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Information on EC 3.1.1.2 - arylesterase and Organism(s) Homo sapiens and UniProt Accession Q15165

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.2 arylesterase
IUBMB 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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Homo sapiens
UNIPROT: Q15165
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
paraoxonase, arylesterase, paraoxonase 1, paraoxonase-1, paraoxonase1, est-1, est-2, paraoxonase/arylesterase, a-esterase, alpha-esterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A-esterase
-
-
-
-
AREase
aromatic esterase
-
-
-
-
Aryl-ester hydrolase
-
-
-
-
arylesterase
HDL-PON1
-
-
K-45
-
-
-
-
paraoxonase
paraoxonase-1
-
-
paraoxonase/arylesterase
paraoxonase1
-
-
PON-aryl
PON1/Aryl
-
serum paraoxonase/arylesterase 1
-
additional information
-
also EC 3.1.8.1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9032-73-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
activity is about 5% of that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
activity is similar to that with PON1 (P27169 (UniProt))
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
activity is about 7% of that with PON1 (P27169 (UniProt))
-
-
?
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
activity is less than 1% of that with PON1 (P27169 (UniProt))
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
-
0.1% of the activity with phenyl acetate, A-type enzyme. 0.25% of the activity with phenyl acetate, B-type enzyme
-
-
?
1-phenylvinyl acetate + H2O
1-phenylethylenol + acetate
show the reaction diagram
-
-
-
?
2,2,2-trifluoroethyl acetate + H2O
2,2,2-trifluoroethanol + acetate
show the reaction diagram
-
-
-
?
2,2-difluoroethyl acetate + H2O
2,2-difluoroethanol + acetate
show the reaction diagram
-
-
-
?
2,3-difluorophenyl acetate + H2O
2,3-difluorophenol + acetate
show the reaction diagram
-
-
-
?
2,4-difluorophenyl acetate + H2O
2,4-difluorophenol + acetate
show the reaction diagram
-
-
-
?
2,6-difluorophenyl acetate + H2O
2,6-difluorophenol + acetate
show the reaction diagram
-
-
-
?
2-carboxythiophenyl acetate + H2O
2-carboxythiophenol + acetate
show the reaction diagram
-
-
-
?
2-fluoroethyl acetate + H2O
2-fluoroethanol + acetate
show the reaction diagram
-
-
-
?
2-fluorophenyl acetate + H2O
2-fluorophenol + acetate
show the reaction diagram
-
-
-
?
2-methoxythiophenyl acetate + H2O
2-methoxythiophenol + acetate
show the reaction diagram
-
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
show the reaction diagram
3,4-dimethyl phenyl acetate + H2O
3,4-dimethylphenol + acetate
show the reaction diagram
-
-
-
?
3-cyanophenyl acetate + H2O
3-cyanophenol + acetate
show the reaction diagram
-
-
-
?
3-fluorophenyl acetate + H2O
3-fluorophenol + acetate
show the reaction diagram
-
-
-
?
3-nitrophenyl acetate + H2O
3-nitrophenol + acetate
show the reaction diagram
-
-
-
?
4-(chloromethyl)phenyl acetate + H2O
4-chloromethyl phenol + acetate
show the reaction diagram
-
-
-
?
4-acetoxyacetophenone + H2O
4-hydroxyacetophenone + acetate
show the reaction diagram
-
-
-
?
4-acetoxybenzaldehyde + H2O
4-hydroxybenzaldehyde + acetate
show the reaction diagram
-
-
-
?
4-acetoxybenzaldehyde + H2O
?
show the reaction diagram
-
-
-
?
4-carboxyphenyl acetate + H2O
4-carboxyphenol + acetate
show the reaction diagram
-
-
-
?
4-chlorophenyl acetate + H2O
4-chlorophenol + acetate
show the reaction diagram
-
-
-
?
4-cyanophenyl acetate + H2O
4-cyanophenol + acetate
show the reaction diagram
-
-
-
?
4-diethyl phosphate methyl benzoate + H2O
?
show the reaction diagram
-
-
-
?
4-methoxy phenyl acetate + H2O
4-methoxy phenol + acetate
show the reaction diagram
-
-
-
?
4-methylphenyl acetate + H2O
4-methylphenol + acetate
show the reaction diagram
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
4-nitrophenyl diethylphosphate + H2O
diethylphosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
9-(2,4-dimethylphenoxycarbonyl)-10-methylacridinium triflate + H2O
2,4-dimethylphenol + 10-methylacridinium trifluoromethanesulfonate
show the reaction diagram
-
-
-
-
?
9-(4-chlorophenoxycarbonyl)-10-methylacridinium triflate + H2O
4-chlorophenol + 10-methylacridinium trifluoromethanesulfonate
show the reaction diagram
-
-
-
-
?
9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate + H2O
9-carboxy-10-methylacridinium triflate + 4-chlorophenol
show the reaction diagram
-
-
-
-
?
9-(4-methylphenoxycarbonyl)-10-methylacridinium triflate + H2O
4-methylphenol + 10-methylacridinium trifluoromethanesulfonate
show the reaction diagram
-
-
-
-
?
9-(4-tert-butylphenoxycarbonyl)-10-methylacridinium triflate + H2O
4-tert-butylphenol + 10-methylacridinium trifluoromethanesulfonate
show the reaction diagram
-
-
-
-
?
9-(phenyloxycarbonyl)-10-methylacridinium triflate + H2O
phenol + 10-methylacridinium trifluoromethanesulfonate
show the reaction diagram
-
-
-
-
?
benzyl acetate + H2O
benzyl alcohol + acetate
show the reaction diagram
-
-
-
?
butyl acetate + H2O
butanol + acetate
show the reaction diagram
-
-
-
?
ethyl acetate + H2O
ethanol + acetate
show the reaction diagram
-
-
-
?
isopropyl acetate + H2O
isobutanol + acetate
show the reaction diagram
-
-
-
?
methyl 4-(acetyloxy)benzoate + H2O
methyl 4-hydroxybenzoate + acetate
show the reaction diagram
-
-
-
?
naphthalen-2-yl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
?
