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(1R,5S)-oxabicyclooctenone + H2O
?
(1S,5R)-oxabicyclooctenone + H2O
?
(2S,4RS)-2-hydroxy-4-butyrolactone + H2O
(S)-2-hydroxy-4-phenylbutyrate
-
-
-
-
?
(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)
-
-
?
(R)-gamma-valerolactone + H2O
4-hydroxypentanoic acid
-
-
-
-
?
(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-bromobutyrolactone + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
2-hydroxybutyrolactone + H2O
?
2450% activity compared to DL-pantoyl lactone
-
-
?
3,4-dihydrocoumarin + H2O
?
3-hydroxyoctanoate + H2O
?
-
-
-
-
?
3-oxo-decanoyl-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
3-oxo-octanoyl-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-L-homoserine
-
-
-
?
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-butyrolactone + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
4-methoxyphenyl acetate + H2O
4-methoxyphenol + acetate
-
-
-
?
4-phenyl-2-hydroxyl-4-butyrolactone + H2O
?
22% activity compared to DL-pantoyl lactone
-
-
?
5-(thiobutyl)butyrolactone + H2O
?
5-(thioethyl)butyrolactone + H2O
?
the lactonase and the esterase activity of PON1 is mediated by the His115-His134 dyad
-
-
?
5-butyl-4-methyldihydro-2(3H)-furanone + H2O
4-hydroxy-3-methyl-octanoate
i.e. whiskey lactone
-
-
?
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
-
-
-
-
?
5-thiobutyl-butyro-1,4-lactone + H2O
?
-
-
-
-
?
7-O-diethyl phosphoryl 3-cyano 4-methyl 7-hydroxycoumarin + H2O
?
-
-
-
?
7-O-diethylphosphoryl-3-cyano-4-methyl-7-hydroxycoumarin + H2O
(2Z)-2-cyano-3-[4-[(diethoxyphosphoryl)oxy]-2-hydroxyphenyl]but-2-enoic acid
-
-
-
-
?
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide + H2O
3-hydroxy-2-[(7-oxononanoyl)amino]propanoic acid
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide + H2O
3-hydroxy-2-[(9-oxoundecanoyl)amino]propanoate
-
-
-
?
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide + H2O
3-hydroxy-2-[(9-oxoundecanoyl)amino]propanoic acid
-
-
-
?
alpha-angelica lactone + H2O
?
-
-
-
?
alpha-angelicalactone + H2O
4-hydroxy-pent-3-enoic acid
-
-
-
?
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)
-
-
?
alpha-hydroxy-beta,beta-dimethyl-gamma-butyrolactone + H2O
2,4-dihydroxy-3,3-dimethylbutanoate
-
-
-
-
?
alpha-hydroxy-gamma-butyrolactone + H2O
2,4-dihydroxybutanoate
-
-
-
-
?
beta-butyrolactone + H2O
3-hydroxybutanoate
-
-
-
-
?
beta-hydroxy-gamma-butyrolactone + H2O
3,4-dihydroxybutanoate
-
-
-
-
?
beta-hydroxybutyrolactone + H2O
?
canrenone + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
D-pantolactone + H2O
D-pantoic acid
-
-
-
-
?
delta valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
-
?
delta-decanolactone + H2O
5-hydroxydecanoic acid
delta-decanolactone + H2O
?
-
-
-
?
delta-dodecalactone + H2O
5-hydroxydecanoate
-
-
-
?
delta-dodecanolactone + H2O
5-hydroxydodecanoate
-
-
-
?
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-undecalactone + H2O
5-hydroxydecanoate
-
-
-
?
delta-undecanolactone + H2O
5-hydroxyundecanoate
-
-
-
?
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
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
DL-3-oxo-hexanoyl-homoserine lactone + H2O
DL-3-oxo-hexanoyl-homoserine
-
-
-
?
DL-3-oxo-hexanoylhomoserine lactone + H2O
DL-3-oxo-hexanoylhomoserine
-
-
-
?
DL-dodecanoyl-homoserine lactone + H2O
DL-dodecanoyl-homoserine
-
-
-
?
DL-dodecanoylhomoserine lactone + H2O
DL-dodecanoylhomoserine
-
-
-
?
DL-heptanoyl-homoserine lactone + H2O
DL-heptanoyl-homoserine
-
-
-
?
DL-heptanoylhomoserine lactone + H2O
DL-heptanoylhomoserine
-
-
-
?
DL-pantoyl lactone + H2O
pantoic acid
-
-
-
-
?
DL-pantoyllactone + H2O
pantoic acid
100% activity
-
-
?
DL-tetradecanoyl-homoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoylhomoserine
-
-
-
?
dodecanoic-1,4-lactone + H2O
4-hydroxydodecanoate
-
-
-
?
dodecanoic-1,5-lactone + H2O
5-hydroxydodecanoate
-
-
-
?
dodecanoic-delta-lactone + H2O
5-hydroxydodecanoate
dodecanoic-gamma-lactone + H2O
dodecanoate
-
-
-
?
epsilon-caprolactone + H2O
6-hydroxyhexanoate
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
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
ethyl acetate + H2O
ethanol + acetate
-
-
-
?
gamma -nonalactone + H2O
?
-
-
-
?
gamma-(R)-caprolactone + H2O
4-hydroxyhexanoate
slight preference but not an exclusive specificity for the (R)-enantiomers of capro- and valerolactone
-
-
?
gamma-(R)-valerolactone + H2O
4-hydroxypentanoate
slight preference but not an exclusive specificity for the (R)-enantiomers of capro- and valerolactone
-
-
?
gamma-(S)-caprolactone + H2O
4-hydroxyhexanoate
slight preference but not an exclusive specificity for the (R)-enantiomers of capro- and valerolactone
-
-
?
gamma-(S)-valerolactone + H2O
4-hydroxypentanoate
slight preference but not an exclusive specificity for the (R)-enantiomers of capro- and valerolactone
-
-
?
gamma-butyrolactone + H2O
4-hydroxy-butyric acid
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
gamma-butyrolactone + H2O
4-hydroxybutanoic acid
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutyric acid
gamma-butyrolactone + H2O
?
-
-
-
-
?
gamma-butyrolactone + H2O
gamma-hydroxybutyrate
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
gamma-caprolactone + H2O
gamma-hydroxycaproate
gamma-decanolactone + H2O
4-hydroxydecanoic acid
gamma-decanolactone + H2O
?
