.4
3-fluorophenyl acetate
-
0.0052
3-naphthyl acetate
pH 7.0, 25°
0.0088
3-naphthyl butanoate
pH 7.0, 25°
2.2
3-nitrophenyl acetate
-
2
4-acetoxy methyl benzoate
-
2.6
4-acetoxyacetophenone
-
2.3
4-acetoxybenzaldehyde
1
4-chlorophenyl acetate
-
4.1
4-methoxy phenyl acetate
-
0.000043 - 8.19
4-nitrophenyl acetate
0.174 - 0.38
4-nitrophenyl butanoate
0.072 - 0.224
4-nitrophenyl butyrate
0.081
4-nitrophenyl caprate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.031
4-nitrophenyl caproate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.028
4-nitrophenyl caprylate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.084
4-nitrophenyl decanoate
EstB, pH 7.5, 30°C
0.029
4-nitrophenyl hexanoate
EstB, pH 7.5, 30°C
0.122
4-nitrophenyl laurate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.23
4-nitrophenyl octanoate
EstB, pH 7.5, 30°C
0.276
4-nitrophenyl palmitate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.063
4-nitrophenyl pentanoate
EstB, pH 7.5, 30°C
0.234
4-nitrophenyl phosphate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
1.4
4-nitrophenyl propionate
EstB, pH 7.5, 30°C
74.6 - 98.7
7-aminocephalosporanic acid
0.029 - 0.19
Alpha-naphthyl acetate
2.1
beta-naphthyl acetate
-
-
119 - 174.7
cephalosporin C
3.2
ethyl hexanoate
EstB, pH 7.5, 30°C
1.6
ketoprofen ethyl ester
-
at pH 8.0
0.043 - 0.29
p-nitrophenyl acetate
1.42
paraoxon
pH 7.4, 25°C
5.5
phenylthioacetate
EstB, pH 7.5, 30°C
7.1 - 7.2
S-methyl thiobutanoate
additional information
9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate
0.039
1-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.041
1-naphthyl acetate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.0079
2-naphthyl acetate
pH 7.0, 25°
0.014
2-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.16
2-naphthyl acetate
pH 8.0, recombinant genetic variant G1A7
0.18
2-naphthyl acetate
pH 8.0, recombinant genetic variant G1B11
0.211
2-naphthyl acetate
pH 8.0
0.26
2-naphthyl acetate
pH 8.0, recombinant genetic variant G2C2
0.5
2-naphthyl acetate
pH 8.0
0.65
2-naphthyl acetate
pH 8.0, recombinant genetic variant G3G3
2.3
4-acetoxybenzaldehyde
-
2.3
4-acetoxybenzaldehyde
recombinant enzyme
0.000043
4-nitrophenyl acetate
-
37°C, pH 7.6
0.0174
4-nitrophenyl acetate
pH 7.0, 25°
0.094
4-nitrophenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.124
4-nitrophenyl acetate
pH 8.0, 25°C
0.289
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.336
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.611
4-nitrophenyl acetate
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.96
4-nitrophenyl acetate
in 50 mM Tris-HCl (pH 8.0), at 37°C
1.5
4-nitrophenyl acetate
-
1.9
4-nitrophenyl acetate
EstB, pH 7.5, 30°C
2.11
4-nitrophenyl acetate
pH 8.3, 25°C
4.2
4-nitrophenyl acetate
-
pH 7.2, 37°C
8.19
4-nitrophenyl acetate
pH 6.5, 50°C
0.174
4-nitrophenyl butanoate
pH 7.0, 25°
0.38
4-nitrophenyl butanoate
EstB, pH 7.5, 30°C
0.072
4-nitrophenyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.224
4-nitrophenyl butyrate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
74.6
7-aminocephalosporanic acid
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
98.7
7-aminocephalosporanic acid
-
free enzyme, at pH 8.0 and 30°C
0.029
Alpha-naphthyl acetate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.19
Alpha-naphthyl acetate
-
-
119
cephalosporin C
-
free enzyme, at pH 8.0 and 30°C
174.7
cephalosporin C
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
0.043
p-nitrophenyl acetate
-
-
0.29
p-nitrophenyl acetate
-
-
0.01
phenyl acetate
pH 7.0, 25°
0.014
phenyl acetate
wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C
0.017
phenyl acetate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.069
phenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.201
phenyl acetate
wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C
0.265
phenyl acetate
-
pH 7.4, 37°C, type B paraoxonase
0.265
phenyl acetate
-
pH 8.0, 25°C, enzyme from phenotype B blood plasma
0.27
phenyl acetate
enzyme variant R192
0.4
phenyl acetate
-
enzyme of breed Holstein, pH 8.0, 25°C
0.46
phenyl acetate
wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C
