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Information on EC 3.1.1.25 - 1,4-lactonase
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3.1.1.25 1,4-lactonaseIUBMB Comments
The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
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Word Map
- 3.1.1.25
-
quorum
- homoserine
-
n-acylated
-
quorum-sensing
- solfataricus
-
ahl-degrading
-
n-acylhomoserine
-
quorum-quenching
-
organophosphate
- pectobacterium
-
phosphotriesterase-like
- phosphotriesterase
- carotovorum
-
hxhxdh
- metallo-beta-lactamase
-
autoinducer
-
bioscavengers
-
acyl-homoserine
- synthesis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
AHL lactonase, AiiA, gamma-lactonase, lactonase, lactonase, gamma, levo-lactonase, Saci_2140, SacPox, SisLac, SSO2522, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AHL lactonase
gamma-lactonase
-
-
-
-
lactonase
lactonase, gamma
-
-
-
-
levo-lactonase
Saci_2140
SacPox
SisLac
SSO2522
SsoPox
VmoLac
VMUT_2255
SisLac
C4KKZ9
the enzyme also shows activity of aryldialkylphosphatase (EC 3.1.8.1) and arylesterase (EC 3.1.1.2)
SisLac
C4KKZ9
the enzyme also shows activity of aryldialkylphosphatase (EC 3.1.8.1) and arylesterase (EC 3.1.1.2)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 1,4-lactone + H2O = a 4-hydroxyacid
-
-
-
-
a 1,4-lactone + H2O = a 4-hydroxyacid
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
1,4-lactone hydroxyacylhydrolase
The enzyme is specific for 1,4-lactones with 4-8 carbon atoms. It does not hydrolyse simple aliphatic esters, acetylcholine, sugar lactones or substituted aliphatic lactones, e.g. 3-hydroxy-4-butyrolactone; requires Ca2+.
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CAS REGISTRY NUMBER
COMMENTARY
37278-38-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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)
-
-
?
(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)
-
-
?
2-bromobutyrolactone + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
2-hydroxybutyrolactone + H2O
?
2450% activity compared to DL-pantoyl lactone
-
-
?
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-phenyl-2-hydroxyl-4-butyrolactone + H2O
?
22% activity compared to DL-pantoyl lactone
-
-
?
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
-
-
-
-
?
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-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-hydroxy-gamma-butyrolactone + H2O
3,4-dihydroxybutanoate
-
-
-
-
?
canrenone + H2O
?
not hydrolyzed by PON1 (P27169 (UniProt)) and PON2 (Q15165 (UniProt))
-
-
?
DL-3-oxo-hexanoyl-homoserine lactone + H2O
DL-3-oxo-hexanoyl-homoserine
-
-
-
?
DL-3-oxo-hexanoylhomoserine lactone + H2O
DL-3-oxo-hexanoylhomoserine
-
-
-
?
DL-tetradecanoyl-homoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoyl-homoserine
-
-
-
?
DL-tetradecanoylhomoserine lactone + H2O
DL-tetradecanoylhomoserine
-
-
-
?
epsilon-caprolactone + H2O
5-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)
-
-
?
ethyl acetate + H2O
?
less than 1% activity compared to DL-pantoyl lactone
-
-
?
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
butyric 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-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenyl-butanoic acid
-
-
-
?
gamma-phenyl-gamma-butyrolactone + H2O
4-hydroxy-4-phenylbutanoic 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
-
-
?
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
C4KKZ9
-
-
-
?
N-(3-oxodecanoyl)-DL-homoserine lactone + H2O
N-(3-oxodecanoyl)-DL-homoserine
C4KKZ9
-
-
-
?
N-(3-oxododecanoyl)-DL-homoserine lactone + H2O
N-(3-oxododecanoyl)-DL-homoserine
C4KKZ9
-
-
-
?
N-(3-oxododecanoyl)-L-homoserine lactone + H2O
N-(3-oxododecanoyl)-L-homoserine
-
-
-
?
