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(1R,5S)-oxabicyclooctenone + H2O
?
(1S,5R)-oxabicyclooctenone + H2O
?
(R)-alpha-hydroxy-gamma-butyrolactone + H2O
(R)-2-hydroxybutyric acid
enzyme variant Q192: 0.88% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 3.95% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(R)-dihydro-5-(hydroxymethyl)-2(3H)-furanone + H2O
?
enzyme variant Q192: 1.23% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 3.29% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(S)-alpha-hydroxy-gamma-butyrolactone + H2O
(S)-2-hydroxybutyric acid
enzyme variant Q192: 8.14% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 19.6% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(S)-beta-hydroxy-gamma-butyrolactone + H2O
(S)-3-hydroxybutyric acid
enzyme variant Q192: 0.6% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 0.76% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(S)-dihydro-5-(hydroxymethyl)-2(3H)-furanone + H2O
?
enzyme variant Q192: 0.78% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 1.12% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
1,3-benzoxazol-2-one + H2O
?
-
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
4-(1-propenyloxymethyl)-1,3-dioxolan-2-one + H2O
?
enzyme variant Q192: 2.23% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 2.52% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
4-methoxyphenyl acetate + H2O
4-methoxyphenol + acetate
-
-
-
?
5-(thiobutyl)butyrolactone + H2O
?
the lactonase and the esterase activity of PON1 is mediated by the His115-His134
-
-
?
5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid 1,5-lactone + H2O
5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid
-
-
-
?
7-O-diethyl phosphoryl 3-cyano 4-methyl 7-hydroxycoumarin + H2O
?
-
-
-
?
alpha-angelica lactone + H2O
?
-
-
-
?
alpha-angelicalactone + H2O
4-hydroxypent-3-enoic acid
-
-
-
?
alpha-angelicalactone + H2O
?
enzyme variant Q192: 19.9% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 14.8% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
alpha-bromo-gamma-butyrolactone + H2O
2-bromobutyric acid
enzyme variant Q192: 47.2% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 40.8% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
beta-hydroxybutyrolactone + H2O
?
delta-decanolactone + H2O
5-hydroxydecanoic acid
delta-decanolactone + H2O
?
-
-
-
?
delta-dodecanolactone + H2O
?
-
-
-
?
delta-hexalactone + H2O
5-hydroxyhexanoic acid
-
-
-
?
delta-hexalactone + H2O
?
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoate
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoic acid
delta-tetradecanolactone + H2O
5-hydroxytetradecanoic acid
-
-
-
?
delta-undecanolactone + H2O
5-hydroxyundecanoic acid
-
-
-
?
delta-undecatiolactone + H2O
?
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
delta-valerolactone + H2O
?
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
weak activity
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
DL-3-oxo-hexanoyl-homoserine lactone + H2O
DL-3-oxo-hexanoyl-homoserine
-
-
-
?
DL-dodecanoyl-homoserine lactone + H2O
DL-dodecanoyl-homoserine
-
-
-
?
DL-heptanoyl-homoserine lactone + H2O
DL-heptanoyl-homoserine
-
-
-
?
DL-tetradecanoyl-homoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
epsilon-caprolactone + H2O
6-hydroxyhexanoic acid
enzyme variant Q192: 14.8% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 25.7% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
ethyl acetate + H2O
ethanol + acetate
-
-
-
?
gamma -nonalactone + H2O
?
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoic acid
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutyric acid
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-decanolactone + H2O
4-hydroxydecanoic acid
gamma-decanolactone + H2O
?
-
-
-
?
gamma-dodecanoic acid lactone + H2O
4-hydroxydodecanoic acid
-
-
-
?
gamma-dodecanoic lactone + H2O
4-hydroxydodecanoic acid
-
-
-
?
gamma-heptalactone + H2O
4-hydroxyheptanoic acid
-
-
-
?
gamma-heptalactone + H2O
?
-
-
-
?
gamma-heptanolide + H2O
4-hydroxyheptanoic acid
-
-
-
?
gamma-hexalactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-hexalactone + H2O
?
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
gamma-nonanoic acid lactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoic acid
-
-
-
?
gamma-octalactone + H2O
?
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenylbutanoic acid
-
-
-
?
gamma-thiobutyrolactone + H2O
?