-
-
-
?
gamma-dodecalactone + H2O
4-hydroxydodecanoate
-
-
-
?
gamma-dodecanoic acid lactone + H2O
4-hydroxydodecanoic acid
-
-
-
?
gamma-dodecanoic lactone + H2O
4-hydroxydodecanoic acid
-
-
-
?
gamma-dodecanolactone + H2O
4-hydroxydodecanoate
-
-
-
?
gamma-heptalactone + H2O
4-hydroxyheptanoate
-
-
-
?
gamma-heptalactone + H2O
4-hydroxyheptanoic acid
-
-
-
?
gamma-heptalactone + H2O
?
-
-
-
?
gamma-heptanolactone + H2O
4-hydroxyheptanoate
-
-
-
?
gamma-heptanolide + H2O
4-hydroxyheptanoate
-
-
-
?
gamma-heptanolide + H2O
4-hydroxyheptanoic acid
-
-
-
?
gamma-heptanolide + H2O
?
-
-
-
?
gamma-hexalactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-hexalactone + H2O
?
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoate
gamma-nonalactone + H2O
4-hydroxynonanoic acid
gamma-nonanoic acid lactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
gamma-octalactone + H2O
4-hydroxyoctanoic acid
-
-
-
?
gamma-octalactone + H2O
?
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenyl-butanoic acid
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenylbutanoic acid
-
-
-
?
gamma-thiobutyrolactone + H2O
?
-
-
-
?
gamma-undecalactone + H2O
4-hydroxyundecanoate
-
-
-
?
gamma-undecanoic acid lactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanoic lactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanolactone + H2O
4-hydroxyundecanoate
-
-
-
?
gamma-undecanolactone + H2O
4-hydroxyundecanoic acid
-
-
-
?
gamma-undecanolactone + H2O
?
gamma-valerolactone + H2O
4-hydroxypentanoic acid
gamma-valerolactone + H2O
?
-
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
homocysteine thiolactone + H2O
?
-
-
-
-
?
homocysteinethiolactone + H2O
homocysteine
-
-
-
-
?
homocysteinthiolactone + H2O
(2S)-2-aminobutanethioic S-acid
-
-
-
?
homogenestic acid lactone + H2O
?
-
-
-
?
homogentisic acid lactone + H2O
homogentisic acid
L-pantoyl lactone + H2O
L-pantoic acid
methyl 2-chloroacetate + H2O
?
11.6% activity compared to DL-pantoyl lactone
-
-
?
methyl 2-chloropropanoate + H2O
?
2.3% activity compared to DL-pantoyl lactone
-
-
?
methyl lactate + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
methyl mandelate + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
mevastatin + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
N-(2-oxotetrahydrofuran-3-yl)nonanamide + H2O
3-hydroxy-2-(nonanoylamino)propanoate
-
-
-
?
N-(2-oxotetrahydrofuran-3-yl)pentanamide + H2O
3-hydroxy-2-(pentanoylamino)propanoate
-
-
-
?
N-(2-oxotetrahydrofuran-3-yl)pentanamide + H2O
3-hydroxy-2-(pentanoylamino)propanoic acid
-
-
-
?
N-(3-oxobutanoyl)-DL-homoserine lactone + H2O
N-(3-oxobutanoyl)-DL-homoserine
-
-
-
?
N-(3-oxodecanoyl)-DL-homoserine lactone + H2O
N-(3-oxodecanoyl)-DL-homoserine
-
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
N-(3-oxododecanoyl)-DL-homoserine lactone + H2O
N-(3-oxododecanoyl)-DL-homoserine
-
-
-
?
N-(3-oxododecanoyl)-L-homoserine lactone + H2O
N-(3-oxododecanoyl)-L-homoserine
-
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
N-(3-oxohexanoyl)-L-homoserine
N-(3-oxohexanoyl)homoserine lactone + H2O
N-(3-oxohexanoyl)homoserine
-
-
-
?
N-(3-oxooctanoyl)-DL-homoserine lactone + H2O
N-(3-oxooctanoyl)-DL-homoserine
-
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-L-homoserine
N-(3-oxooctanoyl)homoserine lactone + H2O
N-(3-oxooctanoyl)homoserine
-
-
-
?
N-butanoyl-DL-homoserine lactone + H2O
N-butanoyl-L-homoserine
-
-
-
?
N-butanoylhomoserine lactone + H2O
N-butanoylhomoserine
-
-
-
?
N-dodecanoyl-DL-homoserine lactone + H2O
N-dodecanoyl-DL-homoserine
-
-
-
?
N-dodecanoylhomoserine lactone + H2O
N-dodecanoylhomoserine
-
-
-
?
N-hexanoyl-(S)-homoserine lactone
N-hexanoyl-(S)-homoserine
N-hexanoylhomoserine lactone + H2O
N-hexanoylhomoserine
-
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
octanoyl-homoserine
-
-
-
?
N-octanoylhomoserine lactone + H2O
N-octanoylhomoserine
-
-
-
?
N-oxodecanoyl-DL-homoserine lactone + H2O
N-(3-oxodecanoyl)homoserine
-
-
-
-
?
N-oxododecanoyl-DL-homoserine lactone + H2O
?
-
-
-
?
nonanoic-1,4-lactone + H2O
4-hydroxynonanoate
-
-
-
?
nonanoic-1,5-lactone + H2O
5-hydroxynonanoate
-
-
-
?
nonanoic-delta-lactone + H2O
5-hydroxynonanoate
-
-
-
?
nonanoic-gamma-lactone + H2O
4-hydroxynonanoate
-
-
-
?
octanoyl-L-homoserine lactone + H2O
N-octanoyl-L-homoserine
-
-
-
?
pantoyl lactone + H2O
2,4-dihydroxy-3,3-dimethylbutanoic acid
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
phenyl acetate + H2O
?
-
-
-
?
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
-
-
?
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)
-
-
?
undecanoic-1,4-lactone + H2O
4-hydroxyundecanoate
-
-
-
?
undecanoic-1,5-lactone + H2O
5-hydroxyundecanoate
-
-
-
?
undecanoic-delta-lactone + H2O
5-hydroxyundecanoate
-
-
-
?
undecanoic-gamma-lactone + H2O
4-hydroxyundecanoate
-
-
-
?
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
-
-
-
?
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)
-
-
?
2-coumaranone + H2O
(2-hydroxyphenyl)acetic acid
-
-
-
-
?
2-coumaranone + H2O
?
-
25% of activity compared to L-pantoyl lactone
-
?
2-coumaranone + H2O
?
-
25% of activity compared to L-pantoyl lactone
-
?
3,4-dihydrocoumarin + H2O
?
-
23% of activity compared to L-pantoyl lactone
-
?
3,4-dihydrocoumarin + H2O
?
-
23% of activity compared to L-pantoyl lactone
-
?
3-oxo-decanoyl-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
-
-
-
?
3-oxo-decanoyl-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
-
-
-
?
5-(thiobutyl)butyrolactone + H2O
?
the lactonase and the esterase activity of PON1 is mediated by the His115-His134
-
-
?