N-(3-oxohexanoyl)homoserine lactone + H2O
N-(3-oxohexanoyl)homoserine
-
-
-
?
N-(3-oxooctanoyl)-DL-homoserine lactone + H2O
N-(3-oxooctanoyl)-DL-homoserine
C4KKZ9
-
-
-
?
N-(3-oxooctanoyl)homoserine lactone + H2O
N-(3-oxooctanoyl)homoserine
-
-
-
?
N-butanoyl-DL-homoserine lactone + H2O
N-butanoyl-L-homoserine
C4KKZ9
-
-
-
?
N-butanoylhomoserine lactone + H2O
N-butanoylhomoserine
-
-
-
?
N-dodecanoyl-DL-homoserine lactone + H2O
N-dodecanoyl-DL-homoserine
C4KKZ9
-
-
-
?
N-dodecanoylhomoserine lactone + H2O
N-dodecanoylhomoserine
-
-
-
?
N-hexanoylhomoserine lactone + H2O
N-hexanoylhomoserine
-
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
octanoyl-homoserine
C4KKZ9
-
-
-
?
N-octanoylhomoserine lactone + H2O
N-octanoylhomoserine
-
-
-
?
octanoyl-L-homoserine lactone + H2O
N-octanoyl-L-homoserine
-
-
-
-
?
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)
-
-
?
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)
-
-
?
(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
?
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
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
?
-
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
-
-
-
-
?
3-oxo-octanoyl-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-L-homoserine
-
-
-
-
?
3-oxo-octanoyl-L-homoserine lactone + H2O
N-(3-oxooctanoyl)-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
-
-
-
?
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide + H2O
3-hydroxy-2-[(9-oxoundecanoyl)amino]propanoic acid
-
-
-
?
9-oxo-N-(2-oxotetrahydrofuran-3-yl)undecanamide + H2O
3-hydroxy-2-[(9-oxoundecanoyl)amino]propanoic acid
-
-
-
?
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
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-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)-propionic acid
-
-
-
?
dihydrocoumarin + H2O
3-(2-hydroxyphenyl)-propionic 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-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-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
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
?
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
-
-
-
-
-
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 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
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-(3-oxodecanoyl)-L-homoserine lactone + H2O
N-(3-oxodecanoyl)-L-homoserine
Q97VT7
the best, possibly natural, substrate of wild-type enzyme
-
-
?
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Co2+
Mn2+
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Ni2+
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Zn2+
additional information
Ca2+
7.4% activation at 1 mM. No significant effect of Ca2+ on the stability of recombinant enzyme is observed when incubated together for 60 h at 30°C or 4°C
Ca2+
-
required for the catalysis. Shows a slight protection of 10% at 5 mM on ascorbate/Cu2+-induced inactivation of lactonase activity
Ca2+
-
is essential for activity and stability of lactonase, modulates oligomeric state
Ca2+
-
activates, hydrolysis is maximal at 0.01 mM , lactonization is maximal with 10 mM
Ca2+
Asp269 and Glu53 participate in the ligation of catalytic Ca2+
Ca2+
-
activates, hydrolysis is maximal at 0.01 mM , lactonization is maximal with 10 mM
Co2+
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Zn2+
-
the catalytic activity strictly depended on bivalent cations (Cd2+> Ni2+> Co2+> Mn2+> Zn2+)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
ascorbate/Cu2+ system is the most potent in inactivating the lactonase activity (by 90%). Cu2+ remarkably enhances the inactivation in the presence of ascorbate. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 95% inactivation. Ascorbate/Cu2+-mediated inactivation of lactonase activity is prevented by catalase (90%), oleic acid (73% at 0.01 mM) and dioleoylphosphatidylcholine (68% at 0.1 mM). Ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows 20% inactivation
D-penicillamine
-
32.4% residual activity after 24 h in the presence of 0.2 mg/ml D-penicillamine
delta-undecanolactone
contrary to the wild-type enzyme and mutant enzyme W263F, the mutant enzymes W263M, W263L, W263I, W263V and W263T exhibit a substrate inhibition
diclofenac sodium
-
diclofenac sodium in 0.845 mM dose during 6-12 h of incubation results in a significant decline in the lactonase activity
high density lipoprotein
-
incubation of serum or high density lipoprotein from healthy subjects with very low density lipoprotein significantly decreases serum paraoxonase 1 lactonase or arylesterase activities by up to 11% or 24%, and HDL-associated paraoxonase 1 lactonase or arylesterase activities by up to 32% or 46%, respectively
-
sodium hypochlorite
-
at 1 mM and 10 mM causes approximately 18 and 34% decrease in lactonase activity, respectively
tenoxicam
-
tenoxicam in 0.74mM dose during 6 h of incubation results in a significant decline in the lactonase activity
very low density lipoprotein
-
inhibits recombinant paraoxonase 1 lactonase or arylesterase activities by up to 20% or 42%, respectively
-
Cu2+
-