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
phenylacetate + H2O
phenol + acetate
show the reaction diagram
propyl acetate + H2O
propanol + acetate
show the reaction diagram
-
-
-
?
S-(4-carboxyphenyl)-thioacetate + H2O
4-carboxythiophenol + acetate
show the reaction diagram
-
-
-
?
thiophenyl acetate + H2O
?
show the reaction diagram
-
27% of the activity with phenyl acetate, A-type enzyme. 34% of the activity with phenyl acetate, B-type enzyme
-
-
?
thiophenyl acetate + H2O
thiophenol + acetate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phenylacetate + H2O
phenol + acetate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
added to assay
Cd2+
-
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyquinoline
4-chloromercuribenzoate
-
complete inhibition at 0.2 mM
6-palmityl-ascorbic acid
-
-
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
D-penicillamine
-
40.5% residual activity after 24 h in the presence of 0.2 mg/ml D-penicillamine
diisopropylfluorophosphate
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
Fe2+
-
ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 51% inactivation after 30 min
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
-
lanthanum(III) chloride
-
about 50% inhibition at 0.05 mM
methylglyoxal
-
decreases specific activity in a concentration-dependent manner
Mg2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
N-ethylmaleimide
-
leads to 24fold reduced enzyme activity at 0.2 mM
NaCl
-
1.0 mM NaCl decreases the serum arylesterase activity of the enzyme
nitrilotriacetic acid
-
organophosphorous compounds
inhibit the enzyme of all genotypes slightly after in vivo exposure
-
paraoxon
-
mixed type inhibition
phenyl acetate
phosphatidylserine
-
-
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
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
-
Zn2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-dilauroyl-phosphatidylcholine
-
stimulation
1-palmitoyl-2-arachidonoylphosphatidylcholine
stimulates arylesterase activity
1-palmitoyl-2-linoleoylphosphatidylcholine
stimulates arylesterase activity
Ca2+
-
required
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
dimyristoyl phosphatidylcholine
-
stimulates
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
-
lecithin
lysolecithin
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
NaCl
-
-
palmitoyl-lysophosphatidylglycerol
0.01 mM, 47% stimulation of arylesterase activity
phosphate
-
preserves activity with considerable fluctuations, modulates oligomeric state
phosphatidylcholine
-
purified A or B-type esterases are stimulated
phosphatidylethanolamine
phosphatidylglycerol
-
stimulation
phosphatidylinositol
enhances arylesterase activity, but slightly decreases paraoxonase activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
0.16 - 0.65
2-naphthyl acetate
2.1
3,4-dimethyl phenyl acetate
-
1.9
3-cyanophenyl acetate
-
1.4
3-fluorophenyl acetate
-
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
-
0.289 - 1.5
4-nitrophenyl acetate
5
Benzyl acetate
-
10
butyl acetate
-
15.4
ethyl acetate
-
1.26
p-tolyl acetate
-
1.42
paraoxon
pH 7.4, 25°C
0.265 - 10.8
phenyl acetate
13
propyl acetate
-
additional information
9-(4-chlorophenyloxycarbonyl)-10-methylacridinium triflate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
1-phenylvinyl acetate
-
4
2,2,2-trifluoroethyl acetate
-
0.82
2,2-difluoroethyl acetate
-
403
2,3-difluorophenyl acetate
-
334
2,4-difluorophenyl acetate
-
145
2,6-difluorophenyl acetate
-
0.5
2-fluoroethyl acetate
-
431
2-fluorophenyl acetate
-
1.9 - 26.25
2-naphthyl acetate
51
3,4-dimethyl phenyl acetate
-
125
3-cyanophenyl acetate
-
571
3-fluorophenyl acetate
-
59
3-nitrophenyl acetate
-
14
4-acetoxy methyl benzoate
-
13
4-acetoxyacetophenone
pH 8.0
26
4-acetoxybenzaldehyde
117
4-chlorophenyl acetate
-
23
4-cyanophenyl acetate
-
0.244
4-diethyl phosphate methyl benzoate
pH 8.0
26 - 2500
4-nitrophenyl acetate
0.0008 - 0.02
Benzyl acetate
0.27
butyl acetate
-
0.242
ethyl acetate
-
18
naphthalen-2-yl acetate
pH 8.0, wild-type enzyme
68
p-tolyl acetate
-
7.4 - 4778
phenyl acetate
0.4
propyl acetate
-
additional information
additional information
-
all kinetic parameters increase with temperature, but the ratios kcat/Km and Kp/Km remain practically constant
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4200 - 4700
4-nitrophenyl acetate
0.000133 - 1670
phenyl acetate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.508 - 0.598
diisopropylfluorophosphate
0.401 - 0.885
phenyl acetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
1.4
pH 8.0, 25°C, substrate: 4-nitrophenyl butyrate, purified recombinant enzyme
0.0636
-
-
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
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
20.7
pH 8.0, 25°C, substrate: 4-nitrophenyl propionate, purified recombinant enzyme
3.5
-
enzyme purified from serum, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
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
465
recombinant enzyme after 90fold purification
5.15
recombinant enzyme from crude cell extract
558
-
purified enzyme from phenotype A blood plasma
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
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8
-
-
additional information
pH-rate profile of PON1 with 2-naphthyl acetate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
purified PON1, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
high density lipoprotein-associated enzyme
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PON2_HUMAN
354
0
39381
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
127500
recombinant enzyme, nondenaturing PAGE
42000
3 * 42000, recombinant enzyme, SDS-PAGE
39000
2 * 39000, recombinant enzyme
40000
41000
-
x * 41000, glycosylated enzyme, SDS-PAGE or mass spectrometry, x * 42000, glycosylated enzyme, SDS-PAGE or mass spectrometry, x * 44000, glycosylated enzyme, SDS-PAGE or mass spectrometry
42000
-
x * 41000, glycosylated enzyme, SDS-PAGE or mass spectrometry, x * 42000, glycosylated enzyme, SDS-PAGE or mass spectrometry, x * 44000, glycosylated enzyme, SDS-PAGE or mass spectrometry
43000
-
x * 43000, SDS-PAGE
44000
45000
91900
serum PON1, nondenaturing PAGE
94900
recombinant enzyme, nondenaturing PAGE
95600
recombinant PON1, nondenaturing PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
3 * 42000, recombinant enzyme, SDS-PAGE
dimer
oligomer