5-(thiobutyl)butyrolactone + H2O
?
the lactonase and the esterase activity of PON1 is mediated by the His115-His134 dyad
-
-
?
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide + H2O
3-hydroxy-2-[(7-oxononanoyl)amino]propanoic acid
-
-
-
?
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide + H2O
3-hydroxy-2-[(7-oxononanoyl)amino]propanoic acid
-
-
-
?
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-hydroxynonanoate
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoate
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoate
-
-
-
?
delta-nonalactone + H2O
5-hydroxynonanoate
-
-
-
?
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
-
-
-
?
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)
-
-
?
delta-valerolactone + H2O
5-hydroxypentanoic acid
-
-
-
?
delta-valerolactone + H2O
?
-
-
-
-
?
delta-valerolactone + H2O
?
-
-
-
?
delta-valerolactone + H2O
?
-
-
-
?
delta-valerolactone + H2O
?
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
-
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
weak activity
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic acid
-
-
-
?
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
-
-
-
?
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)
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)propanoic acid
-
-
-
?
dodecanoic-delta-lactone + H2O
5-hydroxydodecanoate
-
-
-
?
dodecanoic-delta-lactone + H2O
5-hydroxydodecanoate
-
-
-
?
epsilon-caprolactone + H2O
6-hydroxyhexanoate
-
-
-
?
epsilon-caprolactone + H2O
6-hydroxyhexanoate
-
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
epsilon-caprolactone + H2O
?
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
-
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
-
-
-
?
gamma-butyrolactone + H2O
4-hydroxybutanoate
-
-
-
?
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-butyrolactone + H2O
gamma-hydroxybutyrate
-
-
-
-
r
gamma-butyrolactone + H2O
gamma-hydroxybutyrate
-
-
-
-
r
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-caprolactone + H2O
4-hydroxyhexanoic acid
-
-
-
?
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
?
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
r
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
?
gamma-caprolactone + H2O
gamma-hydroxycaproate
-
-
-
-
r
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-hydroxynonanoate
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoate
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoate
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-nonalactone + H2O
4-hydroxynonanoic acid
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
r
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
?
gamma-octalactone + H2O
4-hydroxyoctanoate
-
-
-
-
r
gamma-undecanolactone + H2O
?
-
-
-
-
?
gamma-undecanolactone + H2O
?
-
-
-
?
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)
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
r
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
?
gamma-valerolactone + H2O
gamma-hydroxyvalerate
-
-
-
-
r
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)
-
-
?
L-pantoyl lactone + H2O
L-pantoic acid
-
stereospecific hydrolysis
-
?
L-pantoyl lactone + H2O
L-pantoic acid
-
stereospecific hydrolysis
-
?
lovastatin + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
lovastatin + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
-
-
-
?
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
the best, possibly natural, substrate of wild-type enzyme
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
N-(3-oxohexanoyl)-L-homoserine
-
-
-
?
N-(3-oxohexanoyl)-L-homoserine lactone + H2O
N-(3-oxohexanoyl)-L-homoserine
-
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-L-homoserine
-
-
-
?
N-(3-oxooctanoyl)-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-L-homoserine
-
-
-
?
N-hexanoyl-(S)-homoserine lactone
N-hexanoyl-(S)-homoserine
-
-
-
?
N-hexanoyl-(S)-homoserine lactone
N-hexanoyl-(S)-homoserine
-
-
-
?
N-hexanoyl-(S)-homoserine lactone
N-hexanoyl-(S)-homoserine
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
spironolactone + H2O
?
activity with enzyme variant Q192 and R192
-
-
?
spironolactone + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
additional information
?
-
enzyme degrades acetylate homoserine lactones in a tail length independent manner, but the presence of the tail is required for activity. Residue Y194 seems to show efficacy in stabilizing the intermediate state. The proton shuttling necessary for catalytic activity might be mediated by both water and substrate-based intra-molecular proton transfer. Upon substrate binding, the zinc-bridging hydroxide anion is effectively protected from re-protonation by the plug-like function of the acyl tails whereupon the ring-opening reaction can proceed. Subsequent protonation of the product's alkoxide group can then be accomplished by the intramolecular proton transfer from the intermediate state's carboxylic acid group where the resulting carboxylate group better accommodates the still-neighboring zinc ion
-
-
?
additional information
?
-
no activity with 4-nitrophenyl acetate and 4-nitrophenyl butyrate
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl acetate and 4-nitrophenyl butyrate
-
-
?
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
?
-
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
?
-
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 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 or canrenone
-
-
?
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, 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
-
-
?
additional information
?
-
PON1 is a lipo-lactonase which is associated with high density lipoprotein and possesses antioxidative properties
-
-
?
additional information
?
-
no activity with dihydrocoumarin
-
-
?
additional information
?
-
-
no activity with dihydrocoumarin
-
-
?
additional information
?
-
no activity with dihydrocoumarin
-
-
?
