Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Homo sapiens and UniProt Accession P27169

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-

?

1-methylethyl 4-methyl-2-oxo-2H-chromen-7-yl methylphosphonate + H2O

?

-

-

?

2,4-dinitrophenyl diethyl phosphate + H2O

2,4-dinitrophenol + diethyl phosphate

-

-

?

2,6-difluorophenyl diethyl phosphate + H2O

2,6-difluorophenol + diethyl phosphate

-

-

?

2-fluoro-4-nitrophenyl diethyl phosphate + H2O

2-fluoro-4-nitrophenol + diethyl phosphate

-

-

?

2-methylpropyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl methylphosphonate + H2O

?

-

-

?

2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl N,N,N',N'-tetramethyldiamidophosphate + H2O

?

-

-

?

3,5-dinitrophenyl diethyl phosphate + H2O

3,5-dinitrophenol + diethyl phosphate

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl 1-methylethyl methylphosphonate + H2O

?

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl 2-methylpropyl methylphosphonate + H2O

?

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl cyclohexyl methylphosphonate + H2O

?

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl diethyl phosphate + H2O

?

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl dimethyl phosphate + H2O

?

-

-

?

3-chloro-4-methyl-2-oxo-2H-chromen-7-yl ethyl methylphosphonate + H2O

3-chloro-7-hydroxy-4-methyl-2H-chromen-2-one + ethyl methylphosphonate

-

-

?

3-cyanophenyl diethyl phosphate + H2O

3-cyanophenol + diethyl phosphate

-

-

?

3-fluoro-4-nitrophenyl diethyl phosphate + H2O

3-fluoro-4-nitrophenol + diethyl phosphate

-

-

?

3-fluorophenyl diethyl phosphate + H2O

3-fluorophenol + diethyl phosphate

-

-

?

3-nitrophenyl diethyl phosphate + H2O

3-nitrophenol + diethyl phosphate

-

-

?

4-acetoxy acetophenone + H2O

?

-

-

?

4-chlorophenyl diethyl phosphate + H2O

4-chlorophenol + diethyl phosphate

-

-

?

4-cyanophenyl diethyl phosphate + H2O

4-cyanophenol + diethyl phosphate

-

-

?

4-diethyl phosphate acetophenone + H2O

4-hydroxyacetophenone + diethyl phosphate

-

-

?

4-diethyl phosphate benzaldehyde + H2O

4-hydroxybenzaldehyde + diethyl phosphate

-

-

?

4-diethyl phosphate methyl benzoate + H2O

methyl 4-hydroxybenzoate + diethyl phosphate

-

-

?

4-methyl-2-oxo-2H-chromen-7-yl 2-methylpropyl methylphosphonate + H2O

2-methylpropyl methylphosphonate + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one

-

-

?

4-methyl-2-oxo-2H-chromen-7-yl N,N,N',N'-tetramethyldiamidophosphate + H2O

N,N,N',N'-tetramethylphosphorodiamidic acid + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one

-

-

?

4-nitrophenyl diethyl phosphate + H2O

4-nitrophenol + diethyl phosphate

-

-

?

5-(thiobutyryl)butyrolactone + H2O

?

-

-

?

7-diethylphosphoro-3-cyanocoumarin + H2O

3-cyanocoumarin + diethyl phosphate

-

-

?

7-O-diethylphosphoryl-3-cyano-7-hydroxycoumarin + H2O

?

-

-

?

9-(2,4-dimethylphenoxycarbonyl)-10-methylacridinium triflate + H2O

?

synthesis method, overview. The assay is based on the PON1-mediated hydrolysis of an acridinium ester, and the hydrolysis is monitored by chemiluminescence decrease after incubation with PON enzyme

-

?

9-(4-chlorophenoxycarbonyl)-10-methylacridinium triflate + H2O

?

synthesis method, overview. The assay is based on the PON1-mediated hydrolysis of an acridinium ester, and the hydrolysis is monitored by chemiluminescence decrease after incubation with PON enzyme

-

?

9-(4-methylphenoxycarbonyl)-10-methylacridinium triflate + H2O

?

synthesis method, overview. The assay is based on the PON1-mediated hydrolysis of an acridinium ester, and the hydrolysis is monitored by chemiluminescence decrease after incubation with PON enzyme

-

?

9-(4-tert-butylphenoxycarbonyl)-10-methylacridinium triflate + H2O

?

synthesis method, overview. The assay is based on the PON1-mediated hydrolysis of an acridinium ester, and the hydrolysis is monitored by chemiluminescence decrease after incubation with PON enzyme

-

?

9-(phenyloxycarbonyl)-10-methylacridinium triflate + H2O

?

synthesis method, overview. The assay is based on the PON1-mediated hydrolysis of an acridinium ester, and the hydrolysis is monitored by chemiluminescence decrease after incubation with PON enzyme

-

?

benzyl acetate + H2O

?

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-

?

bis(1-methylethyl) 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl phosphate + H2O

dipropan-2-yl phosphate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one

-

-

?

bis(1-methylethyl) 4-methyl-2-oxo-2H-chromen-7-yl phosphate + H2O

dipropan-2-yl phosphate + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one

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-

?

chlorpyrifos + H2O

3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate

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-

?

chlorpyrifos + H2O

?

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-

?

chlorpyrifos oxon + H2O

3,5,6-trichloro-pyridin-2-ol + diethyl phosphate

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-

?

chlorpyrifos oxon + H2O

?

-

646528

-

?

chlorpyrifos oxon + H2O

diethyl phosphate + 3,5,6-trichloropyridin-2-ol

chlorpyrifos-oxon + H2O

3,5,6-trichloro-2-pyridinol + diethyl phosphate

-

691863, 693354, 695193

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?

chlortion + H2O

?

chlorthion is O,O-dimethyl O-(3-chloro-4-nitrophenyl) thionophosphate

-

?

cyclohexyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl methylphosphonate + H2O

cyclohexyl methylphosphonate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one

-

-

?

cyclohexyl 4-methyl-2-oxo-2H-chromen-7-yl methylphosphonate + H2O

cyclohexyl methylphosphonate + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one

-

-

?

cyclosarin + H2O

?

-

-

?

diazoxon + H2O

2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate

diazoxon + H2O

?

diethyl (3,5,6-trichloropyridin-2-yl) phosphate + H2O

?

i.e. chlorpyrifos-oxon or CPO

-

?

diethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl phosphate + H2O

diethyl phosphate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one

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-

?

diethyl 4-chlorophenyl phosphate + H2O

4-chlorophenol + diethyl phosphate

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?

diethyl-paraoxon + H2O

diethyl phosphate + 4-nitrophenol

diisopropyl fluorophosphate + H2O

?

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?

diisopropyl fluorophosphate + H2O

diisopropyl phosphate + fluoride

diisopropyl fluorophosphate + H2O

isopropanol + ?

-

730898

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?

dimethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl phosphate + H2O

dimethyl phosphate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one

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-

?

dimethyl 4-methyl-2-oxo-2H-chromen-7-yl phosphate + H2O

?

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?

dimethyl-paraoxon + H2O

dimethyl phosphate + 4-nitrophenol

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?

ethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl methylphosphonate + H2O

ethyl methylphosphonate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one

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-

?

ethyl 4-methyl-2-oxo-2H-chromen-7-yl methylphosphonate + H2O

ethyl methylphosphonate + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one

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-

?

ethyl acetate + H2O

?

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-

?

methylphosphonic acid + H2O

?

i.e. MPA, according to the C-P lyase pathway, methylphosphonic acid decomposition by the enzyme is expected to yield methane as a product. But no methane is detected during the reaction process. Methanol cannot be detected either during the MPA decomposition reaction, as well as formaldehyde, but formic acid is identified in the reaction mixture

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?

N-[2-[ethoxy(methyl)phosphoryl]sulfanethyl]-N-propan-2-ylpropan-2-amine + H2O

S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol

the enzyme shows only minimal activity against the nerve agent VX

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?

O,O'-(diisobutyl)methylphosphonate + H2O

?

-

-

?

O,O-dimethyl O-(4-methyl-2-oxo-2H-chromen-7-yl) thiophosphate + H2O

?

-

-

?

O,O-dimethyl O-[2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl] thiophosphate + H2O

?

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-

?

O-(isobutyl)methylphosphonate + H2O

?

very low activity

-

?

O-ethyl O-4-nitrophenyl phenylphosphonothioate + H2O

?

-

-

?

O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate + H2O

?

-

-

?

paraoxon + H2O

4-nitrophenol + diethyl phosphate

10 entries

paraoxon + H2O

4-nitrophenol + diethylphosphate

-

671006

-

?

paraoxon + H2O

diethyl phosphate + 4-nitrophenol

-

750287, 750290

-

?

paraoxon + H2O

diethylphosphate + 4-nitrophenol

22 entries

parathion + H2O

diethyl thiophosphate + 4-nitrophenol

-

-

?

pentafluorophenyl diethyl phosphate + H2O

?