once purified, human PON1 is as a mixture of at least two oligomerization states. The absence of human phosphate binding protein favors homo-oligomerization of PON1 into different state(s) of higher molecular size
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
D54N
no enzymic activity
E313A
slightly decreased activity
E314A
enzymic activity similar to wild-type
F222D
F222Y
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
H115W/N133S
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
L69F
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
Q192R
R192Q
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
complete loss of activity above
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
association of paraoxonase 1 with high-density lipoprotein stabilizes the enzyme
the enzyme is stabilized by the two major high density lipoprotein subfractions LpA-I and LpA-I,A-II
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 6 months, less than 15% loss of activity
4°C, 2 weeks
-
4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month
-
4°C, 6 months, less than 15% loss of activity
4°C, purified PON1 in DEAE buffer, at least two weeks, remains stable
4°C, purified recombinant enzyme in 20 mM Tris pH 7.7, 1 mM CaCl2, at least one month, remains stable
4°C, purified recombinant PON1 preparations typically lose about 20% of the arylesterase activity within the first month after purification, compared with less than 10% loss for the enzyme purified from serum. There is no further significant loss of the PON1 activity afterward, suggesting the existence of two pools in the purified PON1, a labile one and a stable one
4°C, the enzyme activity is significantly lower after 48 h as well as after 1, 2 and 4 weeks storage when compared to enzyme activities assayed in fresh serum
-
4°C, the purified rPON1A maintains stability for several months when stored in the presence of 0.1% Tergitol NP-10 and 1 mM CaCl2
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Trisacryl M column chromatography, Sephacryl S300HR gel filtration, and Cibacron Blue 3GA gel filtration
-
anion-exchange chromatography and concanavalin-A chromatography
blue agarose affinity chromatography and HiTrap DEAE column chromatography
by different types of chromatographies
-
by immobilized metal-ion affinity chromatography
-
by pseudo-affinity chromatography and gel filtration
-
by Triton-X-100-treatment, ammonium sulfate precipitation, cholesterol-conjugated magnetic nanoparticles and gel filtration, at 4°C, to homogeneity, 515fold with 73% yield
-
ceramic HA column chromatography, DEAE-Sepharose column chromatography, Sephadex G-25 gel filtration, and tert-butyl Sepharose column chromatography
Cibacron Blue 3GA-agarose column chromatography, DEAE-Sepharose column chromatography, gel filtration, and Sepharose CL-6B column chromatography
-
co-purification of PON1 and phosphate binding protein from high-density-lipoprotein-particles using hydroxyapatite chromatography, method development
DEAE-Sepharose column chromatography, Concanavalin A-Sepharose column chromatography, and Sepharose CL-6B gel filtration
-
native enzyme from plasma of fasted humans by sequential chromatographic steps
-
Q-Sepharose column chromatography
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant enzyme is expressed in Trichoplusia ni High Five insect cells
a high level of recombinant hPON1 type A (rPON1A) is produced by Hi-5 insect cells. A fraction is secreted into the cell culture medium, but the majority remains associated with the host insect cells
-
application of directed evolution in achieving functional expression of PON1 and PON3 in Escherichia coli culture and a dramatic increase in their hydrolytic proficiency toward the fluorogenic organophosphate substrate 7-O-diethylphosphoryl-3-cyano-7-hydroxycoumarin. The powerful tool of directed evolution opens new prospects for improving their phosphotriesterase activity toward other hazardous organophosphates and toward catalytic activities related to the prevention of atherosclerosis
expressed from Trichoplusia ni larvae
-
expressed in baculovirus system in Hi5 insect cells
expressed in Drosophila melanogaster
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Trichoplusia ni larvae
-
expression in Escherichia coli
expression of PON3 in Spodoptera frugiperda Sf9 cells using the baculovirus expression system
gene PON1, genotyping, naturally occuring polymorphisms in the gene coding and the promoter regions affect the activity and the enzyme level
genotyping of naturally occuring polymorphisms, allele frequency determination
the recombinant enzyme is expressed in Trichoplusia ni High Five insect cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
arylesterase activity is decreased in patients with lacunar infections
-
arylesterase activity is significantly lower in patients with chronic active hepatitis B compared to hepatitis B carrier patients or control group patients
-
blood serum enzyme activity significantly decreases in acute myeloid leukemia
-
enzyme activities in fluorosis patients are considerably decreased up to 56.45% (mild), 61.5% (moderate) and 50% (severe) as compared to control group
-
enzyme levels are significantly lower in patients affected by mild cognitive impairment, vascular dementia, late onset Alzheimer's disease, late onset Alzheimer's disease-vascular dementia mixed dementia as well as those with multiple sclerosis as compared to healthy controls
-
enzyme levels of infants in fasting are significantly lower than the values in postprandial
-
enzyme levels of the patients with papillary thyroid cancer are significantly lower compared to those of the control group
-
mean values of serum arylesterase activity decrease significantly in stage 3 and stage 4 esophageal cancer patients compared with stage 2 esophageal cancer patients
-
serum arylesterase activity is significantly lower in patients with metabolic syndrome than healthy subjects
-
the enzyme activity is reduced in Behcet's disease
-
the mean serum arylesterase activity is significantly higher in the esophageal cancer group compared to healthy controls
-
there is no significant differences in enzyme levels between the patients with autoimmune thyroid disease and healthy control groups
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reiner, E.; Simeon-Rudolf, V.; Skrinjaric-Spoljar, M.
Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera
Toxicol. Lett.