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1.316
(R)-gamma-valerolactone
-
at pH 7.0 and 30°C
0.013 - 4.55
2-coumaranone
290.2
2-hydroxybutyrolactone
recombinant enzyme, at pH 6.7-6.9, 30°C
2.56
3,4-dihydrocoumarin
-
pH 7.4, 30°C
4.5
3-hydroxyoctanoate
-
-
0.231
3-oxo-decanoyl-L-homoserine lactone
pH 8.3, 40°C
0.186
3-oxo-octanoyl-L-homoserine lactone
pH 8.3, 40°C
0.27 - 1.83
5-(thiobutyl)butyrolactone
0.93
5-butyl-4-methyldihydro-2(3H)-furanone
pH 8.3, temperature not specified in the publication
0.836
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide
pH 8.3, 25°C
0.213
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide
pH 8.3, 25°C
0.839
delta-dodecalactone
pH 8.3, 40°C
1.678
delta-dodecanolactone
pH 8.3, 25°C, wild-type enzyme
0.359 - 1.22
delta-nonalactone
0.105
delta-undecalactone
pH 8.3, 40°C
0.057 - 0.219
delta-undecanolactone
0.4 - 8.5
delta-valerolactone
0.013 - 1.376
dihydrocoumarin
121
DL-pantoyllactone
recombinant enzyme, at pH 6.7-6.9, 30°C
0.242
dodecanoic-1,4-lactone
pH 8.3, 25°C
0.185
dodecanoic-1,5-lactone
pH 8.3, 25°C
0.12
dodecanoic-delta-lactone
pH 8.3, 25°C, wild-type enzyme
0.48
dodecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
0.234 - 1.031
epsilon-caprolactone
0.55
gamma-(R)-caprolactone
pH 8.3, temperature not specified in the publication
4.56
gamma-(R)-valerolactone
pH 8.3, temperature not specified in the publication
0.75
gamma-(S)-caprolactone
pH 8.3, temperature not specified in the publication
1.95
gamma-(S)-valerolactone
pH 8.3, temperature not specified in the publication
0.16 - 36.8
gamma-butyrolactone
0.9 - 3.8
Gamma-caprolactone
0.0021
gamma-dodecalactone
pH 8.3, 40°C
0.22
gamma-dodecanoic acid lactone
pH 8.0
0.3 - 0.7
gamma-dodecanoic lactone
1.22
gamma-dodecanolactone
pH 8.3, 25°C, wild-type enzyme
0.872
gamma-heptalactone
pH 8.3, 40°C
0.166
gamma-heptanolactone
pH 8.3, 25°C, wild-type enzyme
0.13 - 0.58
gamma-heptanolide
140
gamma-hydroxybutyrate
-
-
5.7
Gamma-hydroxycaproate
-
-
9 - 20
Gamma-hydroxyvalerate
0.047 - 2.943
gamma-nonalactone
0.39
gamma-nonanoic acid lactone
pH 8.0
1.3 - 3.1
Gamma-octalactone
2.8 - 3.5
gamma-thiobutyrolactone
0.12
gamma-undecalactone
pH 8.3, 40°C
0.6
gamma-undecanoic acid lactone
pH 8.0
0.6
gamma-undecanoiclactone
-
recombinant enzyme
0.013 - 2.099
gamma-undecanolactone
3.3 - 4
gamma-valerolactone
21.2 - 23.5
homocysteine thiolactone
0.45 - 0.52
Homogentisic acid lactone
3.59
L-pantoyl lactone
-
pH 7.4, 30°C
0.178
N-(2-oxotetrahydrofuran-3-yl)pentanamide
pH 8.3, 25°C
0.1
N-(3-oxodecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.143 - 1.605
N-(3-oxodecanoyl)-L-homoserine lactone
0.44
N-(3-oxododecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.0178 - 0.456
N-(3-oxododecanoyl)-L-homoserine lactone
0.558
N-(3-oxohexanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.592
N-(3-oxohexanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.042 - 1.2
N-(3-oxooctanoyl)-DL-homoserine lactone
0.123
N-(3-oxooctanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.256
N-(3-oxooctanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.3
N-dodecanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.345
N-dodecanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.459
N-hexanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.68
N-octanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.145
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.109
nonanoic-1,4-lactone
pH 8.3, 25°C
0.348
nonanoic-1,5-lactone
pH 8.3, 25°C
0.06
nonanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
0.015 - 0.061
nonanoic-gamma-lactone
0.262
octanoyl-L-homoserine lactone
pH 8.3, 40°C
4.3
pantoyl lactone
pH 8.0
0.83
phenyl acetate
pH 8.0, 37°C
0.578
undecanoic-1,4-lactone
pH 8.3, 25°C
0.168
undecanoic-1,5-lactone
pH 8.3, 25°C
0.042 - 0.121
undecanoic-delta-lactone
0.39
undecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
0.013
2-coumaranone
25°C, enzyme variant R192
0.02
2-coumaranone
25°C, enzyme variant Q192
4.55
2-coumaranone
-
pH 7.4, 30°C
0.27
5-(thiobutyl)butyrolactone
pH 8.0, wild-type enzyme
0.68
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H134Q
1.6
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H115Q
1.83
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H115Q/H134Q
0.359
delta-nonalactone
pH 8.3, 25°C, wild-type enzyme
0.812
delta-nonalactone
pH 8.0
1.22
delta-nonalactone
pH 8.3, 40°C
0.057
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
0.094
delta-undecanolactone
pH 8.3, 25°C, wild-type enzyme
0.13
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
0.135
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
0.161
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
0.219
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
0.4
delta-valerolactone
mutant H115W, pH 8.3, 25°C
0.5
delta-valerolactone
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
0.5
delta-valerolactone
mutant H115W/R192K, pH 8.3, 25°C
0.57
delta-valerolactone
-
recombinant enzyme
0.57
delta-valerolactone
pH 8.0
0.57
delta-valerolactone
pH 8.0, wild-type enzyme
0.9
delta-valerolactone
pH 8.3, activity buffer with 0.1% tergitol
0.95
delta-valerolactone
pH 8.0, mutant enzyme H134Q
1
delta-valerolactone
pH 8.3, activity buffer
1.5
delta-valerolactone
wild-type, pH 8.3, 25°C
1.9
delta-valerolactone
25°C, pH not specified in the publication, wild-type enzyme
8.5
delta-valerolactone
pH 8.0, mutant enzyme H115Q
0.013
dihydrocoumarin
25°C, enzyme variant R192
0.022
dihydrocoumarin
25°C, enzyme variant Q192
0.129
dihydrocoumarin
pH 8.0
0.748
dihydrocoumarin
pH 7.0, 37°C
0.84
dihydrocoumarin
pH 8.0, 37°C
1.376
dihydrocoumarin
pH 8.3, 25°C, wild-type enzyme
0.234
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
0.37
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
1.031
epsilon-caprolactone
pH 8.3, 25°C
0.16
gamma-butyrolactone
pH 8.3, 25°C, wild-type enzyme
5.3
gamma-butyrolactone
25°C, enzyme variant R192
6
gamma-butyrolactone
-
-
11.57
gamma-butyrolactone
pH 8.3, temperature not specified in the publication
13.3
gamma-butyrolactone
-
-
15
gamma-butyrolactone
25°C, enzyme variant Q192
21
gamma-butyrolactone
-
recombinant enzyme
21
gamma-butyrolactone
pH 8.0
36.8
gamma-butyrolactone
-
at pH 7.0 and 30°C
0.9
Gamma-caprolactone
-
-
1
Gamma-caprolactone
pH 8.0
1
Gamma-caprolactone
pH 8.0, wild-type enzyme
2.2
Gamma-caprolactone
-
-
2.97
Gamma-caprolactone
pH 8.0, mutant enzyme H134Q
3.7
Gamma-caprolactone
pH 8.3, 40°C
3.8
Gamma-caprolactone
pH 8.0, mutant enzyme H115Q
0.3
gamma-dodecanoic lactone
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
0.7
gamma-dodecanoic lactone
pH 8.3, activity buffer with 0.1% tergitol
0.13
gamma-heptanolide
pH 8.3, 25°C, wild-type enzyme
0.388
gamma-heptanolide
pH 8.3, 25°C
0.58
gamma-heptanolide
pH 8.0
9
Gamma-hydroxyvalerate
-
-
10.4
Gamma-hydroxyvalerate
-
-
20
Gamma-hydroxyvalerate
-
-
0.047
gamma-nonalactone
pH 8.3, 40°C
0.39
gamma-nonalactone
pH 8.0, wild-type enzyme
0.89
gamma-nonalactone
pH 8.0, mutant enzyme H134Q
1.54
gamma-nonalactone
pH 8.0, mutant enzyme H115Q
2.943
gamma-nonalactone
pH 8.3, 25°C, wild-type enzyme
1.3
Gamma-octalactone
-
-
3.1
Gamma-octalactone
-
-
2.8
gamma-thiobutyrolactone
25°C, enzyme variant Q192
3.5
gamma-thiobutyrolactone
25°C, enzyme variant R192
0.013