0.5
phenyl acetate
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
0.5
phenyl acetate
-
enzyme of breed Montofon, pH 8.0, 25°C
0.51
phenyl acetate
mutant E313A, pH 8.0, 25°C
0.53
phenyl acetate
in 50 mM Tris-HCl (pH 8.0), at 37°C
0.59
phenyl acetate
mutant N133S, pH 8.0, 25°C
0.61
phenyl acetate
wild-type, pH 8.0, 25°C
0.61
phenyl acetate
pH 8.0, 25°C, wild-type enzyme
0.64
phenyl acetate
mutant G11S, pH 8.0, 25°C
0.64
phenyl acetate
wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C
0.67
phenyl acetate
mutant E314A, pH 8.0, 25°C
0.68
phenyl acetate
-
pH 8.0, 10°C
0.688
phenyl acetate
-
pH 7.4, 37°C, type A paraoxonase
0.688
phenyl acetate
-
pH 8.0, 25°C, enzyme from phenotype A blood plasma
0.7
phenyl acetate
enzyme variant Q192
0.74
phenyl acetate
mutant G11A or mutant G11C, pH 8.0, 25°C
0.74
phenyl acetate
-
2 mM substrate, at pH 8.0 and 37°C
0.8
phenyl acetate
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
0.8
phenyl acetate
-
enzyme of breed Swiss Black, pH 8.0, 25°C
0.81
phenyl acetate
pH 8.0, 25°C, mutant enzyme F222Y
0.86
phenyl acetate
wild type enzyme, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C
0.89
phenyl acetate
mutant F222Y, pH 8.0, 25°C
0.89
phenyl acetate
mutant enzyme Q192R, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C
0.92
phenyl acetate
-
isozyme 192R, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
0.957
phenyl acetate
recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2
0.97
phenyl acetate
-
pH 8.0, 15°C
0.98
phenyl acetate
-
isozyme 192Q, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
1 - 2.1
phenyl acetate
-
-
1.05
phenyl acetate
-
pH 8.0, 20°C
1.2
phenyl acetate
recombinant enzyme
1.3
phenyl acetate
pH 8.0, wild-type enzyme
1.33
phenyl acetate
-
pH 8.0, 25°C
1.6
phenyl acetate
pH 8.3, activity buffer with 0.1% tergitol
1.8
phenyl acetate
-
pH 8.0, 30°C
2.07
phenyl acetate
-
pH 8.0, 35°C
2.1
phenyl acetate
wild-type, pH 8.0, 25°C
2.1
phenyl acetate
pH 8.0, temperature not specified in the publication
2.6
phenyl acetate
pH 8.3, activity buffer
3.03
phenyl acetate
-
pH 8.0, 40°C
3.6
phenyl acetate
pH 8.0, mutant enzyme H134Q
3.7
phenyl acetate
-
pH 8.0, wild-type enzyme
3.8
phenyl acetate
-
pH 8.0, recombinant enzyme
4.1
phenyl acetate
mutant H115W/R192K, pH 8.0, 25°C
7.46
phenyl acetate
pH 8.0, 37°C
7.47
phenyl acetate
pH 8.0, 37°C
8.1
phenyl acetate
pH 8.0, mutant enzyme H115Q
8.18
phenyl acetate
pH 8.3, 25°C
9.7
phenyl acetate
pH 8.0, mutant enzyme H115Q/H134Q
10.8
phenyl acetate
mutant H115W, pH 8.0, 25°C
16
phenyl acetate
EstB, pH 7.5, 30°C
7.1
S-methyl thiobutanoate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
7.2
S-methyl thiobutanoate
pH 8.0, 25°
additional information
9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate
-
Km value of a serum sample is 85 nM, pH 8.0, 25°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km-values in serum samples
-
additional information
additional information
-
all kinetic parameters increase with temperature, but the ratios kcat/Km and Kp/Km remain practically constant
-
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0.00014
-
partially purified enzyme, substrate diclofop methyl
0.00024
-
partially purified enzyme, substrate binapacryl
0.00031
-
partially purified enzyme, substrate binapacryl, population Rothamsted
0.00043
-
partially purified enzyme, substrate binapacryl, population Peldon
0.00049
-
partially purified enzyme, substrate binapacryl
0.00066
-
partially purified enzyme, substrate diclofop methyl
0.0048
-
partially purified enzyme, substrate bromoxynil octanoate, population Peldon
0.0056
-
partially purified enzyme, substrate bromoxynil octanoate
0.006
-
purified enzyme, substrate binapacryl
0.0061
-
partially purified enzyme, substrate bromoxynil octanoate, population Rothamsted
0.007
-
partially purified enzyme, substrate bromoxynil octanoate
0.03
-
partially purified enzyme, substrate 4-nitrophenyl acetate
0.04
-
partially purified enzyme, substrate 4-nitrophenyl acetate
0.08
-
partially purified enzyme, substrate 4-nitrophenyl acetate
0.086
pH 8.0, 25°C, substrate: phenyl acetate, purified recombinant enzyme