-

-

?

pentafluorophenyl diethyl phosphate + H2O

pentafluorophenol + diethyl phosphate

-

-

?

phenyl acetate + H2O

phenol + acetate

sarin + H2O

?

sarin + H2O

methyl-phosphonic acid monofluoride + isopropyl alcohol

PON1 hydrolyzes sarin more effectively than paraoxon, sarin is o-isopropyl methylphosphonofluoridate

-

?

soman + H2O

?

soman + H2O

methylphosphonofluoride acid + 3,3-dimethylbutan-2-ol

PON1 hydrolyzes soman more effectively than paraoxon, soman is o-pinacolyl methylphosphonofluoridate

-

?

SP-CMP + H2O

?

tabun + H2O

?

-

-

?

1-methylethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O

4-nitrophenol + 1-methylethyl hydrogen (1-methylpropyl)phosphonate

low activity

-

?

1-methylethyl 4-nitrophenyl methylphosphonate + H2O

4-nitrophenol + 1-methylethyl hydrogen methylphosphonate

-

-

?

1-methylpropyl 4-nitrophenyl methylphosphonate + H2O

4-nitrophenol + 1-methylpropyl hydrogen methylphosphonate

best substrate

-

?

1-palmitoyl-2-(5-oxo)valeroyl-sn-glycero-3-phosphocholine + H2O

lysophosphatidylcholine + ?

-

-

?

1-palmitoyl-2-(9-oxo)nonanoyl-sn-glycero-3-phosphocholine + H2O

?

-

-

?

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate + H2O

4-acetylphenol + (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

-

-

?

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate + H2O

4-acetylphenol + (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

-

-

?

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (R)-methylphosphonate + H2O

4-acetylphenol + 4-acetylphenol + (2S)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

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-

?

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate + H2O

4-acetylphenol + (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

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?

4-acetylphenyl 2-methylpropyl (R)-methylphosphonate + H2O

4-acetylphenol + 2-methylpropyl (R)-methylphosphonate

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-

?

4-acetylphenyl 2-methylpropyl (S)-methylphosphonate + H2O

4-acetylphenol + 2-methylpropyl (S)-methylphosphonate

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-

?

4-acetylphenyl cyclohexyl (R)-methylphosphonate + H2O

4-acetylphenol + cyclohexyl (R)-methylphosphonate

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?

4-acetylphenyl cyclohexyl (S)-methylphosphonate + H2O

4-acetylphenol + cyclohexyl (S)-methylphosphonate

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?

4-acetylphenyl ethyl (R)-methylphosphonate + H2O

4-acetylphenol + ethyl (R)-methylphosphonate

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?

4-acetylphenyl ethyl (S)-methylphosphonate + H2O

4-acetylphenol + ethyl (S)-methylphosphonate

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?

4-acetylphenyl propan-2-yl (R)-methylphosphonate + H2O

4-acetylphenol + propan-2-yl (R)-methylphosphonate

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?

4-acetylphenyl propan-2-yl (S)-methylphosphonate + H2O

4-acetylphenol + propan-2-yl (S)-methylphosphonate

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?

4-nitrophenyl phenyl methylphosphonate + H2O

4-nitrophenol + phenyl hydrogen methylphosphonate

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?

4-nitrophenyl phosphate + H2O

4-nitrophenol + phosphate

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?

4-nitrophenyl propyl methylphosphonate + H2O

4-nitrophenol + propyl hydrogen methylphosphonate

best substrate

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?

7-diethylphospho-6,8-difluor-4-methylumbelliferyl + H2O

diethylphosphate + 6,8-difluor-4-methylumbelliferol

-

high level of hydrolysis of the fluorogenic substrate, fluorescence assay method optimization

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?

chlorpyrifos-oxon + H2O

?

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35219

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?

chlorpyrifosoxon + H2O

3,5,6-trichloro-pyridin-2-ol + diethyl phosphate

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?

chlorpyriphosoxon + H2O

?

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?

CVX + H2O

?

-

i.e. diethylamino-ethyl-O-butyl methylphosphonothioate

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?

cyclosarin + H2O

?

-

665987, 714216

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?

cyclosarin + H2O

methyl-phosphonic acid monofluoride + cyclohexanol

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?

diazoxon + H2O

6-methyl-2-(1-methylethyl)pyrimidin-4-ol + diethyl phosphate

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664630

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ir

diazoxon + H2O

?

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?

diethyl 4-nitrophenyl phosphate + H2O

4-nitrophenol + diethyl hydrogen phosphate

low activity

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?

diethyl 4-nitrophenyl phosphate + H2O

4-nitrophenol + diethyl phosphate

diethyl 4-nitrophenyl phosphate + H2O

p-nitrophenol + diethyl phosphate

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752150

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?

diethyl paraoxon + H2O

?

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?

diisopropyl fluorophosphate + H2O

?

diisopropylfluorophosphate + H2O

?

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?

dimethyl paraoxon + H2O

?

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?

ethyl 1-methylethyl 4-nitrophenyl phosphate + H2O

4-nitrophenol + ethyl 1-methylethyl hydrogen phosphate

low activity

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?

ethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O

4-nitrophenol + ethyl hydrogen (1-methylpropyl)phosphonate

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?

ethyl 4-nitrophenyl methylphosphonate + H2O

4-nitrophenol + ethyl hydrogen methylphosphonate

low activity

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?

ethyl paraoxon + H2O

4-nitrophenol + diethyl phosphate

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?

fenitroxon + H2O

?

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?

methyl paraoxon + H2O

4-nitrophenol + dimethyl phosphate

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methyl paraoxon + H2O

4-nitrophenol + dimethylphosphate

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the enzyme reaction also produces two protons, which lower the pH and establish a steady pH gradient

677515

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?

methyl parathion + H2O

dimethyl thiophosphate + 4-nitrophenol

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679074

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?

mono(diethylphosphoryl)obidoxime + H2O

diethyl hydrogenphosphate + obidoxime

-

substrate is a potent inhibitor of human acetylcholinesterase

667551

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?

nitrophenyl isopropyl methylphosphonate + H2O

nitrophenol + propan-2-yl hydrogen methylphosphonate

-

a series of substituted phenoxyalkyl pyridinium oximes enhance the degradation of surrogates of sarin (i.e. nitrophenyl isopropyl methylphosphonate, NIMP) and VX (i.e. nitrophenyl ethyl methylphosphonate, NEMP). Neither NIMP nor NEMP is hydrolyzed effectively by paraoxonase PON1 if one of these oximes is absent. In the presence of eight novel oximes, PON1-mediated degradation of both surrogates occurs

731000

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?

O,O-diethyl O-4-nitrophenyl phosphate + H2O

4-nitrophenol + diethyl phosphate

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750340

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?

O-ethyl S-(2-diisopropylaminoethyl) methylphosphonothioate + H2O

?

-

i.e. VX, a highly toxic organophosphorus nerve agent, stereospecific hydrolysis

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?

O-ethyl-S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + H2O

S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol

-

hydrolysis is exclusively preferential for the P+ isomer. Glycosylation state of PON1 does not affect substrate stereoselectivity

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?

O-ethyl-S-[2-(diisopropylamino)ethyl]methylphosphonothioate + H2O

S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol

-

O-ethyl-S-[2-(diisopropylamino)ethyl]methylphosphonothiate's lone oxygen atom has a strong preference for forming a direct electrostatic interaction with PON1's active site calcium ion. Key residues, which interact with VX are E53, H115, N168, F222, N224, L240, D269, I291, F292, and V346. Residue D183 located in PON1's active site may act as a proton donor or accepter during hydrolysis. PON1's flexible loop region acts as a gatekeeper to the active site residues required for binding VX

709584

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?

O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid + H2O

?

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hydrolysis is exclusively preferential for the P+ isomer. Glycosylation state of PON1 does not affect substrate stereoselectivity

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?

paraoxon + H2O

4-nitrophenol + diethyl phosphate

7 entries

paraoxon + H2O

4-nitrophenol + diethylphosphate

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35208, 35212, 35215, 35216

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?

paraoxon + H2O

diethyl phosphate + 4-nitrophenol

-

paraoxon is diethyl 4-nitrophenyl phosphate

714759

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?

paraoxon + H2O

diethylphosphate + 4-nitrophenol

paraoxon ethylene + H2O

4-nitrophenol + diethyl phosphate

-

-

?

phenyl acetate + H2O

phenol + acetate

phosphatidylcholine isoprostane + H2O

?

-

-

?

russian VX + H2O

methyl-phosphonothioic acid S-(2-diethylamino-ethyl) ester + 2-methylpropanol

-

-

?

sarin + H2O

?

sarin + H2O

methyl-phosphonic acid monofluoride + isopropyl alcohol

-

-

?

sarin + H2O

methylphosphonofluoride acid + ?