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
0.334
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
0.361
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263I
0.372
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
0.373
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
1.76
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
2.099
gamma-undecanolactone
pH 8.3, 25°C, wild-type enzyme
3.3
gamma-valerolactone
-
-
4
gamma-valerolactone
-
-
21.2
homocysteine thiolactone
-
isozyme 192R, in 50 mM HEPES (pH 7.4), 37°C
23.5
homocysteine thiolactone
-
isozyme 192Q, in 50 mM HEPES (pH 7.4), 37°C
0.45
Homogentisic acid lactone
25°C, enzyme variant R192
0.52
Homogentisic acid lactone
25°C, enzyme variant Q192
0.143
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.288
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
1
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
1.346
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
1.605
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
0.0178
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
0.0247
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
0.137
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
0.146
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
0.456
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.042
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.917
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K
1
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
1.2
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.015
nonanoic-gamma-lactone
25°C, pH not specified in the publication, wild-type enzyme
0.025
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
0.047
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.061
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.7
paraoxon
pH 8.3, 25°C, mutant enzyme W263F
0.93
paraoxon
pH 8.3, 25°C, mutant enzyme W263M
24.2
paraoxon
pH 8.3, 25°C, wild-type enzyme
0.042
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
0.043
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.121
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
36.621
(R)-gamma-valerolactone
-
at pH 7.0 and 30°C
0.47
3-oxo-decanoyl-L-homoserine lactone
pH 8.3, 40°C
0.35
3-oxo-octanoyl-L-homoserine lactone
pH 8.3, 40°C
39
4-methoxy phenyl acetate
pH 8.0
1.74 - 116
5-(thiobutyl)butyrolactone
4.2
5-butyl-4-methyldihydro-2(3H)-furanone
pH 8.3, temperature not specified in the publication
0.89
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide
pH 8.3, 25°C
1.03
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide
pH 8.3, 25°C
28.08
delta-dodecalactone
pH 8.3, 40°C
15.32 - 88.91
delta-nonalactone
60.78
delta-undecalactone
pH 8.3, 40°C
7.38 - 93.3
delta-undecanolactone
0.43 - 632
delta-valerolactone
7.32 - 152
dihydrocoumarin
0.53
dodecanoic-1,4-lactone
pH 8.3, 25°C
3.34
dodecanoic-1,5-lactone
pH 8.3, 25°C
11.09
dodecanoic-delta-lactone
pH 8.3, 25°C, wild-type enzyme
1.5
dodecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
4.45 - 15.04
epsilon-caprolactone
3.04
gamma-(R)-caprolactone
pH 8.3, temperature not specified in the publication
6.23
gamma-(R)-valerolactone
pH 8.3, temperature not specified in the publication
1.89
gamma-(S)-caprolactone
pH 8.3, temperature not specified in the publication
2.68
gamma-(S)-valerolactone
pH 8.3, temperature not specified in the publication
2.79 - 147.209
gamma-butyrolactone
2.27 - 112.3
Gamma-caprolactone
0.16
gamma-dodecalactone
pH 8.3, 40°C
26.4
gamma-dodecanoic acid lactone
pH 8.0
34 - 101
gamma-dodecanoic lactone
2.72
gamma-dodecanolactone
pH 8.3, 25°C, wild-type enzyme
27.25
gamma-heptalactone
pH 8.3, 40°C
2.92
gamma-heptanolactone
pH 8.3, 25°C, wild-type enzyme
5.9 - 34
gamma-heptanolide
0.38 - 44.49
gamma-nonalactone
31
gamma-nonanoic acid lactone
pH 8.0
8.86
gamma-undecalactone
pH 8.3, 40°C
62
gamma-undecanoic acid lactone
pH 8.0
62
gamma-undecanoiclactone
-
recombinant enzyme
1.94 - 5.64
gamma-undecanolactone
0.94
N-(2-oxotetrahydrofuran-3-yl)pentanamide
pH 8.3, 25°C
10.65
N-(3-oxodecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.107 - 4.52
N-(3-oxodecanoyl)-L-homoserine lactone
0.39
N-(3-oxododecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.41 - 6.44
N-(3-oxododecanoyl)-L-homoserine lactone
0.083
N-(3-oxohexanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.041
N-(3-oxohexanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.85 - 4.1
N-(3-oxooctanoyl)-DL-homoserine lactone
0.54
N-(3-oxooctanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.42
N-(3-oxooctanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.9
N-dodecanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
1.7
N-dodecanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.36
N-hexanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.71
N-octanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
1
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
2.64
nonanoic-1,4-lactone
pH 8.3, 25°C
4.55
nonanoic-1,5-lactone
pH 8.3, 25°C
51.7
nonanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
1.9 - 3.1
nonanoic-gamma-lactone
0.59
octanoyl-L-homoserine lactone
pH 8.3, 40°C
11.9
pantoyl lactone
pH 8.0
0.34
undecanoic-1,4-lactone
pH 8.3, 25°C
1.05
undecanoic-1,5-lactone
pH 8.3, 25°C
12.8 - 17.65
undecanoic-delta-lactone
2.15
undecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
1.74
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H115Q/H134Q
7.5
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H115Q
19.4
5-(thiobutyl)butyrolactone
pH 8.0, mutant enzyme H134Q
116
5-(thiobutyl)butyrolactone
pH 8.0, wild-type enzyme
15.32
delta-nonalactone
pH 8.3, 25°C, wild-type enzyme
48
delta-nonalactone
pH 8.0
88.91
delta-nonalactone
pH 8.3, 40°C
7.38
delta-undecanolactone
pH 8.3, 25°C, wild-type enzyme
12.65
delta-undecanolactone
pH 8.3, 25°C, wild-type enzyme
44.8
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
56.8
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
58
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263I
66.5
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
71.2
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
93.3
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
0.43
delta-valerolactone
25°C, pH not specified in the publication, wild-type enzyme
0.5
delta-valerolactone
mutant H115W, pH 8.3, 25°C
0.9
delta-valerolactone
mutant H115W/R192K, pH 8.3, 25°C
29.8
delta-valerolactone
wild-type, pH 8.3, 25°C
40
delta-valerolactone
pH 8.0, mutant enzyme H134Q
69.4
delta-valerolactone
pH 8.0, mutant enzyme H115Q
94
delta-valerolactone
pH 8.3, activity buffer
156
delta-valerolactone
pH 8.3, activity buffer with 0.1% tergitol
210
delta-valerolactone
-
recombinant enzyme
210
delta-valerolactone
pH 8.0
210
delta-valerolactone
pH 8.0, wild-type enzyme
632
delta-valerolactone
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
7.32
dihydrocoumarin
pH 8.3, 25°C, wild-type enzyme
152
dihydrocoumarin
pH 8.0
4.45
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
7.27
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
15.04
epsilon-caprolactone
pH 8.3, 25°C
2.79
gamma-butyrolactone
pH 8.3, temperature not specified in the publication
5.75
gamma-butyrolactone
pH 8.3, 25°C, wild-type enzyme
111
gamma-butyrolactone
-
recombinant enzyme
111
gamma-butyrolactone