0.19
-
purified enzyme, substrate bromoxynil octanoate
0.7
pH 8.0, 25°C, substrate: 4-nitrophenyl acetate, purified recombinant enzyme
0.96
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
1.22
-
isozyme 192Q, crude enzyme, using phenyl acetate as substrate, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
1.3
pH 8.0, 25°C, substrate: 4-nitrophenyl butyrate, purified recombinant enzyme
1.34
-
isozyme 192R, crude enzyme, using phenyl acetate as substrate, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
1.4
pH 8.0, 25°C, substrate: 4-nitrophenyl butyrate, purified recombinant enzyme
1048
-
isozyme 192R, after 783fold purification, using phenyl acetate as substrate, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
11.4
pH 8.0, 25°C, substrate: 4-nitrophenyl butyrate, purified recombinant enzyme
1120
pH 8.0, 25°C, substrate: phenyl acetate, purified recombinant enzyme
13.6
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
159.2
-
purified enzyme, substrate beta-naphthyl acetate
170.7
-
purified enzyme, substrate alpha-naphthyl acetate
20.7
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
35
-
recombinant Sm23, with 4-nitrophenyl acetate as substrate
39
pH 8.0, 25°C, substrate: 4-nitrophenyl acetate, purified recombinant enzyme
4.1
pH 8.0, 25°C, substrate: phenyl acetate, purified recombinant enzyme
4.18
-
purified enzyme, substrate 4-nitrophenyl butyrate
465
recombinant enzyme after 90fold purification
486 - 519
purified recombinant wild-type enzyme, substrate phenyl acetate
5.15
recombinant enzyme from crude cell extract
558
-
purified enzyme from phenotype A blood plasma
5580
recombinant enzyme after 858.5fold purification, using phenyl acetate as substrate, at 60°C and pH 7.0
6.5
recombinant enzyme from crude cell extract, using phenyl acetate as substrate, at 60°C and pH 7.0
623
purified recombinant wild-type enzyme, substrate phenyl acetate in presence of 3.5% NaCl
77.9
-
purified enzyme, substrate 4-nitrophenyl acetate
8.5
-
recombinant enzyme, after purification, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
85.05
-
using phenyl acetate as substrate (arylesterase activity of PON1), at 25°C
882
-
purified enzyme from phenotype A blood plasma
970
-
isozyme 192Q, after 795fold purification, using phenyl acetate as substrate, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
15
-
15
pH 8.0, 25°C, substrate: 4-nitrophenyl acetate, purified recombinant enzyme
3.5
-
enzyme purified from serum, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
3.5
-
enzyme purified from serum, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
additional information
-
assay developemnt
additional information
-
activity of different genotypes after exposure to high or low organophosphorous compound levels, overview
additional information
activity of different genotypes after exposure to high or low organophosphorous compound levels, overview
additional information
substrate specificity
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C284A
mutant with 44fold reduced paraoxonase activity
C284D
no enzymic activity
D183N
the mutant disfavors paraoxon binding due to its charged nature and possible electrostatic repulsion with the phosphate group of paraoxon
D269E
no enzymic activity
E313A
slightly decreased activity
E314A
enzymic activity similar to wild-type
G11A
slightly enhanced activity with phenyl acetate and paraoxon
G11C
slightly enhanced activity with phenyl acetate and paraoxon
G11S
slightly enhanced activity with phenyl acetate and paraoxon
H115A
activity with phenyl acetate is 0.3% compared to wild-type activity, activity with 2-naphthyl acetate is 0.3% of wild-type activity
H115Q
activity with phenyl acetate is 0.6% compared to wild-type activity, activity with 2-naphthyl acetate is 1% of wild-type activity
H115W/R192K
partially restores the phenyl acetate-hydrolyzing activity of mutant H115W
H115W/R192Q
complete loss of phenyl acetate-hydrolyzing activity
H134Q
activity with phenyl acetate is 9.9% compared to wild-type activity, activity with 2-naphthyl acetate is 3.1% of wild-type activity
H134W
no enzymic activity
