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Information on EC 3.1.1.2 - arylesterase
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3.1.1.2 arylesteraseIUBMB Comments
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate .
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Word Map
- 3.1.1.2
- lipoprotein
- cholesterol
-
high-density
- atherosclerosis
- cardiovascular
-
low-density
- coronary
- diabetes
-
apolipoproteins
- artery
- triglyceride
-
hdl-associated
-
organophosphate
- malondialdehyde
-
organophosphorus
- mellitus
-
pesticide
-
atherogenic
- lactonase
-
anti-oxidant
- atherogenesis
-
hdl-cholesterol
- cholinesterase
- phenylacetate
- homocysteine
- apoa-i
-
c-reactive
-
antiatherogenic
-
lipoprotein-associated
- esterases
- acetylcholinesterase
-
atheroprotective
- oxons
-
ox-ldl
- carboxylesterase
- butyrylcholinesterase
- chlorpyrifos
- lp-pla2
- drug development
- soman
- clopidogrel
-
lecithin:cholesterol
-
oxidant-antioxidant
- paf-ah
-
allozyme
- thiolactone
-
acetylhydrolase
- sarin
- analysis
- parathion
- phosphotriesterase
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
(R)-specific SGNH arylesterase, A-esterase, alpha-esterase, ARE, AREase, aromatic esterase, Aryl-ester hydrolase, aryldialkylphosphatase, arylesterase, DvvII, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-esterase
alpha-esterase
AREase
aromatic esterase
-
-
-
-
Aryl-ester hydrolase
-
-
-
-
aryldialkylphosphatase
exhibits multiple enzyme activities including organophosphate esterase, carboxyl esterase, lactonase, and phospholipase A2 activity
arylesterase
ESt-A
Est0881
gox0881
K-45
-
-
-
-
paraoxonase
paraoxonase/arylesterase
PON-aryl
PON1
pyrethroid-resistance-associated esterase
Saci_2140
SacPox
SisLac
Sm23
additional information
A-esterase
-
-
-
-
arylesterase
the enzyme is a serine esterase belonging to the A-esterases and contains a catalytic triad composed of Ser156, Asp251, and His281 in the active site
arylesterase
the enzyme is a serine esterase belonging to the A-esterases and contains a catalytic triad composed of Ser156, Asp251, and His281 in the active site
-
paraoxonase
-
-
-
-
SisLac
C4KKZ9
the enzyme also shows activity of aryldialkylphosphatase (EC 3.1.8.1) and 1,4-lactonase aryldialkylphosphatase(EC 3.1.1.25)
SisLac
C4KKZ9
the enzyme also shows activity of aryldialkylphosphatase (EC 3.1.8.1) and 1,4-lactonase aryldialkylphosphatase(EC 3.1.1.25)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phenyl acetate + H2O = a phenol + acetate
-
-
-
-
a phenyl acetate + H2O = a phenol + acetate
H115 acts as general base, H134 acts in a proton shuttle mechanismto increase H115’s basicity
-
a phenyl acetate + H2O = a phenol + acetate
catalytic triad consists of S94, D222 and H251, the active site is significantly occluded
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
aryl-ester hydrolase
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [8].
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CAS REGISTRY NUMBER
COMMENTARY
9032-73-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(chloromethyl)phenyl acetate + H2O
4-chloromethyl phenol + acetate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl decanoate
4-nitrophenol + decanoate
-
low activity
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
?
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 pentanoate + H2O
4-nitrophenol + pentanoate
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
?
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-phenyloxycarbonyl)-10-methylacridinium triflate + H2O
phenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
9-(4-tert-butylphenoxycarbonyl)-10-methylacridinium triflate + H2O
4-tert-butylphenol + 10-methylacridinium trifluoromethanesulfonate
-
-
-
-
?
[(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
A0A061D1S0
-
-
-
?
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
15.4% activity compared to 4-nitrophenyl 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
-
13.5% of the activity with phenyl 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-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
-
-
-
-
?
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
-
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
C4KKZ9
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
highest catalytic efficiency (100% activity)
-
-
?
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
A0A061D1S0
-
-
-
?