pH 8.0
147.209
gamma-butyrolactone
-
at pH 7.0 and 30°C
2.27
Gamma-caprolactone
pH 8.0, mutant enzyme H115Q
25
Gamma-caprolactone
pH 8.0, mutant enzyme H134Q
44
Gamma-caprolactone
pH 8.0
44
Gamma-caprolactone
pH 8.0, wild-type enzyme
112.3
Gamma-caprolactone
pH 8.3, 40°C
34
gamma-dodecanoic lactone
pH 8.3, activity buffer with 0.1% tergitol
101
gamma-dodecanoic lactone
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
5.9
gamma-heptanolide
pH 8.3, 25°C, wild-type enzyme
10.25
gamma-heptanolide
pH 8.3, 25°C
34
gamma-heptanolide
pH 8.0
0.38
gamma-nonalactone
pH 8.0, mutant enzyme H115Q
5.54
gamma-nonalactone
pH 8.3, 25°C, wild-type enzyme
5.57
gamma-nonalactone
pH 8.0, mutant enzyme H134Q
31
gamma-nonalactone
pH 8.0, wild-type enzyme
44.49
gamma-nonalactone
pH 8.3, 40°C
1.94
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263I
3.92
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
4.25
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
4.55
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
4.63
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
4.95
gamma-undecanolactone
pH 8.3, 25°C, wild-type enzyme
5.64
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
0.107
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
0.19
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
0.6
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
3.96
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
4.52
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.41
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
1.01
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.8
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
3
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
6.44
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
0.85
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K
0.92
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.97
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
4.1
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
1.9
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
1.9
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
2
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
3.1
nonanoic-gamma-lactone
25°C, pH not specified in the publication, wild-type enzyme
6.82
paraoxon
pH 8.3, 25°C, mutant enzyme W263M
8.47
paraoxon
pH 8.3, 25°C, mutant enzyme W263F
12.6
paraoxon
pH 8.3, 25°C, wild-type enzyme
12.8
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
12.9
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
14.1
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
17.65
undecanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
27.82
(R)-gamma-valerolactone
-
at pH 7.0 and 30°C
1.3 - 131.6
2-coumaranone
2.05
3-oxo-decanoyl-L-homoserine lactone
pH 8.3, 40°C
1.88
3-oxo-octanoyl-L-homoserine lactone
pH 8.3, 40°C
4.54
5-butyl-4-methyldihydro-2(3H)-furanone
pH 8.3, temperature not specified in the publication
1.07
7-oxo-N-(2-oxotetrahydrofuran-3-yl)nonanamide
pH 8.3, 25°C
4.88
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide
pH 8.3, 25°C
0.0335
delta-dodecalactone
pH 8.3, 40°C
7.54
delta-dodecanolactone
pH 8.3, 25°C, wild-type enzyme
0.073 - 42.7
delta-nonalactone
0.058
delta-undecalactone
pH 8.3, 40°C
78.6 - 792
delta-undecanolactone
0.22 - 19.8
delta-valerolactone
5.32
dihydrocoumarin
pH 8.3, 25°C, wild-type enzyme
2.21
dodecanoic-1,4-lactone
pH 8.3, 25°C
18.1
dodecanoic-1,5-lactone
pH 8.3, 25°C
89.5
dodecanoic-delta-lactone
pH 8.3, 25°C, wild-type enzyme
3.14
dodecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
14.6 - 19.8
epsilon-caprolactone
5.56
gamma-(R)-caprolactone
pH 8.3, temperature not specified in the publication
1.33
gamma-(R)-valerolactone
pH 8.3, temperature not specified in the publication
2.53
gamma-(S)-caprolactone
pH 8.3, temperature not specified in the publication
1.38
gamma-(S)-valerolactone
pH 8.3, temperature not specified in the publication
0.24 - 36.4
gamma-butyrolactone
0.03
Gamma-caprolactone
pH 8.3, 40°C
0.078
gamma-dodecalactone
pH 8.3, 40°C
2.23
gamma-dodecanolactone
pH 8.3, 25°C, wild-type enzyme
0.031
gamma-heptalactone
pH 8.3, 40°C
17.6
gamma-heptanolactone
pH 8.3, 25°C, wild-type enzyme
26.4 - 46.1
gamma-heptanolide
0.948 - 1.88
gamma-nonalactone
0.074
gamma-undecalactone
pH 8.3, 40°C
2.36 - 349
gamma-undecanolactone
1.11 - 21.2
homocysteine thiolactone
5.28
N-(2-oxotetrahydrofuran-3-yl)pentanamide
pH 8.3, 25°C
96.3
N-(3-oxodecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.106 - 31.6
N-(3-oxodecanoyl)-L-homoserine lactone
0.9
N-(3-oxododecanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
2.2 - 121
N-(3-oxododecanoyl)-L-homoserine lactone
0.15
N-(3-oxohexanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.069
N-(3-oxohexanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.76 - 97
N-(3-oxooctanoyl)-DL-homoserine lactone
4.39
N-(3-oxooctanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.63
N-(3-oxooctanoyl)homoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.004
N-butanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
0.012
N-butanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.46
N-dodecanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
4.9
N-dodecanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.78
N-hexanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
1.05
N-octanoyl-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
6.9
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
24.4
nonanoic-1,4-lactone
pH 8.3, 25°C
13.1
nonanoic-1,5-lactone
pH 8.3, 25°C
828
nonanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
31.3 - 204
nonanoic-gamma-lactone
2.23
octanoyl-L-homoserine lactone
pH 8.3, 40°C
0.59
undecanoic-1,4-lactone
pH 8.3, 25°C
6.22
undecanoic-1,5-lactone
pH 8.3, 25°C
106 - 335
undecanoic-delta-lactone
5.49
undecanoic-gamma-lactone
pH 8.3, 25°C, wild-type enzyme
1.3
2-coumaranone
-
lactonase/human phosphate binding protein (9:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
73.3
2-coumaranone
-
lactonase/human phosphate binding protein (1:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
131.6
2-coumaranone
-
recombinant lactonase, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
0.073
delta-nonalactone
pH 8.3, 40°C
42.7
delta-nonalactone
pH 8.3, 25°C, wild-type enzyme
78.6
delta-undecanolactone
pH 8.3, 25°C, wild-type enzyme
259
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
442
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
492
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
717
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
792
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
0.22
delta-valerolactone
25°C, pH not specified in the publication, wild-type enzyme
1.3
delta-valerolactone
mutant H115W, pH 8.3, 25°C
1.9
delta-valerolactone
mutant H115W/R192K, pH 8.3, 25°C
19.8
delta-valerolactone
wild-type, pH 8.3, 25°C
14.6
epsilon-caprolactone
pH 8.3, 25°C
19
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
19.8
epsilon-caprolactone
pH 8.3, 25°C, wild-type enzyme
0.24
gamma-butyrolactone
pH 8.3, temperature not specified in the publication
1.2
gamma-butyrolactone
pH 8.3, 25°C, wild-type enzyme
4
gamma-butyrolactone
-
at pH 7.0 and 30°C
36.4
gamma-butyrolactone
pH 8.3, 25°C, wild-type enzyme
26.4