H134Y
no enzymic activity
H184Q
activity with phenyl acetate is 32% compared to wild-type activity, activity with 2-naphthyl acetate is 66% of wild-type activity
H184T
activity with phenyl acetate is 27% compared to wild-type activity, activity with 2-naphthyl acetate is 35% of wild-type activity
H285D
no enzymic activity
H285Q
activity with phenyl acetate is 12% compared to wild-type activity, activity with 2-naphthyl acetate is 19% of wild-type activity
H285S
activity with phenyl acetate is 10% compared to wild-type activity, activity with 2-naphthyl acetate is 61% of wild-type activity
H285Y
no enzymic activity
L69G/S111T/H115W/H134R/R192K/F222S/T332S
mutant designed for expression in Escherichia coli in soluble and active form. Mutant shows about 45% of phenyl acetate hydrolyzing activity of wild-type
L69V
the mutant shows a 4-16fold increase in enzyme activity compared to the wild type enzyme
L69V/V369A
the mutant shows increased paraoxon binding affinity compared to the wild type enzyme
N133S
enzymic activity similar to wild-type
N168E
no enzymic activity
N224A
no enzymic activity
S193P
the mutation increases phosphotriesterase activity of enzyme
V304A
no enzymic activity
V346A
the mutant shows a 4-16fold increase in enzyme activity compared to the wild type enzyme
C105A
site-directed mutagenesis, 55.9% of the wild-type activity with substrate 4-nitrophenyl butyrate
H137A
site-directed mutagenesis, 17.4% of the wild-type activity with substrate 4-nitrophenyl butyrate
H164A
site-directed mutagenesis, inactive mutant
H56A
site-directed mutagenesis, 30.0% of the wild-type activity with substrate 4-nitrophenyl butyrate
S10A
site-directed mutagenesis, inactive mutant
S112A
site-directed mutagenesis, 99.5% of the wild-type activity with substrate 4-nitrophenyl butyrate
S138G
site-directed mutagenesis, 99.2% of the wild-type activity with substrate 4-nitrophenyl butyrate
S155A
site-directed mutagenesis, 99.0% of the wild-type activity with substrate 4-nitrophenyl butyrate
S42A
site-directed mutagenesis, 33.2% of the wild-type activity with substrate 4-nitrophenyl butyrate
S44A
site-directed mutagenesis, 33.7% of the wild-type activity with substrate 4-nitrophenyl butyrate
C105A
-
site-directed mutagenesis, 55.9% of the wild-type activity with substrate 4-nitrophenyl butyrate
-
H56A
-
site-directed mutagenesis, 30.0% of the wild-type activity with substrate 4-nitrophenyl butyrate
-
S10A
-
site-directed mutagenesis, inactive mutant
-
S112A
-
site-directed mutagenesis, 99.5% of the wild-type activity with substrate 4-nitrophenyl butyrate
-
S42A
-
site-directed mutagenesis, 33.2% of the wild-type activity with substrate 4-nitrophenyl butyrate
-
H115W/T332/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
H115W/T332S
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
H115W/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
I74F/H115W
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/H115W/T332
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/H115W/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/T332S
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
I74F/V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
T332S
site-directed mutagenesis, the mutant shows 2fold increased activity with phenylacetate compared to wild-type
T332S/V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
C105S
mutant shows 24.0% activity compared to the wild type enzyme
C107S
mutant shows 30.8% activity compared to the wild type enzyme
C129S
mutant shows 3.6% activity compared to the wild type enzyme
D251N
mutant shows 0.6% activity compared to the wild type enzyme
H281N
mutant shows 19.4% activity compared to the wild type enzyme
S156A
mutant shows 0.012% activity compared to the wild type enzyme
C105S
-
mutant shows 24.0% activity compared to the wild type enzyme
-
C107S
-
mutant shows 30.8% activity compared to the wild type enzyme
-
C129S
-
mutant shows 3.6% activity compared to the wild type enzyme
-
D251N
-
mutant shows 0.6% activity compared to the wild type enzyme
-
S156A
-
mutant shows 0.012% activity compared to the wild type enzyme
-
S10A