-
-
-
?
gamma-undecanoic acid lactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanolactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanolactone + H2O
?
-
-
-
?
gamma-valerolactone + H2O
4-hydroxypentanoic acid
gamma-valerolactone + H2O
?
-
-
-
?
homocysteinthiolactone + H2O
(2S)-2-aminobutanethioic S-acid
-
-
-
?
homogenestic acid lactone + H2O
?
-
-
-
?
homogentisic acid lactone + H2O
homogentisic acid
lovastatin + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
mevastatin + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
N-oxododecanoyl-DL-homoserine lactone + H2O
?
-
-
-
?
pantoyl lactone + H2O
2,4-dihydroxy-3,3-dimethylbutanoic acid
-
-
-
?
propylene carbonate + H2O
?
enzyme variant Q192: 5.02% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 8.8% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
simvastatin + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
spironolactone + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
thiobutyl butyrolactone + H2O
?
-
-
-
?
undecano-gamma-lactone + H2O
4-hydroxyundecanoic acid
enzyme variant Q192: 11.8% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 12.7% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(R)-gamma-valerolactone + H2O
4-hydroxypentanoic acid
-
-
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
3-hydroxyoctanoate + H2O
?
-
-
-
-
?
5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoic acid 1,5-lactone + H2O
5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoic acid
-
-
-
?
5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid 1,5-lactone + H2O
5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid
-
-
-
?
5-thiobutyl butyrolactone + H2O
4-(butylsulfanyl)-4-hydroxybutanoic acid
-
-
-
-
?
7-O-diethylphosphoryl-3-cyano-4-methyl-7-hydroxycoumarin + H2O
(2Z)-2-cyano-3-[4-[(diethoxyphosphoryl)oxy]-2-hydroxyphenyl]but-2-enoic acid
-
-
-
-
?
alpha-angelicalactone + H2O
4-hydroxy-pent-3-enoic acid
-
-
-
?
canrenone + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
delta valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
-
?
delta-decanolactone + H2O
5-hydroxydecanoic acid
-
-
-
?
delta-hexalactone + H2O
5-hydroxyhexanoic acid
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoic acid
-
-
-
?
delta-tetradecanolactone + H2O
5-hydroxytetradecanoic acid
-
-
-
?
delta-undecanolactone + H2O
5-hydroxyundecanoic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
delta-valerolactone + H2O
?
-
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
-
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
DL-3-oxo-hexanoylhomoserine lactone + H2O
DL-3-oxo-hexanoylhomoserine
-
-
-
?
DL-dodecanoylhomoserine lactone + H2O
DL-dodecanoylhomoserine
-
-
-
?
DL-heptanoylhomoserine lactone + H2O
DL-heptanoylhomoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoylhomoserine
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxy-butyric acid
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
-
-
-
-
?
gamma-butyrolactone + H2O
?
-
-
-
-
?
gamma-butyrolactone + H2O
gamma-hydroxybutyrate
-
-
-
-
r
gamma-caprolactone + H2O
gamma-hydroxycaproate
gamma-decanolactone + H2O
4-hydroxydecanoic acid
-
-
-
?
gamma-heptalactone + H2O
4-hydroxyheptanoic acid
-
-
-
?
gamma-hexalactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
gamma-octalactone + H2O
4-hydroxyoctanoic acid
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenyl-butanoic acid
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenylbutanoic acid
-
-
-
?
gamma-undecanolactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanolactone + H2O
?
-
-
-
-
?
gamma-valerolactone + H2O
4-hydroxypentanoic acid
-
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
homocysteine thiolactone + H2O
?
-
-
-
-
?
homocysteinethiolactone + H2O
homocysteine
-
-
-
-
?
lovastatin + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
N-oxodecanoyl-DL-homoserine lactone + H2O
N-(3-oxodecanoyl)homoserine
-
-
-
-
?
phenyl acetate + H2O
?
-
-
-
?
spironolactone + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
additional information
?
-
(1R,5S)-oxabicyclooctenone + H2O
?
-
-
-
?
(1R,5S)-oxabicyclooctenone + H2O
?
enzyme variant Q192: 0.82% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 0.75% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
(1S,5R)-oxabicyclooctenone + H2O
?
-
-
-
?