gamma-heptanolide
pH 8.3, 25°C
46.1
gamma-heptanolide
pH 8.3, 25°C, wild-type enzyme
0.948
gamma-nonalactone
pH 8.3, 40°C
1.88
gamma-nonalactone
pH 8.3, 25°C, wild-type enzyme
2.36
gamma-undecanolactone
pH 8.3, 25°C, wild-type enzyme
3.2
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
5.37
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263I
10.5
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263L
12.4
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263F
12.7
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
349
gamma-undecanolactone
pH 8.3, 25°C, mutant enzyme W263T
1.11
homocysteine thiolactone
-
isozyme 192Q, in 50 mM HEPES (pH 7.4), 37°C
21.2
homocysteine thiolactone
-
isozyme 192R, in 50 mM HEPES (pH 7.4), 37°C
0.106
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
0.141
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
0.374
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
13.8
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
31.6
N-(3-oxodecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
2.2
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
2.22
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, wild-type enzyme
2.81
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263F
47
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263T
101
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263I
121
N-(3-oxododecanoyl)-L-homoserine lactone
pH 8.3, 25°C, mutant enzyme W263V
0.76
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.93
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K
0.95
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
97
N-(3-oxooctanoyl)-DL-homoserine lactone
25°C, pH not specified in the publication, wild-type enzyme
31.3
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
42.3
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
75.2
nonanoic-gamma-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
204
nonanoic-gamma-lactone
25°C, pH not specified in the publication, wild-type enzyme
0.519
paraoxon
pH 8.3, 25°C, wild-type enzyme
0.883
paraoxon
pH 8.3, 25°C, mutant enzyme W263V
1.06
paraoxon
pH 8.3, 25°C, mutant enzyme W263T
1.21
paraoxon
pH 8.3, 25°C, mutant enzyme W263I
2.37
paraoxon
pH 8.3, 25°C, mutant enzyme W263L
7.33
paraoxon
pH 8.3, 25°C, mutant enzyme W263M
12.1
paraoxon
pH 8.3, 25°C, mutant enzyme W263F
106
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme Y34Q
300
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
335
undecanoic-delta-lactone
25°C, pH not specified in the publication, mutant enzyme E14K
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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
0.0049
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
0.0152
-
substrate gamma-butyrolactone
0.0167
pH 8.0, 25°C, substrate: DL-dodecanoyl-homoserine lactone, 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
0.0334
pH 8.0, 25°C, substrate: DL-3-oxo-hexanoyl-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
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
14.5
pH 8.0, 25°C, substrate: delta-valerolactone, 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
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
251
pH 8.0, 25°C, substrate: delta-decanolactone, 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
287
pH 8.0, 25°C, substrate: delta-undecanolactone, 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
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
341.2
recombinant enzyme after 14.4fold purification, using DL-pantoyl lactone as substrate, at pH 6.7-6.9, 30°C
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
pH 8.0, 25°C, substrate: gamma-valerolactone, purified recombinant enzyme
45.6
pH 8.0, 25°C, substrate: gamma-decanolactone, purified recombinant enzyme
51.7
pH 8.0, 25°C, substrate: gamma-hexalactone, purified recombinant enzyme
549
-
substrate: 5-thiobutyl-butyro-1,4-lactone, pH 8.5, 70°C, Mn2+-containing enzyme
57.2
pH 8.0, 25°C, substrate: gamma-heptalactone, purified recombinant enzyme
6.2
pH 8.0, 25°C, substrate: gamma-valerolactone, 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
71.4
pH 8.0, 25°C, substrate: gamma-undecanolactone, 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
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
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
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
L55M
-
the mutant enzyme shows decreased lactonase activities compared to the wild type
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
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
H115A
activity with 5-(thioethyl)butyrolactone is 1.1% of wild-type activity, activity with 5-(thiobutyl)butyrolactone is 4.2% of wild-type activity, activity with delta-valerolactone, gamma-nonalactone or gamma-undecanoic lactone is less than 1% of wild-type activity
H115Q/H134Q
activity with 5-(thioethyl)butyrolactone is 0.2% compared to wild-type activity, activity with 5-(thiobutyl)butyrolactone is 0.6% of wild-type activity, activity with delta-valerolactone, gamma-nonalactone or gamma-undecanoic lactone is less than 1% of wild-type activity
W263F
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 23.3fold compared to wild-type value. 1.3fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
W263I
mutant exhibits a lower Tm-value compared to the wild-type enzyme. 45.5fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
W263L
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 4.6fold compared to wild-type value
W263M
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 14.1fold compared to wild-type value
W263T
mutant exhibits a lower Tm-value compared to the wild-type enzyme. 21.2fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
W263V
mutant exhibits a lower Tm-value compared to the wild-type enzyme. 54.5fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
W263F
-
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 23.3fold compared to wild-type value. 1.3fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
-
W263I
-
mutant exhibits a lower Tm-value compared to the wild-type enzyme. 45.5fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
-
W263L
-
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 4.6fold compared to wild-type value
-
W263M
-
mutant exhibits a lower Tm-value compared to the wild-type enzyme. Catalytic efficiency (kcat/Km) of paraoxon increases 14.1fold compared to wild-type value
-
W263V
-
mutant exhibits a lower Tm-value compared to the wild-type enzyme. 54.5fold increase in catalytic efficiency (kcat/Km) of N-(3-oxododecanoyl)-L-homoserine lactone
-
E14K
Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
E14K/Y34Q
Tm-value for the mutant enzyme is 4°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
Y34Q
Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
E14K
-
Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
-
Y34Q
-
Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl-paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
-
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
-
the mutant shows a 2fold increase in PON1 activity compared to the wild type enzyme
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
Rodrigo, L.; Gil, F.; Hernandez, A.F.; Lopez, O.; Pla, A.
Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties
Biochem. J.
376
261-268
2003
Rattus norvegicus (Q68FP2)
brenda
Kataoka, M.; Nomura, J.I.; Shinohara, M.; Nose, K.; Sakamoto, K.; Shimizu, S.
Purification and characterization of a novel lactonohydrolase from Agrobacterium tumefaciens
Biosci. Biotechnol. Biochem.
64
1255-1262
2000
Agrobacterium tumefaciens, Agrobacterium tumefaciens AKU 316
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.
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Homo sapiens (P27169)
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Simizu, S.; Ogawa, J.; Kataoka, M.; Kobayashi, M.
Screening of novel microbial enzymes for the production of biologically and chemically useful compounds
New Enzymes for Organic Synthesis
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Fusarium oxysporum
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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.
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Homo sapiens (Q15166)
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Gaidukov, L.; Tawfik, D.S.
High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I
Biochemistry
44
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2005
Homo sapiens (P27169)
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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
Thomas, P.W.; Stone, E.M.; Costello, A.L.; Tierney, D.L.; Fast, W.
The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein
Biochemistry
44
7559-7569
2005
Bacillus thuringiensis serovar kurstaki (P0CJ63), Bacillus thuringiensis serovar kurstaki 4A3 (P0CJ63)
brenda
Khersonsky, O.; Tawfik, D.S.
The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
J. Biol. Chem.
281
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Homo sapiens (P27169), Oryctolagus cuniculus (Q9BGN0)
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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.
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Homo sapiens (P27169), Homo sapiens (Q15165), Homo sapiens (Q15166)
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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.
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2006
Homo sapiens (Q15166)
brenda
Zhang, X.; Xu, J.H.; Xu, Y.; Pan, J.
Isolation and properties of a levo-lactonase from Fusarium proliferatum ECU2002: a robust biocatalyst for production of chiral lactones
Appl. Microbiol. Biotechnol.
75
1087-1094
2007
Fusarium proliferatum
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Gaidukov, L.; Tawfik, D.S.
The development of human sera tests for HDL-bound serum PON1 and its lipolactonase activity
J. Lipid Res.
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2007
Homo sapiens (P27169)
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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
Rozenberg, O.; Shiner, M.; Aviram, M.; Hayek, T.
Paraoxonase 1 (PON1) attenuates diabetes development in mice through its antioxidative properties
Free Radic. Biol. Med.
44
1951-1959
2008
Mus musculus (P52430)
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
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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
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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
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2010
Homo sapiens, synthetic construct
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Chen, B.; Fan, L.; Xu, J.; Zhao, J.; Zhang, X.; Ouyang, L.
Biocatalytic properties of a recombinant Fusarium proliferatum lactonase with significantly enhanced production by optimal expression in Escherichia coli
Appl. Biochem. Biotechnol.
162
744-756
2010
Fusarium proliferatum (B2LYJ5), Fusarium proliferatum
brenda
Chen, B.; Yin, H.F.; Wang, Z.S.; Liu, J.Y.; Xu, J.H.
A new chemo-enzymatic route to chiral 2-hydroxy-4-phenylbutyrates by combining lactonase-mediated resolution with hydrogenation over Pd/C
Chem. Commun. (Camb. )
46
2754-2756
2010
Fusarium proliferatum
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
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2011
Homo sapiens
brenda
Chen, B.; Yin, H.; Wang, Z.; Xu, J.
New synthesis of harzialactone A via kinetic resolution using recombinant Fusarium proliferatum lactonase
Tetrahedron Asymmetry
21
237-240
2010
Fusarium proliferatum
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brenda
Porzio, E.; Di, Gennaro, S.; Palma, A.; Manco, G.
Mn2+ modulates the kinetic properties of an archaeal member of the PLL family
Chem. Biol. Interact.
203
251-256
2013
Sulfolobus acidocaldarius
brenda
Hiblot, J.; Gotthard, G.; Chabriere, E.; Elias, M.
Structural and enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus
PLoS One
7
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2012
Sulfolobus islandicus (C4KKZ9), Sulfolobus islandicus M.16.4 (C4KKZ9)
brenda
Hiblot, J.; Gotthard, G.; Elias, M.; Chabriere, E.
Differential active site loop conformations mediate promiscuous activities in the lactonase SsoPox
PLoS One
8
e75272
2013
Saccharolobus solfataricus (Q97VT7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VT7)
brenda
Hiblot, J.; Gotthard, G.; Champion, C.; Chabriere, E.; Elias, M.
Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia
Acta Crystallogr. Sect. F
69
1235-1238
2013
Vulcanisaeta moutnovskia (F0QXN6), Vulcanisaeta moutnovskia, Vulcanisaeta moutnovskia 768-28 (F0QXN6)
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
Bzdrenga, J.; Hiblot, J.; Gotthard, G.; Champion, C.; Elias, M.; Chabriere, E.
SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase
BMC Res. Notes
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333
2014
Sulfolobus acidocaldarius (Q4J6Z8), Sulfolobus acidocaldarius DSM 639 (Q4J6Z8)
brenda
Kallnik, V.; Bunescu, A.; Sayer, C.; Brsen, C.; Wohlgemuth, R.; Littlechild, J.; Siebers, B.
Characterization of a phosphotriesterase-like lactonase from the hyperthermoacidophilic crenarchaeon Vulcanisaeta moutnovskia
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2014
Vulcanisaeta moutnovskia (F0QXN6), Vulcanisaeta moutnovskia
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Ben-David, M.; Elias, M.; Filippi, J.J.; Dunach, E.; Silman, I.; Sussman, J.L.; Tawfik, D.S.
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2012
synthetic construct
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Charendoff, M.; Shah, H.; Briggs, J.
New insights into the binding and catalytic mechanisms of Bacillus thuringiensis lactonase: insights into B. thuringiensis AiiA mechanism
PLoS ONE
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2013
Bacillus thuringiensis (P0CJ63)
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.
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2013
Homo sapiens (P27169)
brenda
Hiblot, J.; Bzdrenga, J.; Champion, C.; Chabriere, E.; Elias, M.
Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia
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Vulcanisaeta moutnovskia (F0QXN6), Vulcanisaeta moutnovskia, Vulcanisaeta moutnovskia 768-28 (F0QXN6)
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.
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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
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9571-9585
2015
Homo sapiens
brenda