-
completely loses activity
E14K
Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
E14K/Y34Q
Tm-value for the mutant enzyme is 4°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
Y34Q
Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
E14K
-
Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
-
E14K/Y34Q
-
Tm-value for the mutant enzyme is 4°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
-
Y34Q
-
Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
-
F222D
no enzymic activity
F222D
the mutation abolishes both esterase and enzyme activity of PON1
F222Y
hydrolysis of phenyl acetate, but not of paraoxon
F222Y
increased activity with phenyl acetate, no activity with paraoxon
F222Y
the mutation abolishes the PON activity of enzyme but retains the esterase activity with a 1.5fold increase in KM for phenyl acetate
H115W
no enzymic activity with phenyl acetate, increased activity with paraoxon
H115W
no hydrolysis of phenyl acetate, but hydrolysis of paraoxon. Phenyl acetate can act as an inhibitor
H115W
activity with phenyl acetate is 0.06% compared to wild-type activity, activity with 2-naphthyl acetate is 0.3% of wild-type activity
H115W
the mutant shows a 2fold increase in enzyme activity compared to the wild type enzyme
H115W
mutation results in decrease in the affinity and the rate of catalysis of the enzyme
H115W/N133S
no enzymic activity with phenyl acetate, slightly decreased activity with paraoxon
H115W/N133S
no hydrolysis of phenyl acetate, but hydrolysis of paraoxon
L55M
naturally occuring polymorphism, allele frequency in relation to exposure of individuals to organophosphates, overview
L55M
naturally occuring polymorphism, the paraoxonase activity of the enzyme is altered
L55M
the polymorphism accounts for 73% of PON1 activity
Q192R
naturally occuring polymorphism, allele frequency in relation to exposure of individuals to organophosphates, overview
Q192R
naturally occuring polymorphism, the paraoxonase activity of the enzyme is altered
Q192R
a naturally occuring polymorphism, 192QQ, 192RR or 192QR, that reduces PON1 activity and increases the risk of ischemic stroke, genotyping and phenotyping, allele frequency, the paraoxonase/arylesterase activity ratio is unaltered
Q192R
paraoxon is less efficiently hydrolysed compared to the wild type enzyme
Q192R
the mutant shows lower Vmax and kcat/Km values for soman and sarin than the wild type enzyme
Q192R
the mutation is associated with sporadic amyotrophic lateral sclerosis
Q192R
the polymorphism accounts for 69% of PON1 activity, the 192RR genotype carriers have the highest PON1 activity, whereas the the 192QQ genotype carriers have the lowest activity, with the heterozygote 192Q/R having intermediate activity
Q192R
-
the mutation is related to vascular disease and variation in the enzyme activity
R192Q
a naturally occuring polymorphism, 192QQ, 192RR or 192QR, that reduces PON1 activity and increases the risk of ischemic stroke, genotyping and phenotyping, allele frequency, the paraoxonase/arylesterase activity ratio is unaltered
R192Q
the polymorphic residue R192Q interacts with the leaving group of paraoxon, suggesting it plays an important role in the proper positioning of this substrate in the active site
additional information
the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus
additional information
-
the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus
additional information
-
mutant rePON1-G2E6, 91% identity with wild-type and several variations deriving from human, mouse or rat wild-type enzyme, crystal structure
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drug development
-
resistance of strains to permethrin is associated with elevated levels of enzyme
analysis
-
description of an easy and non-toxic method for large scale phenotyping and activity quantitation of arylesterase
analysis
-
the enzyme has the potential to be used as a catalytic bioscavenger of nerve agents. Insect production of the enzyme may provide a source for both in vitro enzymatic and crystallographic studies and in vivo stability and anti-nerve agent efficacy testing
analysis
-