-

a highly toxic organophosphorus nerve agent, stereospecific hydrolysis

-

?

soman + H2O

?

soman + H2O

methyl-phosphonic acid monofluoride + 1,2,2-trimethylpropanol

-

-

?

soman + H2O

methylphosphonofluoride acid + 3,3-dimethylbutan-2-ol

-

i.e. pinacolyl methylphosphonofluoridate, a highly toxic organophosphorus nerve agent, stereospecific hydrolysis

-

?

tabun + H2O

?

tabun + H2O

cyanophosphonic acid dimethylamide + ethanol

-

-

?

VR + H2O

?

VX + H2O

?

VX + H2O

S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol

-

-

?

additional information

?

-

47 entries

chlorpyrifos oxon + H2O

diethyl phosphate + 3,5,6-trichloropyridin-2-ol

-

-

?

diethyl-paraoxon + H2O

diethyl phosphate + 4-nitrophenol

dimethyl-paraoxon + H2O

dimethyl phosphate + 4-nitrophenol

-

-

?

paraoxon + H2O

diethyl phosphate + 4-nitrophenol

-

750287, 750290

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?

parathion + H2O

diethyl thiophosphate + 4-nitrophenol

-

-

?

SP-CMP + H2O

?

SP-CMP is the toxic SP enantiomer of a cyclosarin surrogate in which the fluoride leaving group is replaced by a coumarin derivative

-

?

additional information

?

-

Ca2+

Co2+

activates, required

NaCl

activation effects of NaCl on PON1 activity and serum arylesterase activity, kinetics, overview

Ca2+

12 entries

CaCl2

-

added to optimized fluorescence assay

Cd2+

-

Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+

646527

Mn2+

the enzyme is activated with 0.025 mM Mn2+ at 37°C for 1 h

NaCl

Zn2+

additional information

1-myristoyl-lysophosphatidylglycerol

selective, noncompetitive inhibition of paraoxonase activity

1-palmitoyl-lysophosphatidylglycerol

selective, noncompetitive inhibition of paraoxonase activity, charge interactions, inhibition is almost completely suppressed by 1 M NaCl

1-stearoyl-lysophosphatidylglycerol

selective, noncompetitive inhibition of paraoxonase activity

2-hydroxyquinoline

a specific reversible competitive inhibitor of h-PON1 that is known to bind in the active site of the enzyme and inhibit the hydrolytic activities of the enzyme

citalopram

PON1 activity decreases before and after treatment with citalopram compared with control

691852

diisopropylfluorophosphate

-

664885

dimyristoylphosphatidic acid

0.4 mM, 81% inhibition of arylesterase activity, 64% inhibition of paraoxonase activity

dimyristoylphosphatidylethanol

0.2 mM, 20% inhibition of paraoxonase activity, no effect on arylesterase activity

dimyristoylphosphatidylglycerol

activates the arylesterase activity and inhibits paraoxonase activity

dimyristoylphosphatidylserine

no significant inhibition of both activities up to 0.030 mM, remarkable inhibition of both activities at 0.10.4 mM, with a greater inhibition of arylesterase activity

EDTA

etomidate

non-competitive inhibitor, PON1 is significantly inhibited by 0.3 mg/kg etomidate for up to 5 min following intravenous administration

Ketamine

uncompetitive inhibitor, PON1 is significantly inhibited by 1 mg/kg ketamine for up to 5 min following intravenous administration

lysophosphatidylinositol

inhibition of paraoxonase

methylphosphonic acid

possibly inhibits the enzyme, substrate inhibition

nitrilotriacetic acid

-

nitrite

1 mM nitrite inhibits 23% of PON-1 activity, while 6 mM represses 85% of the enzyme activity, the inhibition of PON-1 activity by nitrite is significantly reduced by tryptophan, reduced glutathione, and catalase additions

phenyl acetate

-

phosphatidylinositol

enhances arylesterase activity, but slightly decreases paraoxonase activity

propofol

competitive inhibitor, PON1 is significantly inhibited by 2 mg/kg propofol for up to 5 min following intravenous administration

1-(4-chlorophenyl)-4-(dimethylamino)butan-1-ol

-

1-biphenyl-4-yl-3-(dimethylamino)propan-1-one

-

2-(4-[[2-methoxy-5-(methylsulfonyl)phenyl]carbonyl]piperazin-1-yl)ethanol

-

2-hydroxyquinoline

6,7-dihydroxy-3-(2-methylphenyl)-2H-chromen-2-one

-

noncompetitive

6,7-dihydroxy-3-(3-methylphenyl)-2H-chromen-2-one

-

noncompetitive

6,7-dihydroxy-3-(4-methylphenyl)-2H-chromen-2-one

-

uncompetitive

6,7-dihydroxycoumarin

-

uncompetitive

6-palmityl-ascorbic acid

-

7-(4-methylbenzyl)-7H-pyrrolo[3,2-f]quinazoline-1,3-diamine

-

acetaminophen

-

at 37°C, 5% slightly reduces activity by 18% concentration

acetone

-

at 37°C, 1 mM reduces activity by 82%

acetyl salicylic acid

-

at 37°C, 5% slightly reduces activity by 10% concentration

ascorbate

-

0.5 mM inhibits by ca. 22%. Ascorbate/Cu2+ (0.5 mM/0.001 mM) system shows ca. 63% inactivation

beta-mercaptoethanol

-

at 37°C, 1 mM reduces activity by 52%

Cd2+

CdCl2

-

60.6% residual activity after 24 h in the presence of 0.02 mg/ml CdCl2

cefazolin

-

inhibits the serum and liver PON1, competitive inhibition

chloramphenicol

Ciprofloxacin

-

IC50 of 0.02175 mg/ml 6 h after the drug application

715744

clarithromycin

clindamiycin phosphate

-

IC50 of 0.2395 mg/ml 6 h after the drug application

Co2+

Cu2+

D-penicillamine

-

20.2% residual activity after 24 h in the presence of 0.2 mg/ml D-penicillamine

diclofenac sodium

-

uncompetitive inhibition

diethyldicarbonate

-

dimethyl sulfoxide

-

at 37°C, 5% completely inhibits activity

dimethylformamide

-

at 37°C, 5% completely inhibits activity

EDTA

ethanol

-

at 37°C, 1 mM reduces activity by 43%

Fe2+

-

ascorbate/Fe2+ (0.5 mM/0.002 mM) system shows ca. 27% inactivation after 30 min

gentamicin sulfate

-

at 37°C, 0.6 mg/ml reduces activity by 50%

gentamycin sulfate

-

inhibits the serum and liver PON1, noncompetitive inhibition

Hg2+

-

noncompetitive inhibition of isoenzymes Q192 and R192

indomethacin

-

competitive inhibition

iodoacetic acid

-

at 37°C, 5% completely inhibits activity

kanamycin sulfate

-

at 37°C, 0.6 mg/ml reduces activity by 50%

Ketoprofen

-

noncompetitive inhibition

lincomycine

-

uncompetitive inhibition, weakest inhibitor

lornoxicam

-

uncompetitive inhibition, strongest inhibitor

Mn2+

-

competitive inhibition of isoenzyme Q192 and R192

Ni2+

p-hydroxymercuribenzoate

Pb2+

-

at 37°C, 1 mM reduces activity by 35%

phosphatidylserine

-

rifamycin SV

-

IC50 of 0.00265 mg/ml 6 h after the drug application

715744

sodium ampicillin

Sodium dodecyl sulfate

-

at 37°C, 5% completely inhibits activity

sodium hypochlorite

-

at 1 mM and in the presence of PBS buffer causes approximately 49% decrease in activity

streptomycin sulfate

-

at 37°C, 0.6 mg/ml reduces activity by 50%

tenoxicam

-

competitive inhibition

Zn2+

-

at 37°C, 1 mM reduces activity by 70%

additional information

-

aspirin

induces paraoxonase 1 expression and stimulates enzymatic activity

693517

didecanoylphosphatidylcholine

stimulation of arylesterase activity is greater than stimulation of paraoxonase activity

dilauroylphosphatidylcholine

stimulation of arylesterase activity is greater than stimulation of paraoxonase activity

dimyristoylphosphatidylcholine

stimulation of arylesterase activity is greater than stimulation of paraoxonase activity

dipalmitoylphosphatidylcholine

stimulation of arylesterase activity is greater than stimulation of paraoxonase activity

high-density lipoprotein

paraoxonase and arylesterase activities are stimulated by high-density lipoprotein by 2-5fold, almost independently of the apoliporotein content

664064

-

palmitoyl-lysophosphatidylglycerol

0.01 mM, 14% stimulation of paraoxonase, 40% stimulation of diazoxonase

salicylic acid

induces paraoxonase 1 expression and stimulates enzymatic activity

693517

Ca2+

-

required

dilauroyl phosphatidylcholine

-

stimulation

dioleoyl phosphatidylcholine

-

stimulation

lecithin

-

stimulation

lysolecithin

-

stimulation

Mg2+

-

Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activity

Mn2+

-

Mg2, Mn2+ and other divalent metal ions can not substitute for Ca2+ and lead to a loss od arylesterase activity

phosphate

-

maintains activity, modulates oligomeric state, modulates oligomeric state

phosphatidylcholine

-

purified A or B-type esterases are stimulated

phosphatidylethanolamine

-

stimulation

phosphatidylglycerol

-

stimulation

simvastatin

-

used for treatment of hyperlipoproteinemia type IIa and IIb, simvastatin leads to lipid lowering of total and LDL cholesterol and an increase in PON1 activity in patients with both types of hyperlipoproteinemia, mechanism involving apolipoprotein A-I, overview