82/83
447-452
1995
Homo sapiens
Manually annotated by BRENDA team
Gan, K.N.; Smolen, A.; Eckerson, H.W.; La Du, B.N.
Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities
Drug Metab. Dispos.
19
100-106
1991
Homo sapiens
Manually annotated by BRENDA team
Smolen, A.; Eckerson, H.W.; Gan, K.N.; Hailat, N.; La Du, B.N.
Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase
Drug Metab. Dispos.
19
107-112
1991
Homo sapiens
Manually annotated by BRENDA team
Haagen, L.; Brock, A.
A new automated method for phenotyping arylesterase (EC 3.1.1.2) based upon inhibition of enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate
Eur. J. Clin. Chem. Clin. Biochem.
30
391-395
1992
Homo sapiens
Manually annotated by BRENDA team
Debord, J.; Dantoine, T.; Bollinger, J.C.; Abraham, M.H.; Verneuil, B.; Merle, L.
Inhibition of arylesterase by aliphatic alcohols
Chem. Biol. Interact.
113
105-115
1998
Homo sapiens
Manually annotated by BRENDA team
La Du, B.N.; Adkins, S.; Kuo, C.L.; Lipsig, D.
Studies on human serum paraoxonase/arylesterase
Chem. Biol. Interact.
87
25-34
1993
Homo sapiens
Manually annotated by BRENDA team
Kuo, C.L.; La Du, B.N.
Comparison of purified human and rabbit serum paraoxonases
Drug Metab. Dispos.
23
935-944
1995
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
La Du, B.N.; Billecke, S.; Hsu, C.; Haley, R.W.; Broomfield, C.A.
Serum paraoxonase (PON1) isozymes: the quantitative analysis of isozymes affecting individual sensitivity to environmental chemicals
Drug Metab. Dispos.
29
566-569
2001
Homo sapiens (P27169)
Manually annotated by BRENDA team
Lorentz, K.; Wirtz, W.; Weiss, T.
Continuous monitoring of arylesterase in human serum
Clin. Chim. Acta
308
69-78
2001
Homo sapiens
Manually annotated by BRENDA team
Billecke, S.; Draganov, D.; Counsell, R.; Stetson, P.; Watson, C.; Hsu, C.; La Du, B.N.
Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters
Drug Metab. Dispos.
28
1335-1342
2000
Homo sapiens (P27169)
Manually annotated by BRENDA team
Brushia, R.J.; Forte, T.M.; Oda, M.N.; La Du, B.N.; Bielicki, J.K.
Baculovirus-mediated expression and purification of human serum paraoxonase 1A
J. Lipid Res.
42
951-958
2001
Homo sapiens
Manually annotated by BRENDA team
Lu, H.; Zhu, J.; Zang, Y.; Ze, Y.; Qin, J.
Cloning, high level expression of human paraoxonase-3 in Sf9 cells and pharmacological characterization of its product
Biochem. Pharmacol.
70
1019-1025
2005
Homo sapiens (Q15166)
Manually annotated by BRENDA team
Gaidukov, L.; Tawfik, D.S.
High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I
Biochemistry
44
11843-11854
2005
Homo sapiens (P27169)
Manually annotated by BRENDA team
Khersonsky, O.; Tawfik, D.S.
Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
Biochemistry
44
6371-6382
2005
Homo sapiens (P27169)
Manually annotated by BRENDA team
Yeung, D.T.; Josse, D.; Nicholson, J.D.; Khanal, A.; McAndrew, C.W.; Bahnson, B.J.; Lenz, D.E.; Cerasoli, D.M.
Structure/function analyses of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model
Biochim. Biophys. Acta
1702
67-77
2004
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Yeung, D.T.; Lenz, D.E.; Cerasoli, D.M.
Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates
FEBS J.
272
2225-2230
2005
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Nguyen, S.D.; Sok, D.E.
Effect of 3,4-dihydroxyphenylalanine on Cu2+-induced inactivation of HDL-associated paraoxonase1 and oxidation of HDL; inactivation of paraoxonase1 activity independent of HDL lipid oxidation
Free Radic. Res.
38
969-976
2004
Homo sapiens
Manually annotated by BRENDA team
Khersonsky, O.; Tawfik, D.S.
The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
J. Biol. Chem.
281
7649-7656
2006
Homo sapiens (P27169)
Manually annotated by BRENDA team
Draganov, D.I.; Teiber, J.F.; Speelman, A.; Osawa, Y.; Sunahara, R.; La Du, B.N.
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
J. Lipid Res.
46
1239-1247
2005
Homo sapiens (P27169), Homo sapiens (Q15165), Homo sapiens (Q15166), Homo sapiens
Manually annotated by BRENDA team
Aharoni, A.; Gaidukov, L.; Yagur, S.; Toker, L.; Silman, I.; Tawfik, D.S.
Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
Proc. Natl. Acad. Sci. USA
101
482-487
2004
Homo sapiens (Q15166), Mus musculus (Q62087), Oryctolagus cuniculus (Q9BGN0)
Manually annotated by BRENDA team
Lu, H.; Zhu, J.; Zang, Y.; Ze, Y.; Qin, J.
Cloning, purification, and refolding of human paraoxonase-3 expressed in Escherichia coli and its characterization
Protein Expr. Purif.
46
92-99
2006
Homo sapiens (Q15166), Homo sapiens
Manually annotated by BRENDA team
Kilic, S.S.; Aydin, S.; Kilic, N.; Erman, F.; Celik, I.
Serum arylesterase and paraoxonase activity in patients with chronic hepatitis
World J. Gastroenterol.
11
7351-7354
2005
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Sumegova, K.; Blazicek, P.; Waczulikova, I.; Zitnanova, I.; Durackova, Z.
Activity of paraoxonase 1 (PON1) and its relationship to markers of lipoprotein oxidation in healthy Slovaks
Acta Biochim. Pol.
53
783-787
2006
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Juretic, D.; Motejlkova, A.; Kunovi?, B.; Reki?, B.; Flegar-Mestri?, Z.; Vuji?, L.; Mesi?, R.; Lukac-Bajalo, J.; Simeon-Rudolf, V.
Paraoxonase/arylesterase in serum of patients with type II diabetes mellitus
Acta Pharm.
56
59-68
2006
Homo sapiens
Manually annotated by BRENDA team
Santanam, N.; Parthasarathy, S.
Aspirin is a substrate for paraoxonase-like activity: implications in atherosclerosis
Atherosclerosis
191
272-275
2007
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Nguyen, S.D.; Sok, D.E.
Preferable stimulation of PON1 arylesterase activity by phosphatidylcholines with unsaturated acyl chains or oxidized acyl chains at sn-2 position
Biochim. Biophys. Acta
1758
499-508
2006
Homo sapiens (P27169)
Manually annotated by BRENDA team
Rochu, D.; Renault, F.; Clery-Barraud, C.; Chabriere, E.; Masson, P.
Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s)
Biochim. Biophys. Acta
1774
874-883
2007
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Sirivarasai, J.; Kaojarern, S.; Yoovathaworn, K.; Sura, T.
Paraoxonase (PON1) polymorphism and activity as the determinants of sensitivity to organophosphates in human subjects
Chem. Biol. Interact.
168
184-192
2007
Homo sapiens, Homo sapiens (P27169)
Manually annotated by BRENDA team
Can Demirdoegen, B.; Tuerkanoglu, A.; Bek, S.; Sanisoglu, Y.; Demirkaya, S.; Vural, O.; Arinc, E.; Adali, O.
Paraoxonase/arylesterase ratio, PON1 192Q/R polymorphism and PON1 status are associated with increased risk of ischemic stroke
Clin. Biochem.
41
1-9
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Schulpis, K.H.; Karikas, G.A.; Bartzeliotou, A.; Papakonstantinou, E.D.; Kalogerakou, M.; Tsakiris, S.
The effect of diet on paraoxonase 1/arylesterase activities in patients with disorders of galactose metabolism
Clin. Endocrinol. (Oxf.)
67
687-692
2007
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Isik, A.; Koca, S.S.; Ustundag, B.; Celik, H.; Yildirim, A.
Paraoxonase and arylesterase levels in rheumatoid arthritis
Clin. Rheumatol.
26
342-348
2007
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Gur, M.; Aslan, M.; Yildiz, A.; Demirbag, R.; Yilmaz, R.; Selek, S.; Erel, O.; Ozdogru, I.
Paraoxonase and arylesterase activities in coronary artery disease
Eur. J. Clin. Invest.
36
779-787
2006
Homo sapiens
Manually annotated by BRENDA team
Schulpis, K.H.; Bartzeliotou, A.; Tsakiris, S.; Gounaris, A.; Papassotiriou, I.
Serum paraoxonase/arylesterase activities in phenylketonuric patients on diet
Eur. J. Clin. Nutr.
61
803-808
2007
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Renault, F.; Chabriere, E.; Andrieu, J.; Dublet, B.; Masson, P.; Rochu, D.
Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography
J. Chromatogr. B
836
15-21
2006
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Park, C.H.; Nguyen, S.D.; Kim, M.R.; Jeong, T.S.; Sok, D.E.
Differential effect of lysophospholipids on activities of human plasma paraoxonase1, either soluble or lipid-bound
Lipids
41
371-380
2006
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Kanamori-Kataoka, M.; Seto, Y.
Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R)
Anal. Biochem.
385
94-100
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Tavori, H.; Khatib, S.; Aviram, M.; Vaya, J.
Characterization of the PON1 active site using modeling simulation, in relation to PON1 lactonase activity
Bioorg. Med. Chem.
16
7504-7509
2008
Homo sapiens (P27169)
Manually annotated by BRENDA team
Yildiz, A.; Gur, M.; Demirbag, R.; Yilmaz, R.; Akyol, S.; Aslan, M.; Erel, O.
Paraoxonase and arylesterase activities in untreated dipper and non-dipper hypertensive patients
Clin. Biochem.
41
779-784
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Krzystek-Korpacka, M.; Boehm, D.; Matusiewicz, M.; Diakowska, D.; Grabowski, K.; Gamian, A.
Paraoxonase 1 (PON1) status in gastroesophageal malignancies and associated paraneoplastic syndromes - connection with inflammation
Clin. Biochem.
41
804-811
2008
Homo sapiens (P27169)
Manually annotated by BRENDA team
Kasprzak, M.; Iskra, M.; Majewski, W.; Wielkoszynski, T.
Arylesterase and paraoxonase activity of paraoxonase (PON1) affected by ischemia in the plasma of patients with arterial occlusion of the lower limbs
Clin. Biochem.
42
50-56
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Garces, C.; Lopez-Simon, L.; Rubio, R.; Benavente, M.; Cano, B.; Ortega, H.; de Oya, M.
High-density lipoprotein cholesterol and paraoxonase 1 (PON1) genetics and serum PON1 activity in prepubertal children in Spain
Clin. Chem. Lab. Med.
46
809-813
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Dullaart, R.P.; de Vries, R.; Sluiter, W.J.; Voorbij, H.A.
High plasma C-reactive protein (CRP) is related to low paraoxonase-I (PON-I) activity independently of high leptin and low adiponectin in type 2 diabetes mellitus
Clin. Endocrinol. (Oxf.)
70
221-226
2009
Homo sapiens (P27169)
Manually annotated by BRENDA team
Liu, Y.; Mackness, B.; Mackness, M.
Comparison of the ability of paraoxonases 1 and 3 to attenuate the in vitro oxidation of low-density lipoprotein and reduce macrophage oxidative stress
Free Radic. Biol. Med.
45
743-748
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Camuzcuoglu, H.; Arioz, D.T.; Toy, H.; Kurt, S.; Celik, H.; Erel, O.
Serum paraoxonase and arylesterase activities in patients with epithelial ovarian cancer
Gynecol. Oncol.