(1S,5R)-oxabicyclooctenone + H2O
?
enzyme variant Q192: 1.67% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 2.92% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
-
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
enzyme variant Q192: 18.3% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 13.5% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
beta-hydroxybutyrolactone + H2O
?
-
-
-
?
beta-hydroxybutyrolactone + H2O
?
enzyme variant Q192: 3.83% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 7.53% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
delta-decanolactone + H2O
5-hydroxydecanoic acid
-
-
-
?
delta-decanolactone + H2O
5-hydroxydecanoic acid
enzyme variant Q192: 9.65% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 12.8% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoic acid
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
enzyme variant Q192: 75.4% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 71.0% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
enzyme variant Q192: 14.3% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 17% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutyric acid
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutyric acid
enzyme variant Q192: 2.46% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 9.05% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
gamma-decanolactone + H2O
4-hydroxydecanoic acid
-
-
-
?
gamma-decanolactone + H2O
4-hydroxydecanoic acid
enzyme variant Q192: 12.4% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 19.0% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-valerolactone + H2O
4-hydroxypentanoic acid
-
-
-
?
gamma-valerolactone + H2O
4-hydroxypentanoic acid
enzyme variant Q192: 7.28% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 6.97% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
homogentisic acid lactone + H2O
homogentisic acid
-
-
-
?
homogentisic acid lactone + H2O
homogentisic acid
enzyme variant Q192: 44% of the activity with phenyl acetate (cf. EC 3.1.1.2), enzyme variant R192: 49.7% of the activity with phenyl acetate (cf. EC 3.1.1.2)
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
-
-
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
?
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
r
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
r
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
r
additional information
?
-
PON's native enzyme activity is as a lactonase, the lactonase function of PON1 can protect transgenic flies from lethal Pseudomonas aeruginosa infection
-
-
?
additional information
?
-
PON1 is a lipolactonase that associates with HDL-apolipoprotein A-I and thereby plays a role in the prevention of atherosclerosis
-
-
?
additional information
?
-
contains arylesterase, paraoxonase, and lactonase activities
-
-
?
additional information
?
-
enzyme protein also shows activities of paraoxonase (EC 3.1.8.1) and arylesterase (EC 3.1.1.2)
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone or canrenone
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone or canrenone
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone or canrenone
-
-
?
additional information
?
-
PON3 is not able to prevent macrophage oxidative stress, however, is able to retard macrophage-induced low-density lipoprotein oxidation
-
-
?
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
?
-
no activity with homogentisic acid lactone and DL-3-oxo-hexanoyl-homoserine lactone
-
-
?
additional information
?
-
no activity with homogentisic acid lactone and DL-3-oxo-hexanoyl-homoserine lactone
-
-
?
additional information
?
-
no activity with homogentisic acid lactone and DL-3-oxo-hexanoyl-homoserine lactone
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone, canrenone, homogentisic acid lactone, gamma-butyrolactone, gamma-valerolactone, gamma-hexalactone, gamma-heptalactone, gamma-octalactone, gamma-nonalactone, gamma-decanolactone, gamma-undecanolactone, alpha-angelicalactone, delta-valerolactone, delta-hexalactone, delta-nonalactone, delta-decanolactone, delta-undecanolactone, delta-tetradecanolactone
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone, canrenone, homogentisic acid lactone, gamma-butyrolactone, gamma-valerolactone, gamma-hexalactone, gamma-heptalactone, gamma-octalactone, gamma-nonalactone, gamma-decanolactone, gamma-undecanolactone, alpha-angelicalactone, delta-valerolactone, delta-hexalactone, delta-nonalactone, delta-decanolactone, delta-undecanolactone, delta-tetradecanolactone
-
-
?
additional information
?
-
no activity with lovastatin, spironolactone, canrenone, homogentisic acid lactone, gamma-butyrolactone, gamma-valerolactone, gamma-hexalactone, gamma-heptalactone, gamma-octalactone, gamma-nonalactone, gamma-decanolactone, gamma-undecanolactone, alpha-angelicalactone, delta-valerolactone, delta-hexalactone, delta-nonalactone, delta-decanolactone, delta-undecanolactone, delta-tetradecanolactone
-
-
?
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 is most likely a lactonase, whereas the phosphotriesterase and esterase activities can be categorized as accidental
-
-
?