677884

additional information

-

2.1

2,4-dinitrophenyl diethyl phosphate

pH 8.0

1.3

2,6-difluorophenyl diethyl phosphate

pH 8.0

0.91

2-fluoro 4-nitrophenyl diethyl phosphate

pH 8.0

1.8

3,5-dinitrophenyl diethyl phosphate

pH 8.0

2.1

3-cyanophenyl diethyl phosphate

pH 8.0

1.7

3-fluoro 4-nitrophenyl diethyl phosphate

-

2

3-fluorophenyl diethyl phosphate

pH 8.0

1.3

3-nitrophenyl diethyl phosphate

pH 8.0

1.9

4-chlorophenyl diethyl phosphate

pH 8.0

1.9

4-cyanophenyl diethyl phosphate

pH 8.0

1.56

4-diethyl phosphate acetophenone

pH 8.0

1.2

4-diethyl phosphate benzaldehyde

pH 8.0

1.9

4-diethyl phosphate methyl benzoate

pH 8.0

0.8

4-nitrophenyl diethyl phosphate

pH 8.0

0.131

chlorpyrifos

recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2

1.33

diazoxon

recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2

0.53 - 0.81

diethyl-paraoxon

0.5 - 1.3

dimethyl-paraoxon

4.6

O,O'-(diisobutyl)methylphosphonate

pH 10.5, 25°C, recombinant His6-tagged enzyme

1400

O-(isobutyl)methylphosphonate

pH 10.5, 25°C, recombinant His6-tagged enzyme

0.2

O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate

0.085 - 1.42

paraoxon

37 entries

4

pentafluorophenyl diethyl phosphate

pH 8.0

0.074 - 0.21

sarin

0.27 - 0.44

soman

0.091 - 0.2

7-diethylphospho-6,8-difluor-4-methylumbelliferyl

0.67 - 0.772

diethyl paraoxon

0.5

O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid

-

in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

0.271 - 4.16

paraoxon

23 entries

1.4 - 3.5

phenyl acetate

additional information

7 entries

-

0.27 - 9160

2,4-dinitrophenyl diethyl phosphate

0.062 - 950

2,6-difluorophenyl diethyl phosphate

3.7

2-fluoro 4-nitrophenyl diethyl phosphate

pH 8.0

11080

2-fluoro-4-nitrophenyl diethyl phosphate

pH 8.0, genetic variant PON1 G2E6

10.2 - 1477

3,5-dinitrophenyl diethyl phosphate

0.178 - 1610

3-cyanophenyl diethyl phosphate

13.9

3-fluoro 4-nitrophenyl diethyl phosphate

pH 8.0

11680

3-fluoro-4-nitrophenyl diethyl phosphate

pH 8.0, genetic variant PON1 G2E6

0.0011 - 656

3-fluorophenyl diethyl phosphate

0.076 - 840

3-nitrophenyl diethyl phosphate

13

4-acetoxy acetophenone

pH 8.0, genetic variant PON1 G2E6

0.0008 - 848

4-chlorophenyl diethyl phosphate

0.4 - 7495

4-cyanophenyl diethyl phosphate

0.44 - 8080

4-diethyl phosphate acetophenone

0.47 - 12620

4-diethyl phosphate benzaldehyde

5485

4-diethyl phosphate methyl benzoate

pH 8.0, genetic variant PON1 G2E6

4.8 - 10520

4-nitrophenyl diethyl phosphate

166

5-(thiobutyryl)butyrolactone

pH 8.0, recombinant wild-type PON1 genetic variant G2E6

0.02

Benzyl acetate

about, pH 8.0, genetic variant PON1 G2E6

0.104 - 0.202

diethyl-paraoxon

0.1 - 10.7

dimethyl-paraoxon

0.24

ethyl acetate

pH 8.0, genetic variant PON1 G2E6

0.54 - 12.7

paraoxon

21 entries

0.6 - 678

pentafluorophenyl diethyl phosphate

0.41 - 8.5

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

0.21 - 1.5

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

0.016 - 2.9

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

20 - 110

4-acetylphenyl 2-methylpropyl (R)-methylphosphonate

12 - 100

4-acetylphenyl 2-methylpropyl (S)-methylphosphonate

0.81 - 150

4-acetylphenyl cyclohexyl (R)-methylphosphonate

0.14 - 19

4-acetylphenyl cyclohexyl (S)-methylphosphonate

7.3 - 150

4-acetylphenyl ethyl (R)-methylphosphonate

110 - 670

4-acetylphenyl ethyl (S)-methylphosphonate

18 - 250

4-acetylphenyl propan-2-yl (R)-methylphosphonate

7.4 - 370

4-acetylphenyl propan-2-yl (S)-methylphosphonate

4.3 - 5.7

diethyl paraoxon

698

dihydrocoumarin

-

recombinant PON3

663985

0.1

O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid

-

in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

0.007 - 10.98

paraoxon

9 entries

89 - 1236

phenyl acetate

15 - 300

sarin

2.2 - 89

soman

additional information

-

-

0.2 - 0.25

diethyl-paraoxon

0.11 - 11.89

dimethyl-paraoxon

0.367 - 10.7

paraoxon

0.367

parathion

pH 8.0, 25°C, enzyme administered in rats in vivo

0.283

SP-CMP

pH 8.0, 25°C, enzyme administered in mice in vivo

0.003 - 2.3

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate

0.016 - 0.59

4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

0.0011 - 1.7

4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate

1.5 - 850

4-acetylphenyl 2-methylpropyl (R)-methylphosphonate

0.099 - 180

4-acetylphenyl 2-methylpropyl (S)-methylphosphonate

0.25 - 28

4-acetylphenyl cyclohexyl (R)-methylphosphonate

0.00094 - 28

4-acetylphenyl cyclohexyl (S)-methylphosphonate

1.5 - 520

4-acetylphenyl ethyl (R)-methylphosphonate

130 - 1200

4-acetylphenyl ethyl (S)-methylphosphonate

1.8 - 580

4-acetylphenyl propan-2-yl (R)-methylphosphonate

3.1 - 110

4-acetylphenyl propan-2-yl (S)-methylphosphonate

0.00083

cyclosarin

-

in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

6.5 - 7.3

diethyl paraoxon

0.2

O-ethyl-S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid

-

in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

0.2

O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid

-

in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

0.02167 - 3.67

paraoxon

0.44

diisopropylfluorophosphate

pH 8.5, 25°C, wild-type enzyme, substrate paraoxon

664885

0.059

etomidate

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

6.48

Ketamine

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

0.041

palmitoyl-lysophosphatidylglycerol

pH 7.4, 25°C

0.47 - 1.95

phenyl acetate

0.322

propofol

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

0.008

6,7-dihydroxy-3-(2-methylphenyl)-2H-chromen-2-one

-

pH 10.5, 37°C

0.0003

6,7-dihydroxy-3-(3-methylphenyl)-2H-chromen-2-one

-

pH 10.5, 37°C

0.001

6,7-dihydroxy-3-(4-methylphenyl)-2H-chromen-2-one

-

pH 10.5, 37°C

0.093

6,7-dihydroxycoumarin

-

pH 10.5, 37°C

0.0012

cefazolin

-

pH 8.0, 37°C, serum PON1, versus paraoxon

0.805

diclofenac sodium

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.026

gentamycin sulfate

-

pH 8.0, 37°C, serum PON1

0.097

indomethacin

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

13.01

Ketoprofen

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

11.12

lincomycine

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.009

lornoxicam

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.306

tenoxicam

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

additional information

-

in vivo and in vitro inhibition kinetic analysis, overview

-

0.021

etomidate

Homo sapiens

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

3.8

Ketamine

Homo sapiens

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

0.328

propofol

Homo sapiens

in 50 mM glycine/NaOH (pH 10.5) containing 1 mM CaCl2, at 25°C

0.012

6,7-dihydroxy-3-(2-methylphenyl)-2H-chromen-2-one

Homo sapiens

-

pH 10.5, 37°C

0.022

6,7-dihydroxy-3-(3-methylphenyl)-2H-chromen-2-one

Homo sapiens

-

pH 10.5, 37°C

0.003

6,7-dihydroxy-3-(4-methylphenyl)-2H-chromen-2-one

Homo sapiens

-

pH 10.5, 37°C

0.178

6,7-dihydroxycoumarin

Homo sapiens

-

pH 10.5, 37°C

0.152 - 0.218

Cd2+

0.0084

cefazolin

Homo sapiens

-

pH 8.0, 37°C, serum PON1

0.781 - 3.91

Co2+

0.061 - 0.31

Cu2+

1.639

diclofenac sodium

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.887

gentamycin sulfate

Homo sapiens

-

pH 8.0, 37°C, serum PON1

0.106 - 0.891

Hg2+

0.195

indomethacin

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

6.23

Ketoprofen

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

9.638

lincomycine

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.136

lornoxicam

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

0.304 - 0.609

Mn2+

1.026 - 1.144

Ni2+

0.34

tenoxicam

Homo sapiens

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

additional information

Homo sapiens

-

-

0.0012

wild type enzyme from crude extract, using paraoxon as substrate

0.0013

mutant enzyme Q192R from crude extract, using paraoxon as substrate

0.15

purified recombinant PON1 wild-type enzyme, pH 10.5, 25°C, substrate diethyl-paraoxon