inhibits in a concentration-dependent manner. Cu2+ alone inhibits the lactonase activity by 30% at concentrations as low as 0.001 mM. Ascorbate/Cu2+ system is the most potent in inactivating the lactonase activity (by 90%). Cu2+ remarkably enhances the inactivation in the presence of ascorbate. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 95% inactivation. Ascorbate/Cu2+-mediated inactivation of lactonase activity is prevented by catalase (90%), oleic acid (73% at 0.01 mM) and dioleoylphosphatidylcholine (68% at 0.1 mM)
Fe2+
-
ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows 20% inactivation. Fe2+ alone shows no inhibition
Mg2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Mg2+
Mg2+
-
only inhibition of hydrolytic activity without affecting its lactonizing function
Mg2+
-
only inhibition of hydrolytic activity without affecting its lactonizing function
Zn2+
activity is strongly reduced when Ca2+ is removed from the purified enzyme and replaced by Zn2+
additional information
EDTA does not exhibit significant effect on enzyme activity
-
additional information
-
EDTA does not exhibit significant effect on enzyme activity
-
additional information
-
neither ascorbate alone nor Mn2+, Zn2+, Co2+ or 3-morpholinosydnoimine cause a significant loss of lactonase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
apolipoprotein apoA-I
-
only apolipoprotein apoA-I is capable of stimulating the lactonase activity, while apoA-IV and apoA-II have almost no effect
-
dilauroyl phosphatidylcholine
stimulates activity of enzyme variants Q192 and R192
additional information
-
pomegranate juice and pomegranate polyphenol extract (from variety Wonderful) consumption contributes to PON1 stabilization, increased association with high density lipoprotein, and enhanced catalytic activity
-
additional information
-
binding of human phosphate binding protein amends the size of the oligomeric states and exerts a stabilizing effect on the activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
290.2
2-hydroxybutyrolactone
recombinant enzyme, at pH 6.7-6.9, 30°C
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
0.55
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
0.1
N-(3-oxodecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.44
N-(3-oxododecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
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
0.123
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
C4KKZ9
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.145
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
0.06
nonanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.057
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
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
0.5
delta-valerolactone
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
1.9
delta-valerolactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
11.57
gamma-butyrolactone
-
pH 8.3, temperature not specified in the publication
0.3
gamma-dodecanoic lactone
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
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
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.917
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
1
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
1.2
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.015
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.025
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
0.047
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.061
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.042
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
0.043
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.121
undecanoic-delta-lactone
C4KKZ9
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.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
10.65
N-(3-oxodecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.39
N-(3-oxododecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
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
0.54
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
C4KKZ9
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
1
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
51.7
nonanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, 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
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
632
delta-valerolactone
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
2.79
gamma-butyrolactone
-
pH 8.3, temperature not specified in the publication
101
gamma-dodecanoic lactone
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
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
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
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
0.92
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.97
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
4.1
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
1.9
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K; 25°C, pH not specified in the publication, mutant enzyme Y34Q
2
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
3.1
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
12.8
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
12.9
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
14.1
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