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0.0035
pH 8.0, 25°C, substrate: DL-tetradecanoyl-homoserine lactone, purified recombinant enzyme
0.0036
pH 8.0, 25°C, substrate: DL-heptanoyl-homoserine lactone, purified recombinant enzyme
0.0167
pH 8.0, 25°C, substrate: DL-dodecanoyl-homoserine lactone, purified recombinant enzyme
0.0334
pH 8.0, 25°C, substrate: DL-3-oxo-hexanoyl-homoserine lactone, purified recombinant enzyme
127.6
pH 8.0, 25°C, substrate: gamma-undecanolactone, purified recombinant enzyme
129.9
pH 8.0, 25°C, substrate: dihydrocoumarin, purified recombinant enzyme
135.7
pH 8.0, 25°C, substrate: 2-coumaranone, purified recombinant enzyme
144.7
pH 8.0, 25°C, substrate: gamma-nonalactone, purified recombinant enzyme
150
pH 8.0, 25°C, substrate: delta-nonalactone, purified recombinant enzyme
154
pH 8.0, 25°C, substrate: delta-tetradecanolactone, purified recombinant enzyme
173.8
pH 8.0, 25°C, substrate: gamma-decanolactone, purified recombinant enzyme
183
pH 8.0, 25°C, substrate: alpha-angelicalactone, purified recombinant enzyme
251
pH 8.0, 25°C, substrate: delta-decanolactone, purified recombinant enzyme
287
pH 8.0, 25°C, substrate: delta-undecanolactone, purified recombinant enzyme
32.1
pH 8.0, 25°C, substrate: gamma-butyrolactone, purified recombinant enzyme
329.5
pH 8.0, 25°C, substrate: homogentisic acid lactone, purified recombinant enzyme
45
pH 8.0, 25°C, substrate: gamma-valerolactone, purified recombinant enzyme
51.7
pH 8.0, 25°C, substrate: gamma-hexalactone, purified recombinant enzyme
57.2
pH 8.0, 25°C, substrate: gamma-heptalactone, purified recombinant enzyme
63
pH 8.0, 25°C, substrate: gamma-phenyl-gamma-butyrolactone, purified recombinant enzyme
671
pH 8.0, 25°C, substrate: delta-valerolactone, purified recombinant enzyme
69.2
pH 8.0, 25°C, substrate: gamma-octalactone, purified recombinant enzyme
72
pH 8.0, 25°C, substrate: delta-hexalactone, purified recombinant enzyme
75.4
pH 8.0, 25°C, substrate: 5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid 1,5-lactone, purified recombinant enzyme
0.0049
pH 8.0, 25°C, substrate: DL-heptanoyl-homoserine lactone, purified recombinant enzyme
0.011
pH 8.0, 25°C, substrate: spironolactone, purified recombinant enzyme
0.013
pH 8.0, 25°C, substrate: canrenone, purified recombinant enzyme
0.0255
pH 8.0, 25°C, substrate: DL-tetradecanoyl-homoserine lactone, purified recombinant enzyme
0.0268
pH 8.0, 25°C, substrate: DL-3-oxo-hexanoyl-homoserine lactone, purified recombinant enzyme
0.0311
pH 8.0, 25°C, substrate: DL-heptanoyl-homoserine lactone, purified recombinant enzyme
0.0977
pH 8.0, 25°C, substrate: DL-dodecanoyl-homoserine lactone, purified recombinant enzyme
0.266
pH 8.0, 25°C, substrate: lovastatin, purified recombinant enzyme
0.4239
pH 8.0, 25°C, substrate: DL-tetradecanoyl-homoserine lactone, purified recombinant enzyme
0.4588
pH 8.0, 25°C, substrate: DL-dodecanoyl-homoserine lactone, purified recombinant enzyme
0.68
pH 8.0, 25°C, substrate: gamma-phenyl-gamma-butyrolactone, purified recombinant enzyme
0.81
pH 8.0, 25°C, substrate: gamma-butyrolactone, purified recombinant enzyme
1.83
pH 8.0, 25°C, substrate: 5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid 1,5-lactone, purified recombinant enzyme
10.9
pH 8.0, 25°C, substrate: 2-coumaranone, purified recombinant enzyme
11.1
pH 8.0, 25°C, substrate: delta-nonalactone, purified recombinant enzyme
11.4
pH 8.0, 25°C, substrate: gamma-phenyl-gamma-butyrolactone, purified recombinant enzyme
11.7
pH 8.0, 25°C, substrate: delta-hexalactone, purified recombinant enzyme
126.1
pH 8.0, 25°C, substrate: dihydrocoumarin, purified recombinant enzyme
14.5
pH 8.0, 25°C, substrate: delta-valerolactone, purified recombinant enzyme
20.7
pH 8.0, 25°C, substrate: alpha-angelicalactone, purified recombinant enzyme
22.7
pH 8.0, 25°C, substrate: delta-tetradecanolactone, purified recombinant enzyme
23.9
pH 8.0, 25°C, substrate: gamma-hexalactone, purified recombinant enzyme
25.6
pH 8.0, 25°C, substrate: gamma-octalactone, purified recombinant enzyme
27.5
pH 8.0, 25°C, substrate: 5-hydroxy-6E,8Z,11Z,14Z-eicosatetraenoic acid 1,5-lactone, purified recombinant enzyme
27.7
pH 8.0, 25°C, substrate: gamma-heptalactone, purified recombinant enzyme
3.1
pH 8.0, 25°C, substrate: dihydrocoumarin, purified recombinant enzyme
30.9
pH 8.0, 25°C, substrate: gamma-nonalactone, purified recombinant enzyme
40.7
pH 8.0, 25°C, substrate: 2-coumaranone, purified recombinant enzyme
44.3
pH 8.0, 25°C, substrate: delta-decanolactone, purified recombinant enzyme
45.6
pH 8.0, 25°C, substrate: gamma-decanolactone, purified recombinant enzyme
6.2
pH 8.0, 25°C, substrate: gamma-valerolactone, purified recombinant enzyme
71.4
pH 8.0, 25°C, substrate: gamma-undecanolactone, purified recombinant enzyme
84.4
pH 8.0, 25°C, substrate: delta-undecanolactone, purified recombinant enzyme
additional information
new enzymatic tests are developed that detect total PON1 levels, irrespective of high-density lipoprotein status and R/Q polymorphism, as well as the degree of catalytic stimulation and increased stability that follows tight binding of PON1 to HDLapoA-I. The tests are based on measuring total PON1 levels with a fluorogenic phosphotriester, measuring the lipolactonase activity with a chromogenic lactone, and assaying the chelator-mediated inactivation rate of the enzyme. The latter two are affected by tight binding of high-density lipoprotein and thereby derive the levels of the serum PON1-HDL complex. The new tests are demonstrated with a group of healthy individuals and show that the levels of PON1-HDL vary by a factor of 12
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C284A
no lactonase activity with either homogentisic acid lactone or undecanoic-delta-lactone
H115A
activity with dicoumarin is 366% compared to wild-type activity, activity with delta-valerolactone is 3% of wild-type activity, activity with gamma-nonalactone is 1% of wild-type activity
H115Q
activity with dicoumarin is 268% compared to wild-type activity, activity with delta-valerolactone is 4.96% of wild-type activity, activity with gamma-nonalactone is 1.2% of wild-type activity. kcat/Km for delta-valerolactone is 2.2% of wild-type value, kcat/Km for gamma-nonalactone is 0.3% of wild-type value, kcat/Km for gamma-caprolactone is 1.4% of wild-type value, kcat/Km for 5-(thiobutyl)butyrolactone is 1.1% of wild-type value. Mutant with reduced lactonase activity, exhibits reduced or no biological function in ex vivo assay
H115Q/H134Q
kcat/Km for 5-(thiobutyl)butyrolactone is 0.2% of wild-type value mutant with reduced lactonase activity, exhibits reduced or no biological function in ex vivo assay
H115W/R192K
kinetic parameters comparable to mutant H115W
H115W/R192Q
complete loss of activity
H134Q
activity with dicoumarin is 77% compared to wild-type activity, activity with delta-valerolactone is 13% of wild-type activity, activity with gamma-nonalactone is 22% of wild-type activity. kcat/Km for delta-valerolactone is 11% of wild-type value, kcat/Km for gamma-nonalactone is 8% of wild-type value, kcat/Km for gamma-caprolactone is 19% of wild-type value, kcat/Km for 5-(thiobutyl)butyrolactone is 6.5% of wild-type value. Mutant with reduced lactonase activity, exhibits reduced or no biological function in ex vivo assay
H184Q
activity with dicoumarin is 57% compared to wild-type activity, activity with delta-valerolactone is 44% of wild-type activity, activity with gamma-nonalactone is 44% of wild-type activity
H184T
activity with dicoumarin is 17% compared to wild-type activity, activity with delta-valerolactone is 35% of wild-type activity, activity with gamma-nonalactone is 39% of wild-type activity
H285Q
activity with dicoumarin is 22% compared to wild-type activity, activity with delta-valerolactone is 20% of wild-type activity, activity with gamma-nonalactone is 38% of wild-type activity
H285S