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 diethylphosphate + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
?
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
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
665028, 692695, 693321, 695051, 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
-
-
664064, 664111, 664184, 665745, 678376, 678464, 679262, 679293, 679306, 679634, 681055, 681730, 690419, 691863, 691873, 692541, 692732, 693354, 693357, 695124, 695193, 729324, 730898
-
-
?
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
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
-
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
best substrate
-
?
phenyl acetate + H2O
phenol + acetate
best substrate
-
?
phenyl acetate + H2O
phenol + acetate
166% activity compared to 4-nitrophenyl acetate
-
-
?
phenylthioacetate + H2O
thiophenol + acetate
-
-
?
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
-
-
?
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
?
-
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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
?
-
-
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
?
-
-
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 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 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
?
-
-
exhibits diazoxonase, paraoxonase, and arylesterase activities
-
-
-
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 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
?
-
-
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 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
?
-
-
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
?
-
C4KKZ9
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
?
-
C4KKZ9
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
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
?
-
-
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 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 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
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Mn2+
NaCl
Ni2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Zn2+
Ca2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
Ca2+
-
is essential for activity and stability of arylesterase, modulates oligomeric state
Ca2+
-
0.9 mM, the further increase of the calcium concentration does not significantly increase arylesterase activity
Ca2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
Ca2+
-
0.9 mM, the further increase of the calcium concentration does not significantly increase arylesterase activity
Ca2+
-
is essential for activity and stability of arylesterase, modulates oligomeric state
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Cd2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Mn2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
NaCl
-
paraoxonase activity of the B type isozyme is considerably higher and stimulated more by 1 M NaCl than A-type paraoxonase
NaCl
-
B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
catalytic activity is strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-propanol
55% residual activity in the presence of 90% (v/v) 2-propanol, after 60 min at 70°C
acetonitrile
43% residual activity in the presence of 90% (v/v) acetonitrile, after 60 min at 70°C
ascorbate
-
0.5 mM inhibits by ca. 19%. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 91% inactivation
D-penicillamine
-
40.5% residual activity after 24 h in the presence of 0.2 mg/ml D-penicillamine
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 0.1–0.4 mM, with a greater inhibition of arylesterase activity
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
-
methanol
48% residual activity in the presence of 90% (v/v) methanol, after 60 min at 70°C
organophosphorous compounds
-
inhibit the enzyme of all genotypes slightly after in vivo exposure
-
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
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 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
-
specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
-
dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
2-hydroxyquinoline
-
specific paraoxonase 1 inhibitor, dose-dependent inhibition
2-hydroxyquinoline
-
dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
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
diethyl dicarbonate
6% residual activity in the presence of 5 mM diethyl dicarbonate, after 30 min at 30°C
diisopropylfluorophosphate
complete inactivation at 5 mM diisopropylfluorophosphate, after 30 min at 30°C
EDTA
92% residual activity in the presence of 10 mM EDTA, after 30 min at 75°C
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+
-
ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 51% inactivation after 30 min
Hg2+
complete inactivation at 5 mM Hg2+, after 30 min at 30°C
Mg2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
NaCl
76% residual activity in the presence of 2 M NaCl, after 60 min at 70°C
p-chloromercuribenzoate
23% residual activity in the presence of 5 mM p-chloromercuribenzoate, after 30 min at 30°C
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
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
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
Zn2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
additional information
-
no inhibition by diisopropyl fluorophosphate and sodium fluoride
-
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
-
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
no inhibition by EDTA and iodoacetic acid
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-palmitoyl-2-arachidonoylphosphatidylcholine
-
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
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
dilauroylphosphatidylcholine
-
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
dimethyl sulfoxide
21% increase of activity at 50% (v/v) dimethyl sulfoxide, at 30°C
dimyristoylphosphatidylcholine
-
stimulation of arylesterase activity is greater than stimulation of paraoxonase activity
dimyristoylphosphatidylglycerol
-
activates the arylesterase activity and inhibits paraoxonase activity
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
-
Mg2+
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
Mn2+
-
Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activty
monooleoyl-lysophosphatidylserine
-
0.01 mM, 8% stimulation of arylesterase activity
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
phosphatidylinositol
-