17.65
undecanoic-delta-lactone
C4KKZ9
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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
96.3
N-(3-oxodecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.9
N-(3-oxododecanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
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
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
C4KKZ9
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
C4KKZ9
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
6.9
N-octanoylhomoserine lactone
pH 8.3, 25°C, wild-type enzyme
828
nonanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, 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
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
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
0.24
gamma-butyrolactone
-
pH 8.3, temperature not specified in the publication
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
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
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.93
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
0.95
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
97
N-(3-oxooctanoyl)-DL-homoserine lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
31.3
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
42.3
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
75.2
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
204
nonanoic-gamma-lactone
C4KKZ9
25°C, pH not specified in the publication, wild-type enzyme
106
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme Y34Q
300
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
335
undecanoic-delta-lactone
C4KKZ9
25°C, pH not specified in the publication, mutant enzyme E14K
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.789
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263V
7.4
delta-undecanolactone
pH 8.3, 25°C, mutant enzyme W263M
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
0.0167
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
0.4239
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
3.1
pH 8.0, 25°C, substrate: dihydrocoumarin, purified recombinant enzyme
6.2
pH 8.0, 25°C, substrate: gamma-valerolactone, 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
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
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
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
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
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
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
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
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
549
-
substrate: 5-thiobutyl-butyro-1,4-lactone, pH 8.5, 70°C, Mn2+-containing enzyme
671
pH 8.0, 25°C, substrate: delta-valerolactone, 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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
pH 5.0: about 55% of maximal activity, pH 10.0: about 35% of maximal activity
6 - 9.6
pH 6.0: about 70% of maximal activity, pH 9.6: about 55% of maximal activity, hydrolysis of dihydrocoumarin
7 - 9
-
pH 7.0: about 30% of maximal activity, pH 9.0: about 80% of maximal activity, substrate: methyl paraoxon
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
32
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 37
70 - 90
-
70°C: about 60% of maximal activity, 90°C: about 50% of maximal activity, substrate: methyl paraoxon
15 - 37
-
15°C: about 65% of maximal activity, 37°C: about 90% of maximal activity
15 - 37
-
15°C: about 65% of maximal activity, 37°C: about 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
-
695051, 702421, 709261, 715735, 729341, 749628, 749762, 750345, 750428, 750462, 750511, 751389, 94285, 94286
-
-
brenda
chimeric mammalian dubbed G3C9-8His, obtained using directed evolution via gene shuffling of human, rabbit, rat and mouse genes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
high density lipoprotein-associated enzyme
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the presence of a particular amino acid residue at position 192 differentially alters the effect of the H115W substitution, and the H115 residue is not always needed for the lactonase and arylesterase activities of the enzyme. The amino acid residues at position 192 and 115 act in conjunction in modulating the hydrolytic activities of the enzyme
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A1C3TPK5_XANCT
307
0
33059
TrEMBL
A0A017H8B9_9RHOB
287
0
31507
TrEMBL
A0A0J9E0Q3_9RHOB
268
0
29666
TrEMBL
A2R8C2_ASPNC
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
429
1
46245
TrEMBL
W4S9J8_9XANT
303
0
33550
TrEMBL
B0RTW2_XANCB
Xanthomonas campestris pv. campestris (strain B100)
303
0
33653
TrEMBL
A0A017HKG9_9RHOB
286
0
31346
TrEMBL
AHLLA_BACTK
250
0
28220
Swiss-Prot
PHP_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
314
0
35565
Swiss-Prot
Q4J6Z8_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
315
0
35308
TrEMBL
F0QXN6_VULM7
Vulcanisaeta moutnovskia (strain 768-28)
315
0
35458
TrEMBL
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Mycoplasma synoviae (strain 53)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE