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Enzyme Nomenclature
Information on EC 3.1.1.25 - 1,4-lactonase
for references in articles please use BRENDA:EC3.1.1.25
Word Map on EC 3.1.1.25
- 3.1.1.25
-
quorum
- homoserine
-
quorum-sensing
- sulfolobus
-
n-acylated
- solfataricus
-
quorum-quenching
-
organophosphate
-
ahl-degrading
- phosphotriesterase
-
n-acylhomoserine
-
phosphotriesterase-like
- pectobacterium
- carotovorum
-
autoinducer
- metallo-beta-lactamase
-
acyl-homoserine
-
hyperthermostable
-
bioscavengers
-
ahl-mediated
- veronii
-
n-acyl-l-homoserine
- synthesis
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.1.1.25
-
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RECOMMENDED NAME
GeneOntology No.
1,4-lactonase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
chimeric mammalian dubbed G3C9-8His, obtained using directed evolution via gene shuffling of human, rabbit, rat and mouse genes
-
-
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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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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
-
-
-
?
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
-
-
-
?
N-(3-oxodecanoyl)-DL-homoserine lactone + H2O
N-(3-oxodecanoyl)-DL-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)homoserine lactone + H2O
N-(3-oxohexanoyl)homoserine
-
-
-
?
N-(3-oxooctanoyl)-DL-homoserine lactone + H2O
N-(3-oxooctanoyl)-DL-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-hexanoylhomoserine lactone + H2O
N-hexanoylhomoserine
-
-
-
?
N-octanoyl-DL-homoserine lactone + H2O
octanoyl-homoserine
-
-
-
?
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
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
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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+)
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INHIBITORS
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
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
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
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
-
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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
-
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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
25°C, pH not specified in the publication, wild-type enzyme
0.44
N-(3-oxododecanoyl)-DL-homoserine lactone
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
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
0.06
nonanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
0.5
delta-valerolactone
-
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
1.9
delta-valerolactone
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
0.143
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
0.042
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
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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
25°C, pH not specified in the publication, wild-type enzyme
0.39
N-(3-oxododecanoyl)-DL-homoserine lactone
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
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
51.7
nonanoic-delta-lactone
25°C, pH not specified in the publication, wild-type enzyme
0.43
delta-valerolactone
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
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; 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
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
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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
25°C, pH not specified in the publication, wild-type enzyme
0.9
N-(3-oxododecanoyl)-DL-homoserine lactone
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
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
828
nonanoic-delta-lactone
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
0.22
delta-valerolactone
25°C, pH not specified in the publication, wild-type enzyme
0.24
gamma-butyrolactone
-
pH 8.3, temperature not specified in the publication
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
high density lipoprotein-associated enzyme
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35548
-
and dimer, 1 * 35000, SDS-PAGE, 1 * 35548, mass spectrometry; and monomer, 2 * 35000, SDS-PAGE, 2 * 35548, mass spectrometry
40000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
additional information
dimer
-
and monomer, 2 * 35000, SDS-PAGE, 2 * 35548, mass spectrometry
dimer
-
and monomer, 2 * 35000, SDS-PAGE, 2 * 35548, mass spectrometry
-
monomer
-
and dimer, 1 * 35000, SDS-PAGE, 1 * 35548, mass spectrometry
monomer
-
and dimer, 1 * 35000, SDS-PAGE, 1 * 35548, mass spectrometry
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in order to understand the structural consequences of variations at position 263, the crystal structures of the mutant enzymes (W263F, W263M, W263L, W263I, W263V, W263T) is solved
phosphate ion is bound to the catalytic calcium in the structure of crystallized recombinant G2E6
-
protein at pH 6.5 and in complex with 2-hydroxyquinoline. The models suggest that promiscuity is driven by coincidental overlaps between the reactive intermediate for the native lactonase reaction and the ground and/or intermediate states of the promiscuous reactions. This overlap is also enabled by different active-site conformations: the lactonase activity utilizes one active-site conformation whereas the promiscuous phosphotriesterase activity utilizes another
-
sitting drop vapor diffusion method at 20°C, X-ray structures of the enzyme bound to a fatty acid and to its substrate acyl-homoserine lactone
-
to 2.4 A resolution, space group P64, with unit-cell parameters a=b=174.06, c = 61.32 A. The asymmetric unit contains one homodimer
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
almost 100% activity is maintained during the incubation period of 180 min
649767
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
80
90
additional information
mutant enzymes (W263F, W263M, W263L, W263I, W263V, W263T) exhibit a lower Tm-value compared to the wild-type enzyme
90