enhances arylesterase activity, but slightly decreases paraoxonase activity
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
dilauroyl phosphatidylcholine
stimulates activity of enzyme variants Q192 and R192
ethanol
4%, 150% of initial activity, 12%, 120% of intial activity
ethanol
15% increase of activity at 50% (v/v) ethanol, at 30°C
phosphate
-
preserves activity with considerable fluctuations, modulates oligomeric state
Tween 20
the enzyme is activated by 67% by incubation for 60 min with 1% (v/v) Tween 20 at 30°C
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
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.369
1-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.1
2-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
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
0.122
4-nitrophenyl laurate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.276
4-nitrophenyl palmitate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.234
4-nitrophenyl phosphate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.039
1-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.014
2-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
0.094
4-nitrophenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 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
0.072
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
0.029
Alpha-naphthyl acetate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
174.7
cephalosporin C
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
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
0.46
phenyl acetate
-
wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C
0.64
phenyl acetate
-
wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C
0.8
phenyl acetate
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
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 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
0.98
phenyl acetate
-
isozyme 192Q, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
7.1
S-methyl thiobutanoate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
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
-
all kinetic parameters increase with temperature, but the ratios kcat/Km and Kp/Km remain practically constant
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
1-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
9.8
1-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
22.7
2-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
341
4-nitrophenyl caprate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
467
4-nitrophenyl caproate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
410
4-nitrophenyl caprylate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
264
4-nitrophenyl laurate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
265
4-nitrophenyl palmitate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
269
4-nitrophenyl phosphate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
450
Alpha-naphthyl acetate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
additional information
additional information
-
all kinetic parameters increase with temperature, but the ratios kcat/Km and Kp/Km remain practically constant
-
15.2
2-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
25.7
4-nitrophenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
1300
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
2500
4-nitrophenyl acetate
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
2500
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
17.6
4-nitrophenyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
285
4-nitrophenyl butyrate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
69.5
7-aminocephalosporanic acid
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
20.81
cephalosporin C
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
102
phenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
521
phenyl acetate
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
685
phenyl acetate
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
9.3
S-methyl thiobutanoate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
1-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
220
2-naphthyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
240
4-nitrophenyl butyrate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
110
1-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
1100
2-naphthyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
270
4-nitrophenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
4200
4-nitrophenyl acetate
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
4700
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
7500
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.9
7-aminocephalosporanic acid
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
0.1
cephalosporin C
-
immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C
0.000133
phenyl acetate
-
isozyme 192R, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
0.98
phenyl acetate
-
isozyme 192Q, in 50 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 25°C
1480
phenyl acetate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
1
S-methyl thiobutanoate
-
immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.508
diisopropylfluorophosphate
-
pH 8.0, 25°C, enzyme from phenotype B blood plasma
0.52
diisopropylfluorophosphate
-
pH 8.0, 25°C, wild-type enzyme, substrate phenyl acetate
0.598
diisopropylfluorophosphate
-
pH 8.0, 25°C, enzyme from phenotype A blood plasma
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00031
-
partially purified enzyme, substrate binapacryl, population Rothamsted
0.00043
-
partially purified enzyme, substrate binapacryl, population Peldon
0.0048
-
partially purified enzyme, substrate bromoxynil octanoate, population Peldon
0.0061
-
partially purified enzyme, substrate bromoxynil octanoate, population Rothamsted
0.086
pH 8.0, 25°C, substrate: phenyl acetate, purified recombinant enzyme
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
3.5
6.5
recombinant enzyme from crude cell extract, using phenyl acetate as substrate, at 60°C and pH 7.0
8.5
-
recombinant enzyme, after purification, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
11.4
pH 8.0, 25°C, substrate: 4-nitrophenyl butyrate, purified recombinant enzyme
13.6
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
15
20.7
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
39
pH 8.0, 25°C, substrate: 4-nitrophenyl acetate, purified recombinant enzyme
85.05
-
using phenyl acetate as substrate (arylesterase activity of PON1), at 25°C
155.6