0.18

purified recombinant PON1-hFc fusion enzyme, pH 10.5, 25°C, substrate diethyl-paraoxon

0.94

mutant enzyme Q192R after 1018fold purification, using paraoxon as substrate

1.21

wild type enzyme after 1018fold purification, using paraoxon as substrate

1.94

pH 8.5, 25°C, substrate: paraoxon, purified recombinant enzyme

113

pH 8.5, 25°C, substrate: diazoxon, purified recombinant enzyme

40.9

pH 8.5, 25°C, substrate: chlorpyrifos oxon, purified recombinant enzyme

465

recombinant enzyme after 90fold purification

5.15

recombinant enzyme from crude cell extract

0.205

pH 8.5, 25°C, substrate: paraoxon, purified recombinant enzyme

0.391

-

0.611

-

using paraoxin as substrate (paraoxonase activity of PON1), at 25°C

693321

0.85

-

plasma, at 37°C

0.962

-

purified enzyme from phenotype A blood plasma

35212

1.76

-

Q192 isoenzyme, serum, pH 8 at 37°C, in Tris-base buffer

1.88

-

isozyme 192Q, crude enzyme, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C

1168

-

isozyme 192R, crude enzyme, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C

1730

-

purified serum enzyme

2109

-

Q192 isoenzyme, 901fold purified, pH 8 at 37°C, in Tris-base buffer

227.3

-

pH 8.0, 37°C

3221

-

isozyme 192R, after 742fold purification, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C

3333

-

R192 isoenzyme, 453fold purified, pH 8 at 37°C, in Tris-base buffer

3840

-

in 50 mM glycine/NaOH, pH 10.5, 1 mM CaCl2, at 25°C

4.34

-

isozyme 192Q, after 589.7fold purification, using paraoxon as substrate, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C

438.2

-

515fold purified enzyme, at 37°C

5.21

-

R192 isoenzyme, serum, pH 8 at 37°C, in Tris-base buffer

6.64

-

purified enzyme from phenotype A blood plasma

35212

additional information

10.5

7.4

assay at

7.5 - 8

assay at

8

8.5

10 - 10.5

-

10.5

7.4

-

assay at

8

8.5

assay at

8.5 - 9.5

using CHES buffer

9.5

-

9.7

-

assay at

677515

additional information

pH-rate profile of PON1 with paraoxon

6.5 - 9.4

-

7.5 - 10.5

optimal activity at pH 10.5, inactivation at pH 7.5

25

25 - 30

paraoxonase activity of recombinant PON1-hFc or PON1

46 - 48

-

22

-

assay at room temperature

25

37

25 - 50

optimal activity at 25°C, inactivation at 50°C, the paraoxonase activity of recombinant PON1-hFc or PON1 rapidly decreases when the temperature is over 30°C

5.1

-

5.3

-

purified PON1, isoelectric focusing

commercial preparation

arterial smooth muscle cell

purified recombinant human PON1

-

-

-

-

-

35216, 646513, 693321

-

-

-

-

35210, 702421, 707214, 709264

serum

additional information

the enzyme is synthesized primarily in the liver and secreted into the plasma, where it is associates with high density lipoproteins (HDL)

-

-

external membrane

-

additional information

malfunction

physiological function

7 entries

physiological function

additional information

P27169 pBLAST

PON1_HUMAN

355

0

39731

Swiss-Prot

Show Sequence

Secretory Pathway (Reliability: 4)

40000

43000

SDS-PAGE

45000

91900

serum PON1, nondenaturing PAGE

95600

recombinant PON1, nondenaturing PAGE

380000

-

gel filtration

35218

39000

2 * 39000, recombinant enzyme

39620

-

calculation from DNA sequence, without allowance for contribution from glycosylation

35219

40600

-

human serum contains one major species of PON monomer (44300 Da) and a minor species of PON monomer (40600 kDa)

646527

41000

-

x * 41000, glycosylated PON1, SDS-PAGE or mass spectrometry, x * 42000, glycosylated PON1, SDS-PAGE or mass spectrometry, x * 44000, glycosylated PON1, SDS-PAGE or mass spectrometry

42000

-

x * 41000, glycosylated PON1, SDS-PAGE or mass spectrometry, x * 42000, glycosylated PON1, SDS-PAGE or mass spectrometry, x * 44000, glycosylated PON1, SDS-PAGE or mass spectrometry

43000

-

x * 43000, SDS-PAGE

35212, 35213, 664153, 678489, 709262

44000

45000

-

x * 45000, SDS-PAGE

702421, 707214, 715735

46000

-

x * 46000, SDS-PAGE

71000

SDS-PAGE

94900

recombinant enzyme, nondenaturing PAGE

?

dimer

2 * 40000, recombinant enzyme, SDS-PAGE

oligomer

once purified, human PON1 is as a mixture of at least two oligomerization states. The absence of human phosphate binding protein favors homo-oligomerization of PON1 into different state(s) of higher molecular size

?

dimer

2 * 39000, recombinant enzyme

homodimer

-

multimer

-

x * 46000, SDS-PAGE

35218

additional information

13 entries

glycoprotein

glycoprotein

additional information

-

the deduced rabbit amino acid sequence contains five potential N-glycosylation sites, whereas the human sequence predicts four possible N-glycosylation sites

646507

purified recombinant wild-type and selenomethionine-labeled PON1 genetic variant G2E6 by use of different mother liquors, microbatch method, X-ray diffracion structure determination and analysis at 2.2-2.6 A resolution

C284A

mutant with 20fold reduced paraoxonase activity

C284D

no enzymic activity

D183N

the mutant disfavors paraoxon binding due to its charged nature and possible electrostatic repulsion with the phosphate group of paraoxon

D269E

no enzymic activity

D54N

no enzymic activity

E313A

slightly decreased activity

E314A

enzymic activity similar to wild-type

F222D

F222Y

G11A

slightly enhanced activity with phenyl acetate and paraoxon

G11C

slightly enhanced activity with phenyl acetate and paraoxon

G11S

slightly enhanced activity with phenyl acetate and paraoxon

H115A

activity with paraoxon is 167% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 119% of wild-type activity

H115Q

activity with paraoxon is 32% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 25% of wild-type activity

H115W

H115W/N133S

H115W/R192A

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192D

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192E

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192F

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192G

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192H

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192I

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192K

H115W/R192K/A137T

site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type

H115W/R192K/A137T/D94H/S211T

site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type

H115W/R192K/A137T/L130F

site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type

H115W/R192K/A137T/M127I/D263H

site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type

H115W/R192K/A137T/S81R/P165A

site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type

H115W/R192L

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192M

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192N

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192P

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192Q

H115W/R192R

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192S

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192T

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192V

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192W

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H115W/R192Y

site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview

H134Q

activity with paraoxon is 602% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 38% of wild-type activity

H134W

no enzymic activity

H134Y

no enzymic activity

H184Q

activity with paraoxon is 8.9% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 7.9% of wild-type activity

H184T

activity with paraoxon is 9.3% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 2.7% of wild-type activity

H285D

no enzymic activity

H285Q

activity with paraoxon is 13% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 4.3% of wild-type activity

H285S

activity with paraoxon is 53% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 25% of wild-type activity

H285Y

no enzymic activity

L55M

L69F

no enzymic activity

L69G/S111T/H115W/H134R/R192K/F222S/T332S

mutant designed for expression in Escherichia coli in soluble and active form. Mutants is more than 20fold better in hydrolyzing paraoxon substrate compared to wild-type and more than 100fold better in hydrolsis of diisopropyl fluorophosphate

730898

L69V

the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme

L69V/V369A

the mutant shows increased paraoxon binding affinity compared to the wild type enzyme

N133S

enzymic activity similar to wild-type

N168E

no enzymic activity

N224A

no enzymic activity

Q192R

R192A

site-directed mutagenesis

R192E

natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme

R192I

site-directed mutagenesis

R192K

site-directed mutagenesis

R192Q

R192V

site-directed mutagenesis

S193P

the mutation increases phosphotriesterase activity of PON1

V304A

no enzymic activity

V346A

the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme

C283A

-

retains enzymatic activity, not inactivated by p-hydroxymercuribenzoate

646525

C283S

-

retains enzymatic activity, not inactivated by p-hydroxymercuribenzoate

646525

C284D

site-directed mutagenesis, inactive mutant

D269E

site-directed mutagenesis, inactive mutant

D54N

site-directed mutagenesis, inactive mutant

E313A

site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme

E314A

site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme

F132G

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

F222A

site-directed mutagenesis, inactive mutant

F222D

site-directed mutagenesis, inactive mutant

F222Y

site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme

G11A

site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme

G11C

site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme

G11S

site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme

G60A

-

the mutant shows increased catalytic efficiency with sarin and soman compared to the wild type enzyme

H114N

-

catalytically inactive

H115W

site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme

H115W/N133S

site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme

H115W/R192K

the mutant enzyme exhibits considerably increased organophosphate-hydrolyzing activity compared to the wild type enzyme

H133N

-

catalytically inactive

H134W

site-directed mutagenesis, inactive mutant

H134Y

site-directed mutagenesis, inactive mutant

H254Q/H257F

-

the mutant shows increased catalytic efficiency compared to the wild type enzyme

H257Y/L303T

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

H284N

-

catalytically inactive

H285D

site-directed mutagenesis, inactive mutant

H285Y

site-directed mutagenesis, inactive mutant

I106A/F132A/H257Y

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

I106A/H257Y/S308A

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

I106G

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

I106G/F132G/H257Y

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

I106G/H257Y

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

L69F

site-directed mutagenesis, inactive mutant

N133S

site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme

N168E

site-directed mutagenesis, inactive mutant

N224A

site-directed mutagenesis, inactive mutant

Q192R

R180T

the mutant enzyme exhibits 180fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme

R460T

the mutant enzyme exhibits 23fold increased ethyl paraoxon-hydrolyzing activity and 340fold increased diisopropylfluorophosphate-hydrolyzing activity compared to the wild type enzyme

R478T

the mutant enzyme exhibits 8fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme

R784T

the mutant enzyme exhibits 3fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme

R789T

the mutant enzyme exhibits 15fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme

S308G

-

the mutant shows decreased catalytic efficiency compared to the wild type enzyme

V304A

site-directed mutagenesis, inactive mutant

additional information

13 entries

5 - 10

the pH stability of activity of recombinant PON1-hFc is similar compared to recombinant wild-type PON1, highest stability at pH 7.0-8.0, profiles overview

752102

5.5 - 10.5

-

35210

additional information

-

activity is reduced below pH 7.0 and at alkaline pH

707214

30 - 60

the thermostability of hydrolyric activity of recombinant PON1-hFc is slightly increased compared to recombinant wild-type PON1, inactivation of PON1 at 55°C, inactivation of PON1-hFc at 60°C, profiles overview

60

complete loss of activity above

678464

37

-

is stable for 8 to 10 h at 37°C. Completely loses activity at 50°C

45

-

60 min, stable

35205

52

-

inactivation

35205

61

-

the melting point of the native enzyme is at 61°C

73

-

the melting point of the recombinant enzyme is at 73°C

additional information

association of paraoxonase 1 with high-density lipoprotein stabilizes the enzyme

692732

nanocapsulation of enzyme into enzyme-polyelectrolyte complexes leads to its expected stabilisation and significant improvement of Km and Ksi with methylphosphonic acid

human paraoxonase 1 alone is unstable. But it is stabilized by the presence of its most common partner protein, the human phosphate binding protein

-

human phosphate-binding protein stabilizes the enzyme and its conformations

-

the HDL composition has an influence on the enzyme stability, overview

-

4°C, purified PON1 in DEAE buffer, at least two weeks, remains stable

4°C, purified recombinant enzyme in 20 mM Tris pH 7.7, 1 mM CaCl2, at least one month, remains stable

4°C, purified recombinant PON1 preparations typically lose about 20% of the arylesterase activity within the first month after purification, compared with less than 10% loss for the enzyme purified from serum. There is no further significant loss of the PON1 activity afterward, suggesting the existence of two pools in the purified PON1, a labile one and a stable one

4°C, 2 mM CaCl2

-

4°C, 2 weeks

-

4°C, 20% glycerol

-

4°C, 50 mM Tris buffer, 50 mM NaCl, 1 mM CaCl2, 0.1% tergitol, pH 8.0, 1 month

-

4°C, 6 months, less than 15% loss of activity

4°C, the enzyme activity is significantly lower after 48 h as well as after 1, 2 and 4 weeks storage when compared to enzyme activities assayed in fresh serum

-

4°C, the purified rPON1A maintains stability for several months when stored in the presence of 0.1% Tergitol NP-10 and 1 mM CaCl2

-

human phosphate-binding protein increases the storage stability of PON1

-

-

ammonium sulfate precipitation, DEAE-Sephadex gel filtration and Sephadex G-200 gel filtration

anion-exchange chromatography and concanavalin-A chromatography

692445

blue agarose affinity chromatography and HiTrap DEAE column chromatography

ceramic HA column chromatography, DEAE-Sepharose column chromatography, Sephadex G-25 gel filtration, and tert-butyl Sepharose column chromatography

Cibacron Blue 3GA agarose gel chromatography and Q-Sepharose resin chromatography

co-purification of PON1 and phosphate binding protein from high-density-lipoprotein-particles using hydroxyapatite chromatography, method development

681055

recombinant His6-tagged catalytically active paraoxwild-type and mutant enzymes refolded from inclusion bodies in Escherichia coli strain BL21(DE3) by anion exchange chromatography

752094

recombinant human paraoxonase 1 fused to human immunoglobulin Fc domain from Drosophila melanogaster S2 cells by protein A affinity chromatography and dialysis. Recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis

recombinant thioredoxin-fusion PON1 genetic variant G2E6 from Escherichia coli, the tag is spontaneously cleaved

666426

recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by isolating inclusion bodies, refolding of the proteins, and anion exchange chromatography

recombinant wild-type and mutant enzymes refolded from Escherichia coli strain BL21(DE3) inclusion bodies by ion exchange chromatography

-

ammonium sulfate precipitation, DEAE-Trisacryl M column chromatography, Sephacryl S300HR gel filtration, and Cibacron Blue 3GA gel filtration

-

ammonium sulfate precipitation, Ultrogel AcA 54 gel filtration, and DEAE-Sephadex A-25 gel filtration

-

by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, 314.9fold with a yield of 25.3%

-

by ammonium sulfate precipitation and hydrophobic interaction chromatography specifically designed for PON1 enzyme, 901fold with 14.5% yield for R192 isoenzyme and 453fold with 6.9% yield for Q192 isoenzyme

-

by different types of chromatographies

-

by immobilized metal-ion affinity chromatography

-

by pseudo-affinity chromatography and gel filtration

-

by Triton-X-100-treatment, ammonium sulfate precipitation, cholesterol-conjugated magnetic nanoparticles and gel filtration, at 4°C, to homogeneity, 515fold with 73% yield

-

Cibacron Blue 3GA-agarose column chromatography, DEAE-Sepharose column chromatography, gel filtration, and Sepharose CL-6B column chromatography

-

DEAE-Sepharose column chromatography, Concanavalin A-Sepharose column chromatography, and Sepharose CL-6B gel filtration

-

714045

HisTrap affinity column chromatography

native enzyme 227fold by ammonium sulfate fractionation and L-tyrosine-1-naphthylamine hydrophobic interaction chromatography to homogeneity

-

native extracellular serum enzyme by ammonium sulfate fractionation and hydrophobic interaction chromatography on a L-tyrosine and 1-naphthylamine containing resin to homogeneity

-

native PON1 from serum, overview, recombinant mutant enzymes from Escherichia coli, transient expression of mutant enzymes in HEK293 cells

PON1-HDL complex, overview

-

Q-Sepharose column chromatography

recombinant enzyme

-

-

application of directed evolution in achieving functional expression of PON1 and PON3 in Escherichia coli culture and a dramatic increase in their hydrolytic proficiency toward the fluorogenic organophosphate substrate 7-O-diethylphosphoryl-3-cyano-7-hydroxycoumarin. The powerful tool of directed evolution opens new prospects for improving their phosphotriesterase activity toward other hazardous organophosphates and toward catalytic activities related to the prevention of atherosclerosis

expressed in baculovirus system in Hi5 insect cells

692445

expressed in Drosophila melanogaster

693354

expressed in Escherichia coli

expression in Escherichia coli

729324

expression of PON1 genetic variant G2E6 as thioredoxin-fusion protein, fusion via a His6-linker, in Escherichia coli

666426

gene PON1 genotyping, analysis of the relationship between genotype, prenatal exposure to organophosphate insecticides, and autism spectrum disorders and related behaviors, overview