activity with dicoumarin is 13% compared to wild-type activity, activity with delta-valerolactone is 8% of wild-type activity, activity with gamma-nonalactone is 16% of wild-type activity
L69G/S111T/H115W/H134R/R192K/F222S/T332S
mutant designed for expression in Escherichia coli in soluble and active form. Activity towards delta-valerolactone and homocysteinthiolactone is similar to wild-type, ativity towards N-oxododecanoyl-DL-homoserine lactone is 4fold increased
D183N
-
the mutant disfavors paraoxon binding due to its charged nature and possible electrostatic repulsion with the phosphate group of paraoxon
F222D
-
the mutation abolishes both esterase and PON activity of PON1
F222Y
-
the mutation abolishes the PON activity of PON1 but retains the esterase activity with a 1.5fold increase in KM for phenyl acetate
H115W
-
the mutant shows a 2fold increase in PON1 activity compared to the wild type enzyme
L55M
-
the mutant enzyme shows decreased lactonase activities compared to the wild type
L69V
-
the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme
L69V/V369A
-
the mutant shows increased paraoxon binding affinity compared to the wild type enzyme
R180T
-
the mutant retains a partial hydrolyzing activity against homocysteinethiolactone, whereas the delta-valerolactone-hydrolyzing activity is completely abolished
R192Q
-
the polymorphic residue R192Q interacts with the leaving group of paraoxon, suggesting it plays an important role in the proper positioning of this substrate in the active site
S193P
-
the mutation increases phosphotriesterase activity of PON1
V346A
-
the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme
additional information
the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus
H115W
activity with dicoumarin is 261% compared to wild-type activity, activity with delta-valerolactone is 0.6% of wild-type activity, activity with gamma-nonalactone is 0.1% of wild-type activity
H115W
significant decrease in the rate of catalysis, moderate increase of the affinity of the substrate
Q192R
-
the mutant enzyme shows increased lactonase activities compared to the wild type
Q192R
-
the mutant exhibits significantly lower homocysteine-thiolactone/creatinine levels and has 2.6 and 3.3fold greater catalytic efficiency with homocysteine-thiolactone and paraoxon, respectively, than the wild type enzyme
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Fishbein, W.N.; Bessman, S.P.
Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. I. Tissue localization, stoichiometry, specificity, distinction from esterase
J. Biol. Chem.
241
4835-4841
1966
Homo sapiens, Rattus norvegicus
brenda
Fishbein, W.N.; Bessman, S.P.
Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of gamma-lactones. II. Metal ion effects, kinetics, and equilibria
J. Biol. Chem.
241
4842-4847
1966
Homo sapiens, Rattus norvegicus
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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), Oryctolagus cuniculus (Q9BGN0)
brenda
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)
brenda
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)
brenda
Gaidukov, L.; Tawfik, D.S.
The development of human sera tests for HDL-bound serum PON1 and its lipolactonase activity
J. Lipid Res.
48
1637-1646
2007
Homo sapiens (P27169)
brenda
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)
brenda
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 (Q15166)
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Zhang, Y.; Liu, H.; He, J.; Xu, K.; Bai, H.; Wang, Y.; Zhang, F.; Zhang, J.; Cheng, L.; Fan, P.
Lactonase activity and status of paraoxonase 1 in Chinese women with polycystic ovarian syndrome
Eur. J. Endocrinol.
172
391-402
2015
Homo sapiens
brenda
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
brenda
Le, Q.A.; Kim, S.; Chang, R.; Kim, Y.H.
Insights into the lactonase mechanism of serum paraoxonase 1 (PON1) experimental and quantum mechanics/molecular mechanics (QM/MM) studies
J. Phys. Chem. B
119
9571-9585
2015
Homo sapiens
brenda