quantification of arylesterase activity in routine clinical studies by monitoring the formation of acetic acid, upon the hydrolysis of phenyl acetate, using 10 microl of sample. The method accuracy is higher than 90% and intra-assay and inter-assay precisions are 96% and 95%, respectively. The procedure is suitable for use in human serum and heparinized plasma samples, while ethylenediaminetetra-acetic acid containing samples should be avoided
analysis
-
use of 9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate as a substrate for serum PON arylesterase activity assay. The apparent Km value of a serum sample for the substrate is 85 nmol/l, close to the Km value of recombinant human isoform PON1. Recombinant human PON1 in presence of CaCl2 shows at least 7.8 times selectivity over acetylcholinesterase and lipases. The method allows reliable, cost-saving, and specific determination in a buffer of physiological pH
medicine
aryl esterase activitiy correlates positively with total antioxidant status, high density lipoprotein and apolipoprotein A-I
medicine
-
baseline and stimulated ARE activity is significantly lower in patients with chronic liver disease than in controls, serum ARE activity can be a suitable biomarker for the evaluation of the presence and severity of chronic liver damage
medicine
-
both PON1 bioavailability and catalytic activity are decreased in children with autism spectrum disorders
medicine
diminished paraoxonase and arylesterase activity is associated with particular stage, grade and CA-125 level of ovarian cancer
medicine
-
enzyme activity is reduced in subjects with type 1 and type 2 diabetes, the enzyme is associated with proteinuria in subjects with type 2 diabetes mellitus, there is an independent inverse association of enzyme mass with cystatin C Aboriginal subjects with type 2 diabetes
medicine
low paraoxonase-I activity in type 2 diabetes mellitus may contribute to increased cardiovascular risk via an effect on enhanced systemic low-grade inflammation
medicine
PON1 activity is lower in chronic hepatitis patients compared with the control subjects
medicine
PON1 moderately indicates cancer presence and regional metastasis, PON1 activity decreases in gastroesophageal cancers and corresponds to inflammation severity and cancer-related anemia, PON1's arylesterase activity reflects anemia severity, being correlated with hemoglobin, hematocrit, and iron
medicine
PON1 overexpression is associated with decreased diabetes-induced macrophage oxidative stress, decreased diabetes development, and decreased mortality
medicine
the arylesterase activity of PON1 is affected by critical ischemia of the lower limbs
medicine
-
biologic monitoring for AREase status among pesticide handlers may be warranted to identify individuals who are at particularly high risk of organophosphate-related health effect
medicine
-
serum ARE activity may be a suitable biomarker for identifying the presence and severity of chronic liver injury
medicine
-
paraoxonase 1 significantly protects against sarin and soman exposure in guinea pigs and supports the development of paraoxonase 1 as a catalytic bioscavenger for protection against lethal exposure of chemical warfare nerve agents exposure
medicine
-
paraoxonase 1 significantly protects against sarin and soman exposure in guinea pigs and supports the development of paraoxonase 1 as a catalytic bioscavenger for protection against lethal exposure of chemical warfare nerve agents exposure
medicine
-
the lower enzyme activity in metabolic syndrome are considered an independent risk factor for cardiovascular disease
medicine
-
ethanol consumption causes a significant decrease in liver paraoxonase activity. Gallic acid treatment partly restores this decreased paraoxonase activity. A gallic acid dose of 100 mg/kg shows highest restoring effect for paraoxonase activity. The activity of arylesterase is decreased in the ethanol group, but this decrease is not significant. Gallic acid treatment restores the loss of this activity due to ethanol exposure
medicine
-