750427

gene PON1, recombinant expression of His6-tagged enzyme in Escherichia coli strain SG13009[pREP4]

gene PON1, recombinant expression of the human paraoxonase 1 in Drosophila melanogaster S2 stable cell line with induction by CuSO4 for 14 days. The recombinant human PON1 is fused with the human immunoglobulin Fc domain (PON1-hFc) to improve protein stability and purification efficiency, method optimization, overview. Recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) harboring the pGTf2 plasmid expressing GroEL-GroES and TF chaperones

gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies, subcloning in Escherichia coli strain DH5alpha

gene PON1, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), mutants H115W/R192H and H115W/R192M are expressed as truncated proteins, subcloning in Escherichia coli strain DH5alpha

genotyping of naturally occuring polymorphisms, allele frequency determination

679182

recombinant overexpression of the C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) in inclusion bodies

752094

the recombinant enzyme is expressed in Trichoplusia ni High Five insect cells

-

-

a high level of recombinant hPON1 type A (rPON1A) was produced by Hi-5 insect cells. A fraction is secreted into the cell culture medium, but the majority remains associated with the host insect cells

-

application of directed evolution in achieving functional expression of PON1 and PON3 in Escherichia coli culture and a dramatic increase in their hydrolytic proficiency toward the fluorogenic organophosphate substrate 7-O-diethylphosphoryl-3-cyano-7-hydroxycoumarin. The powerful tool of directed evolution opens new prospects for improving their phosphotriesterase activity toward other hazardous organophosphates and toward catalytic activities related to the prevention of atherosclerosis

distribution of three PON1 polymorphisms in individuals of different age, overview

-

677570

expressed from Trichoplusia ni larvae

-

expressed in Escherichia coli

-

expressed in Escherichia coli BL-21(DE3) cells

-

expressed in Escherichia coli BL21(DE3) cells

expressed in Trichoplusia ni larvae

-

714045, 716956

expression of PON1 mutant enzymes in Escherichia coli

expression of wild-type PON1 and PON1-human phosphate-binding protein hybrid in Escherichia coli

-

gene PON1, DNA and amino acid sequence determination and analysis, gene structure, expression in CHO cells and in human hepatocyte Huh-7 cells

-

gene PON1, expression of two naturally occurring allelic variant isozymes L55R192 PON1 and L55Q192 PON1 in Escherichia coli strain DH5alpha and in CHO cells

-

genotyping of PON1_192 and PON1_55

-

664620

overexpression in HeLa cells, expression as GST-fusion protein in Escherichia coli BL21

-

646524

the cytosolic protein, with N-terminal hexahistidine tag, is expressed using the Escherichia coli Rosetta (DE3) strain

the recombinant enzyme is expressed in Trichoplusia ni High Five insect cells

analysis of the role of nuclear receptors in the regulation of PON1 expression

750290

blood serum enzyme activity is not significantly altered in acute myeloid leukemia

-

750483

enzyme activities in fluorosis patients are considerably decreased up to 56.45% (mild), 61.5% (moderate) and 50% (severe) as compared to control group

-

750345

enzyme activity is decreased in patients with autoimmune thyroid disease

-

752150

enzyme levels of infants in fasting are significantly lower than the values in postprandial

-

750482

enzyme levels of the patients with papillary thyroid cancer are significantly lower compared to those of the control group

-

752173

mean values of serum paraoxonase-1 activity decrease significantly in stage 3 and stage 4 esophageal cancer patients compared with stage 2 esophageal cancer patients

-

714895

paraoxonase activity is significantly lower in patients with chronic active hepatitis B compared to hepatitis B carrier patients or control group patients

-

715738

paraoxonase-1 activity is increased in patients with lacunar infections

-

714759

serum paraoxonase activity is significantly lower in patients with metabolic syndrome than healthy subjects

-

714893

the enzyme activity is reduced in Behcet's disease

-

749840

the mean serum paraoxonase-1 activity is significantly higher in the esophageal cancer group compared to healthy controls

-

714895

refolding of recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) inclusion bodies. The recombinant proteins are refolded to their active form by in vitro refolding, and the active protein present in the refolding reaction mixture is further purified

refolding of recombinant wild-type and mutant enzymes from inclusion bodies in Escherichia coli strain BL21(DE3) by 8 M urea

the inactive recombinant His6-tagged wild-type and mutant enzymes present in the inclusion bodies in Escherichia coli strain BL21(DE3) are refolded to their active form using in vitro refolding, best from refolding buffer containing 200 mM TAPS, pH 8.5, 1.0 M NDSB 201, 1 mM EDTA, 2.2 mM GSH, 0.22 mM GSSH, and 10 mM CaCl2, method optimization, overview. The catalytic properties of the refolded enzymes are similar to their soluble counterparts. The extent of refolding of rh-PON1 is more when 8 M urea is used as a chaotropic agent to denature the rh-PON1 present in inclusion bodies, low concentration of rh-PON1 protein (0.005 mg/ml) is used in the refolding reaction, and when the refolding reaction is incubated for 12 h at 25°C, but low concentration of protein in in vitro refolding is generally not economical for large-scale production of protein, thus 0.020 mg/ml protein concentration is selected for the refolding reaction

-

-

diagnostics

decrease of serum PON1 activities is usually related to many chronic diseases, such as atherosclerosis, diabetes, cancers, migraine, pulmonary tuberculosis, polycystic ovary syndrome, gastroesophageal malignancies, depression, nephritic syndrome, hemodialysis, metabolic syndrome, and liver disease. Determination of PON1 activity has a significant diagnostic value in predicting disease status. PON1 shows very good adaptability in assay development with different substrates, PON1 substrate exhibit many degrees of freedom in docking simulations

medicine

analysis

degradation

-

a series of substituted phenoxyalkyl pyridinium oximes enhance the degradation of surrogates of sarin (i.e. nitrophenyl isopropyl methylphosphonate, NIMP) and VX (i.e. nitrophenyl ethyl methylphosphonate, NEMP). Neither NIMP nor NEMP is hydrolyzed effectively by paraoxonase PON1 if one of these oximes is absent. In the presence of eight novel oximes, PON1-mediated degradation of both surrogates occurs

731000

medicine

19 entries

additional information

35205

Gonzalo, M.C.; Gil, F.; Hernandez, A.F.; Rodrigo, L.; Villanueva, E.; Pla, A.

Human liver paraoxonase (PON1): subcellular distribution and characterization

J. Biochem. Mol. Toxicol.

12

61-69

1998

Homo sapiens

9414488

35207

Reiner, E.; Simeon-Rudolf, V.; Skrinjaric-Spoljar, M.

Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera

Toxicol. Lett.

82/83

447-452

1995

Homo sapiens

8597092

Aviram, M.; Rosenblatt, M.; Bisgaier, C.L.; Newton, R.S.; Primo-Parmo, S.L.; La Du, B.N.

Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase

J. Clin. Invest.

101

1581-1590

1998

Homo sapiens

9541487

35210

Hernandez, A.F.; Pla, A.; Valenzuela, A.; Gil, F.; Villanueva, E.

Characterization of paraoxonase activity in pericardial fluid: usefulness as a marker of coronary disease

Chem. Biol. Interact.

87

173-177

1993

Homo sapiens

8393740

35212

Gan, K.N.; Smolen, A.; Eckerson, H.W.; La Du, B.N.

Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities

Drug Metab. Dispos.

19

100-106

1991

Homo sapiens

1673382

35213

Smolen, A.; Eckerson, H.W.; Gan, K.N.; Hailat, N.; La Du, B.N.

Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase

Drug Metab. Dispos.

19

107-112

1991

Homo sapiens

1673383

35215

Haagen, L.; Brock, A.

A new automated method for phenotyping arylesterase (EC 3.1.1.2) based upon inhibition of enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate

Eur. J. Clin. Chem. Clin. Biochem.

30

391-395

1992

Homo sapiens

1525262

35216

Nishio, E.; Watanabe, Y.

Cigarette smoke extract inhibits plasma paraoxonase activity by modification of the enzyme s free thiols

Biochem. Biophys. Res. Commun.

236

289-293

1997

Homo sapiens

9240427

35218

Tanaka-Kawai, H.; Yomoda, S.

Molecular weight and substrate characteristics of human serum arylesterase following purification by immuno-affinity chromatography

Clin. Chim. Acta

215

127-138

1993

Homo sapiens

8403430

35219

Furlong, C.E.; Richter, R.J.; Chapline, C.; Crabb, J.W.

Purification of rabbit and human serum paraoxonase

Biochemistry

30

10133-10140

1991

Oryctolagus cuniculus, Homo sapiens

1718413

646500

Mackness, M.I.; Thompson, H.M.; Hardy, A.R.; Walker, C.H.

Distinction between A-esterases and arylesterases. Implications for esterase classification

Biochem. J.

245

293-296

1987

Bos taurus, Felis catus, Homo sapiens, Hydrochoerus hydrochaeris, Meles taxus, Mus musculus, no activity in aves, Rattus norvegicus, Sus scrofa

2822017

Mackness, M.I.; Arrol, S.; Durrington, P.N.

Substrate specificity of human serum paraoxonase

Biochem. Soc. Trans.