112
481-485
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Parker-Katiraee, L.; Bousiaki, E.; Monk, D.; Moore, G.E.; Nakabayashi, K.; Scherer, S.W.
Dynamic variation in allele-specific gene expression of Paraoxonase-1 in murine and human tissues
Hum. Mol. Genet.
17
3263-3270
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Keskin, M.; Dolar, E.; Dirican, M.; Kiyici, M.; Yilmaz, Y.; Gurel, S.; Nak, S.G.; Erdinc, S.; Gulten, M.
Baseline and salt-stimulated paraoxonase and arylesterase activities in patients with chronic liver disease: Relation with disease severity
Intern. Med. J.
39
243-248
2009
Homo sapiens
Manually annotated by BRENDA team
Rock, W.; Rosenblat, M.; Miller-Lotan, R.; Levy, A.P.; Elias, M.; Aviram, M.
Consumption of wonderful variety pomegranate juice and extract by diabetic patients increases paraoxonase 1 association with high-density lipoprotein and stimulates its catalytic activities
J. Agric. Food Chem.
56
8704-8713
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Pasca, S.P.; Dronca, E.; Nemes, B.; Kaucsar, T.; Endreffy, E.; Iftene, F.; Benga, I.; Cornean, R.; Dronca, M.
Paraoxonase 1 activities and polymorphisms in autism spectrum disorders
J. Cell. Mol. Med.
14
600-607
2010
Homo sapiens
Manually annotated by BRENDA team
Stoltz, D.A.; Ozer, E.A.; Taft, P.J.; Barry, M.; Liu, L.; Kiss, P.J.; Moninger, T.O.; Parsek, M.R.; Zabner, J.
Drosophila are protected from Pseudomonas aeruginosa lethality by transgenic expression of paraoxonase-1
J. Clin. Invest.
118
3123-3131
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Aksoy, H.; Aksoy, A.N.; Ozkan, A.; Polat, H.
Serum lipid profile, oxidative status, and paraoxonase 1 activity in hyperemesis gravidarum
J. Clin. Lab. Anal.
23
105-109
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Moren, X.; Deakin, S.; Liu, M.L.; Taskinen, M.R.; James, R.W.
HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress
J. Lipid Res.
49
1246-1253
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Connelly, P.W.; Zinman, B.; Maguire, G.F.; Mamakeesick, M.; Harris, S.B.; Hegele, R.A.; Retnakaran, R.; Hanley, A.J.
Association of the novel cardiovascular risk factors paraoxonase 1 and cystatin C in type 2 diabetes
J. Lipid Res.
50
1216-1222
2009
Homo sapiens
Manually annotated by BRENDA team
Wills, A.M.; Landers, J.E.; Zhang, H.; Richter, R.J.; Caraganis, A.J.; Cudkowicz, M.E.; Furlong, C.E.; Brown, R.H.
Paraoxonase 1 (PON1) organophosphate hydrolysis is not reduced in ALS
Neurology
70
929-934
2008
Homo sapiens (P27169)
Manually annotated by BRENDA team
Stevens, R.C.; Suzuki, S.M.; Cole, T.B.; Park, S.S.; Richter, R.J.; Furlong, C.E.
Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning
Proc. Natl. Acad. Sci. USA
105
12780-12784
2008
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Hu, X.; Jiang, X.; Lenz, D.E.; Cerasoli, D.M.; Wallqvist, A.
In silico analyses of substrate interactions with human serum paraoxonase 1
Proteins
75
486-498
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Karikas, G.A.; Schulpis, K.H.; Bartzeliotou, A.; Regoutas, S.; Thanopoulou, C.; Papaevangelou, V.; Giannoulia-Karantana, A.; Papassotiriou, I.; Fytou-Pallikari, A.
Early effects of sodium valproate monotherapy on serum paraoxonase/arylesterase activities
Scand. J. Clin. Lab. Invest.
69
31-35
2009
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Richter, R.J.; Jarvik, G.P.; Furlong, C.E.
Paraoxonase 1 (PON1) status and substrate hydrolysis
Toxicol. Appl. Pharmacol.
235
1-9
2009
Homo sapiens (P27169)
Manually annotated by BRENDA team
Nguyen, S.D.; Hung, N.D.; Cheon-Ho, P.; Ree, K.M.; Dai-Eun, S.
Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1)
Biochim. Biophys. Acta
1790
155-160
2009
Homo sapiens
Manually annotated by BRENDA team
Hofmann, J.; Keifer, M.; Furlong, C.; De Roos, A.; Farin, F.; Fenske, R.; van Belle, G.; Checkoway, H.
Serum cholinesterase inhibition in relation to paraoxonase-1 (PON1) status among organophosphate-Exposed agricultural pesticide handlers
Environ. Health Perspect.
117
1402-1408
2009
Homo sapiens
Manually annotated by BRENDA team
Popa, C.; van Tits, L.J.; Barrera, P.; Lemmers, H.L.; van den Hoogen, F.H.; van Riel, P.L.; Radstake, T.R.; Netea, M.G.; Roest, M.; Stalenhoef, A.F.
Anti-inflammatory therapy with tumour necrosis factor alpha inhibitors improves high-density lipoprotein cholesterol antioxidative capacity in rheumatoid arthritis patients
Ann. Rheum. Dis.
68
868-872
2009
Homo sapiens
Manually annotated by BRENDA team
Samra, Z.Q.; Shabir, S.; Rehmat, Z.; Zaman, M.; Nazir, A.; Dar, N.; Athar, M.A.
Synthesis of cholesterol-conjugated magnetic nanoparticles for purification of human paraoxonase 1
Appl. Biochem. Biotechnol.
162
671-686
2010
Homo sapiens
Manually annotated by BRENDA team
Antognelli, C.; Gambelunghe, A.; Del Buono, C.; Murgia, N.; Talesa, V.N.; Muzi, G.
Crystalline silica Min-U-Sil 5 induces oxidative stress in human bronchial epithelial cells BEAS-2B by reducing the efficiency of antiglycation and antioxidant enzymatic defenses
Chem. Biol. Interact.