in patients with ankylosing spondylitis with active disease, levels of serum triglycerides, total cholesterol, low denstiy lipoprotein and malondialdehyde are significantly elevated while high density liporpoteon, paraoxonase PON1 and arylesterase ARE levels are lower than those with no active ankylosing spondylitis. Decrease in the PON1/ARE activity leading to generation of oxidative stress may play an important role in the pathogenesis of ankylosing spondylitis. Activity of PON1/ARE in patients with ankylosing spondylitis seems to be strictly correlated with the activity of the inflammatory process
medicine
-
in patients with idiopathic Parkinson's disease, total antioxidant status levels are significantly lower than that of controls. Total oxidant status levels are higher than those of controls. Paraoxonase PON1 and arylesterase activities of patients are lower than those of controls. Serum levels of total and low density lipid cholesterol are significantly reduced in Parkinson's disease patients
medicine
-
in patients with relapsing-remitting multiple sclerosis, total antioxidant status levels are significantly lower than that of controls. Total oxidant status levels of the patients are higher than that of controls. Paraoxonase PON1 and arylesterase activities of the patients are lower, but not significantly, than those of controls. There is no correlation between serum PON1 activity and oxidaive stress index in patients with relapsing-remitting multiple sclerosis. Endogenousantioxidants may have been exhausted by increased oxidative stress and additional antioxidant treatment might be beneficial for these patients
medicine
-
in patients with selective serotonin reuptake inhibitor intoxication, the serum total antioxidant capacity levels and the paraoxonase and arylesterase activities are significantly lower, whereas the serum malondialdehyde levels are significantly higher than in the controls, indicating that decreased paraoxonase PON1 activity and increased oxidative stress represent alternative mechanisms in selective serotonin reuptake inhibitor toxicity
medicine
-
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. Very low density lipoprotein also inhibits recombinant paraoxonase 1 lactonase or arylesterase activities by up to 20% or 42%, respectively. Bezafibrate therapy to three hypertriglyceridemic patients (400 mg/day, for one month) significantly decreased serum triglyceride concentration by 67%, and increased serum high density lipoproteincholesterol levels by 48%. Paraoxonase 1 arylesterase or paraoxonase activities in the patients' high density lipoprotein fractions after drug therapy are significantly increased by 86-88%, as compared to paraoxonase 1 activities before treatment. High density lipoprotein-paraoxonase 1 protein levels significantly increased after bezafibrate therapy
medicine
-
quantification of arylesterase activity in routine clinical studies by monitoring the formation of acetic acid, upon the hydrolysis of phenyl acetate, using 10 microl of sample. The method accuracy is higher than 90% and intra-assay and inter-assay precisions are 96% and 95%, respectively. The procedure is suitable for use in human serum and heparinized plasma samples, while ethylenediaminetetra-acetic acid containing samples should be avoided
medicine
-
serum paraoxonase and arylesterase activities are significantly lower in patients with osteomyelitis compared to control individuals. Arylesterase activity is inversely correlated with triglyceride and cholesterol concentrations
medicine
-
use of 9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate as a substrate for serum PON arylesterase activity assay. The apparent Km value of a serum sample for the substrate is 85 nmol/l, close to the Km value of recombinant human isoform PON1. Recombinant human PON1 in presence of CaCl2 shows at least 7.8 times selectivity over acetylcholinesterase and lipases. The method allows reliable, cost-saving, and specific determination in a buffer of physiological pH
medicine
-
paraoxonase-1 arylesterase activity is an independent predictor of myeloperoxidase levels in overweight patients with or without cardiovascular complications