182
13-21
2009
Homo sapiens
Manually annotated by BRENDA team
Otto, T.C.; Kasten, S.A.; Kovaleva, E.; Liu, Z.; Buchman, G.; Tolosa, M.; Davis, D.; Smith, J.R.; Balcerzak, R.; Lenz, D.E.; Cerasoli, D.M.
Purification and characterization of functional human paraoxonase-1 expressed in Trichoplusia ni larvae
Chem. Biol. Interact.
187
388-392
2010
Homo sapiens
Manually annotated by BRENDA team
Renault, F.; Carus, T.; Clery-Barraud, C.; Elias, M.; Chabriere, E.; Masson, P.; Rochu, D.
Integrative analytical approach by capillary electrophoresis and kinetics under high pressure optimized for deciphering intrinsic and extrinsic cofactors that modulate activity and stability of human paraoxonase (PON1)
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
878
1346-1355
2010
Homo sapiens, synthetic construct
Manually annotated by BRENDA team
Camuzcuoglu, H.; Toy, H.; Cakir, H.; Celik, H.; Erel, O.
Decreased paraoxonase and arylesterase activities in the pathogenesis of future atherosclerotic heart disease in women with gestational diabetes mellitus
J. Womens Health (Larchmt)
18
1435-1439
2009
Homo sapiens
Manually annotated by BRENDA team
Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Doctor, B.P.; Nambiar, M.P.
Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1
Biochem. Biophys. Res. Commun.
403
97-102
2010
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Valiyaveettil, M.; Alamneh, Y.; Rezk, P.; Biggemann, L.; Perkins, M.W.; Sciuto, A.M.; Doctor, B.P.; Nambiar, M.P.
Protective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs
Biochem. Pharmacol.
81
800-809
2011
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Moghtaderi, A.; Hashemi, M.; Dabiri, S.; Moazeni-Roodi, A.; Hosseini, M.
Serum paraoxonase and arylesterase activities in patients with lacunar infarction: a case control study
Clin. Biochem.
44
288-292
2011
Homo sapiens
Manually annotated by BRENDA team
Hashemi, M.; Kordi-Tamandani, D.M.; Sharifi, N.; Moazeni-Roodi, A.; Kaykhaei, M.A.; Narouie, B.; Torkmanzehi, A.
Serum paraoxonase and arylesterase activities in metabolic syndrome in Zahedan, southeast Iran
Eur. J. Endocrinol.
164
219-222
2011
Homo sapiens
Manually annotated by BRENDA team
Cayir, K.; Bilici, M.; Tekin, S.; Kara, F.; Turkyilmaz, A.; Yildirim, A.
Serum paraoxonase and arylesterase activities in esophageal cancer: A controlled study
Eur. J. Gen. Med.
7
398-403
2010
Homo sapiens
-
Manually annotated by BRENDA team
Bayrak, A.; Bayrak, T.; Demirpence, E.; Kilinc, K.
Differential hydrolysis of homocysteine thiolactone by purified human serum (192)Q and (192)R PON1 isoenzymes
J. Chromatogr. B
879
49-55
2011
Homo sapiens
Manually annotated by BRENDA team
Duygu, F.; Tekin Koruk, S.; Aksoy, N.
Serum paraoxonase and arylesterase activities in various forms of hepatitis B virus infection
J. Clin. Lab. Anal.
25
311-316
2011
Homo sapiens
Manually annotated by BRENDA team
Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Farag, H.A.; Agrawal, P.; Doctor, B.P.; Nambiar, M.P.
In vitro efficacy of paraoxonase 1 from multiple sources against various organophosphates
Toxicol. In Vitro
25
905-913
2011
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Dias, C.; Batuca, J.; Marinho, A.; Caixas, U.; Monteiro, E.; Antunes, A.; Pereira, S.
Quantification of the arylesterase activity of paraoxonase-1 in human blood
Anal. Methods
6
289-294
2014
Homo sapiens
-
Manually annotated by BRENDA team
Bajaj, P.; Aggarwal, G.; Tripathy, R.K.; Pande, A.H.
Interplay between amino acid residues at positions 192 and 115 in modulating hydrolytic activities of human paraoxonase 1
Biochimie
105
202-210
2014
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Bavec, A.; Knez, D.; Makovec, T.; Stojan, J.; Gobec, S.; Golicnik, M.
Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate
Biochimie
106
184-186
2014
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Debord, J.; Bollinger, J.C.; Harel, M.; Dantoine, T.
Temperature dependence of binding and catalysis for human serum arylesterase/paraoxonase
Biochimie
97
72-77
2014
Homo sapiens
Manually annotated by BRENDA team
Rosenblat, M.; Ward, S.; Volkova, N.; Hayek, T.; Aviram, M.
VLDL triglycerides inhibit HDL-associated paraoxonase 1 (PON1) activity: in vitro and in vivo studies
Biofactors
38
292-299
2012
Homo sapiens
Manually annotated by BRENDA team
Kirbas, A.; Kirbas, S.; Anlar, O.; Efe, H.; Yilmaz, A.
Serum paraoxonase and arylesterase activity and oxidative status in patients with multiple sclerosis
J. Clin. Neurosci.
20
1106-1109
2013
Homo sapiens
Manually annotated by BRENDA team
Kirbas, A.; Kirbas, S.; Cure, M.C.; Tufekci, A.
Paraoxonase and arylesterase activity and total oxidative/anti-oxidative status in patients with idiopathic Parkinson's disease
J. Clin. Neurosci.
21
451-455
2014
Homo sapiens
Manually annotated by BRENDA team
Kati, C.; Karadas, S.; Aslan, M.; Gonullu, H.; Duran, L.; Demir, H.
Serum paraoxonase and arylesterase activities and oxidative stress levels in patients with SSRI intoxication
J. Membr. Biol.
247
17-21
2014
Homo sapiens
Manually annotated by BRENDA team
Bajaj, P.; Tripathy, R.K.; Aggarwal, G.; Pande, A.H.
Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme
Protein Sci.
22
1799-1807
2013
Homo sapiens (P27169), Homo sapiens
Manually annotated by BRENDA team
Olama, S.M.; Elarman, M.M.
Evaluation of paraoxonase and arylesterase activities in Egyptian patients with ankylosing spondylitis
Rheumatol. Int.
33
1487-1494
2013
Homo sapiens
Manually annotated by BRENDA team
Tekin Koruk, S.; Aksoy, N.; Hamidanoglu, M.; Karsen, H.; Unlu, S.; Bilinc, H.
The activity of paraoxonase and arylesterase in patients with osteomyelitis
Scand. J. Clin. Lab. Invest.
72
513-517
2012
Homo sapiens
Manually annotated by BRENDA team
Mu, X.; Yu, N.; Wang, C.; Zou, X.; Abulimite, Z.; Xia, Z.
Evaluation of a new substrate for measurement of serum PON arylesterase activity
Talanta
88
711-716
2012
Homo sapiens
Manually annotated by BRENDA team
Abulimite, Z.; Mu, X.; Xiao, S.; Liu, M.; Li, Q.; Chen, G.
New chemiluminescent substrates of paraoxonase 1 with improved specificity synthesis and properties
Appl. Biochem. Biotechnol.
176
301-316
2015
Homo sapiens
Manually annotated by BRENDA team
Tripathy, R.K.; Aggarwal, G.; Bajaj, P.; Kathuria, D.; Bharatam, P.V.; Pande, A.H.
Towards understanding the catalytic mechanism of human paraoxonase 1 experimental and in silico mutagenesis studies
Appl. Biochem. Biotechnol.
182
1642-1662
2017
Homo sapiens
Manually annotated by BRENDA team
Solmaz Avcikurt, A.; Korkut, O.
Effect of certain non-steroidal anti-inflammatory drugs on the paraoxonase 2 (PON2) in human monocytic cell line U937
Arch. Physiol. Biochem.
124
378-382
2018
Homo sapiens
Manually annotated by BRENDA team
Kul, A.; Uzkeser, H.; Ozturk, N.
Paraoxonase and arylesterase levels in Behcets disease and their relations with the disease activity
Biochem. Genet.
55
335-344
2017
Homo sapiens
Manually annotated by BRENDA team
Zsiros, N.; Koncsos, P.; Lorincz, H.; Seres, I.; Katko, M.; Szentpeteri, A.; Varga, V.E.; Fueloep, P.; Paragh, G.; Harangi, M.
Paraoxonase-1 arylesterase activity is an independent predictor of myeloperoxidase levels in overweight patients with or without cardiovascular complications
Clin. Biochem.
49
862-867
2016
Homo sapiens
Manually annotated by BRENDA team
Arulkumar, M.; Vijayan, R.; Penislusshiyan, S.; Sathishkumar, P.; Angayarkanni, J.; Palvannan, T.
Alteration of paraoxonase, arylesterase and lactonase activities in people around fluoride endemic area of Tamil Nadu, India
Clin. Chim. Acta
471
206-215
2017
Homo sapiens
Manually annotated by BRENDA team
Bizon, A.; Milnerowicz, H.
The effect of divalent metal chelators and cadmium on serum phosphotriesterase, lactonase and arylesterase activities of paraoxonase 1
Environ. Toxicol. Pharmacol.
58
77-83
2018
Homo sapiens
Manually annotated by BRENDA team
Kahveci, H.; Laloglu, F.; Kilic, O.; Ciftel, M.; Yildirim, A.; Orbak, Z.; Ertekin, V.; Laloglu, E.
Serum paraoxonase and arylesterase values as antioxidants in healthy premature infants at fasting and posprandial times
Eur. Rev. Med. Pharmacol. Sci.
19
1761-1765
2015
Homo sapiens
Manually annotated by BRENDA team
Cebi, A.; Akgun, E.; Esen, R.; Demir, H.; Cifci, A.
The activities of serum paraoxonase and arylesterase and lipid profile in acute myeloid leukemia preliminary results
Eur. Rev. Med. Pharmacol. Sci.
19
4590-4594
2015
Homo sapiens
Manually annotated by BRENDA team
Zargari, M.; Sharafeddin, F.; Mahrooz, A.; Alizadeh, A.; Masoumi, P.
The common variant Q192R at the paraoxonase 1 (PON1) gene and its activity are responsible for a portion of the altered antioxidant status in type 2 diabetes
Exp. Biol. Med.
241
1489-1496
2016
Homo sapiens
Manually annotated by BRENDA team
Perla-Kajan, J.; Borowczyk, K.; Glowacki, R.; Nygard, O.; Jakubowski, H.
Paraoxonase 1 Q192R genotype and activity affect homocysteine thiolactone levels in humans
FASEB J.
32
6019
2018
Homo sapiens
Manually annotated by BRENDA team
Castellazzi, M.; Trentini, A.; Romani, A.; Valacchi, G.; Bellini, T.; Bonaccorsi, G.; Fainardi, E.; Cavicchio, C.; Passaro, A.; Zuliani, G.; Cervellati, C.
Decreased arylesterase activity of paraoxonase-1 (PON-1) might be a common denominator of neuroinflammatory and neurodegenerative diseases
Int. J. Biochem. Cell Biol.
81
356-363
2016
Homo sapiens
Manually annotated by BRENDA team
Korkmaz, H.; Tabur, S.; Ozkaya, M.; Oguz, E.; Elboga, U.; Aksoy, N.; Akarsu, E.
Paraoxonase and arylesterase levels in autoimmune thyroid diseases
Redox Rep.
21
227-231
2016
Homo sapiens
Manually annotated by BRENDA team
Korkmaz, H.; Tabur, S.; Oezkaya, M.; Aksoy, N.; Yildiz, H.; Akarsu, E.
Paraoxonase and arylesterase activities in patients with papillary thyroid cancer
Scand. J. Clin. Lab. Invest.
75
259-264
2015
Homo sapiens
Manually annotated by BRENDA team