19

304S

1991

Homo sapiens

1664382

646507

Hassett, C.; Richter, R.J.; Humbert, R.; Chapline, C.; Crabb, J.W.; Omiecinski, C.J.; Furlong, C.E.

Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence

Biochemistry

30

10141-10149

1991

Oryctolagus cuniculus, Homo sapiens

1657140

La Du, B.N.; Adkins, S.; Kuo, C.L.; Lipsig, D.

Studies on human serum paraoxonase/arylesterase

Chem. Biol. Interact.

87

25-34

1993

Homo sapiens

8393742

646513

Pellin, M.C.; Moretto, A.; Lotti, M.; Vilanova, E.

Distribution and some biochemical properties of rat paraoxonase activity

Neurotoxicol. Teratol.

12

611-614

1990

Homo sapiens, Rattus norvegicus

2175012

646520

Josse, D.; Ebel, C.; Stroebel, D.; Fontaine, A.; Borges, F.; Echalier, A.; Baud, D.; Renault, F.; le Maire, M.; Chabrieres, E.; Masson, P.

Oligomeric states of the detergent-solubilized human serum paraoxonase (PON1)

J. Biol. Chem.

277

33386-33397

2002

Homo sapiens

12080042

646522

Deakin, S.; Leviev, I.; Gomaraschi, M.; Calabresi, L.; Franceschini, G.; James, R.W.

Enzymatically active paraoxonase-1 is located at the external membrane of producing cells and released by a high affinity, saturable, desorption mechanism

J. Biol. Chem.

277

4301-4308

2002

Homo sapiens

11726658

646524

Ng, C.J.; Wadleigh, D.J.; Gangopadhyay, A.; Hama, S.; Grijalva, V.R.; Navab, M.; Fogelman, A.M.; Reddy, S.T.

Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein

J. Biol. Chem.

276

44444-44449

2001

Homo sapiens

11579088

646525

Sorenson, R.C.; Primo-Parmo, S.L.; Kuo, C.L.; Adkins, S.; Lockridge, O.; La Du, B.N.

Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase

Proc. Natl. Acad. Sci. USA

92

7187-7191

1995

Homo sapiens

7638166

646526

Costa, L.G.; Li, W.F.; Richter, R.J.; Shih, D.M.; Lusis, A.; Furlong, C.E.

The role of paraoxonase (PON1) in the detoxication of organophosphates and its human polymorphism

Chem. Biol. Interact.

119-120

429-438

1999

Homo sapiens

10421480

646527

Kuo, C.L.; La Du, B.N.

Comparison of purified human and rabbit serum paraoxonases

Drug Metab. Dispos.

23

935-944

1995

Oryctolagus cuniculus, Homo sapiens

8565784

646528

La Du, B.N.; Billecke, S.; Hsu, C.; Haley, R.W.; Broomfield, C.A.

Serum paraoxonase (PON1) isozymes: the quantitative analysis of isozymes affecting individual sensitivity to environmental chemicals

Drug Metab. Dispos.

29

566-569

2001

Homo sapiens (P27169)

11259353

646529

Serhatlioglu, S.; Gursu, M.F.; Gulcu, F.; Canatan, H.; Godekmerdan, A.

Levels of paraoxonase and arylesterase activities and malondialdehyde in workers exposed to ionizing radiation

Cell Biochem. Funct.

21

371-375

2003

Homo sapiens

14624476

646531

Ahmed, Z.; Babaei, S.; Maguire, G.F.; Draganov, D.; Kuksis, A.; La Du, B.N.; Connelly, P.W.

Paraoxonase-1 reduces monocyte chemotaxis and adhesion to endothelial cells due to oxidation of palmitoyl, linoleoyl glycerophosphorylcholine

Cardiovasc. Res.

57

225-231

2003

Homo sapiens

12504832

Ahmed, Z.; Ravandi, A.; Maguire, G.F.; Emili, A.; Draganov, D.; La Du, B.N.; Kuksis, A.; Connelly, P.W.

Multiple substrates for paraoxonase-1 during oxidation of phosphatidylcholine by peroxynitrite

Biochem. Biophys. Res. Commun.

290

391-396

2002

Homo sapiens

11779181

646533

Leviev, I.; Deakin, S.; James, R.W.

Decreased stability of the M54 isoform of paraoxonase as a contributory factor to variations in human serum paraoxonase concentrations

J. Lipid Res.

42

528-535

2001

Homo sapiens

11290824

Doorn, J.A.; Sorenson, R.C.; Billecke, S.S.; Hsu, C.; La Du, B.N.

Evidence that several conserved histidine residues are required for hydrolytic activity of human paraoxonase/arylesterase

Chem. Biol. Interact.

119-120

235-241

1999

Homo sapiens

10421457

646539

Costa, L.G.; Cole, T.B.; Furlong, C.E.

Polymorphisms of paraoxonase (PON1) and their significance in clinical toxicology of organophosphates

J. Toxicol. Clin. Toxicol.

41

37-45

2003

Homo sapiens

12645966

646544

Kuo, C.L.; La Du, B.N.

Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymic activity

Drug Metab. Dispos.

26

653-660

1998

Oryctolagus cuniculus, Homo sapiens

9660847

650953

Billecke, S.; Draganov, D.; Counsell, R.; Stetson, P.; Watson, C.; Hsu, C.; La Du, B.N.

Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters

Drug Metab. Dispos.

28

1335-1342

2000

Homo sapiens (P27169), Homo sapiens

11038162

Brushia, R.J.; Forte, T.M.; Oda, M.N.; La Du, B.N.; Bielicki, J.K.

Baculovirus-mediated expression and purification of human serum paraoxonase 1A

J. Lipid Res.

42

951-958

2001

Homo sapiens

11369803

Soukharev, S.; Hammond, D.J.

A fluorogenic substrate for detection of organophosphatase activity

Anal. Biochem.

327

140-148

2004

Homo sapiens

15033522

664064

Gaidukov, L.; Tawfik, D.S.

High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I

Biochemistry

44

11843-11854

2005

Homo sapiens (P27169)

16128586

Khersonsky, O.; Tawfik, D.S.

Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase

Biochemistry

44

6371-6382

2005

Homo sapiens (P27169)

15835926

Sinan, S.; Kockar, F.; Gencer, N.; Yildirim, H.; Arslan, O.

Amphenicol and macrolide derived antibiotics inhibit paraoxonase enzyme activity in human serum and human hepatoma cells (HepG2) in vitro

Biochemistry (Moscow)

71

46-50

2006

Homo sapiens

16457617

Yeung, D.T.; Josse, D.; Nicholson, J.D.; Khanal, A.; McAndrew, C.W.; Bahnson, B.J.; Lenz, D.E.; Cerasoli, D.M.

Structure/function analyses of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model

Biochim. Biophys. Acta

1702

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2004

Homo sapiens, Homo sapiens (P27169)

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Distribution spectrum of paraoxonase activity in HDL fractions

Clin. Chem.

50

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Homo sapiens

15459089

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Costa, L.G.; Cole, T.B.; Vitalone, A.; Furlong, C.E.

Measurement of paraoxonase (PON1) status as a potential biomarker of susceptibility to organophosphate toxicity

Clin. Chim. Acta

352

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2005

Homo sapiens

15653099

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Yeung, D.T.; Lenz, D.E.; Cerasoli, D.M.

Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates

FEBS J.

272

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2005

Homo sapiens (P27169), Homo sapiens

15853807

James, R.W.; Deakin, S.P.

The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity

Free Radic. Biol. Med.

37

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15544917

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The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases

J. Biol. Chem.

281

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Draganov, D.I.; Teiber, J.F.; Speelman, A.; Osawa, Y.; Sunahara, R.; La Du, B.N.

Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities

J. Lipid Res.

46

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2005

Homo sapiens (P27169), Homo sapiens (Q15166)

15772423

Briseno-Roa, L.; Hill, J.; Notman, S.; Sellers, D.; Smith, A.P.; Timperley, C.M.; Wetherell, J.; Williams, N.H.; Williams, G.R.; Fersht, A.R.; Griffiths, A.D.

Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents

J. Med. Chem.

49

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Harel, M.; Aharoni, A.; Gaidukov, L.; Brumshtein, B.; Khersonsky, O.; Meged, R.; Dvir, H.; Ravelli, R.B.G.; McCarthy, A.; Toker, L.; Silman, I.; Sussman, J.L.; Tawfik, D.S.

Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes

Nat. Struct. Mol. Biol.

11

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2004

Homo sapiens (P27169)

15098021

Aharoni, A.; Gaidukov, L.; Yagur, S.; Toker, L.; Silman, I.; Tawfik, D.S.

Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization

Proc. Natl. Acad. Sci. USA

101

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2004

Homo sapiens (P27169), Homo sapiens (Q15166), Mus musculus (Q62087), Oryctolagus cuniculus (Q9BGN0)

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Formation and disposition of diethylphosphoryl-obidoxime, a potent anticholinesterase that is hydrolyzed by human paraoxonase (PON1)

Biochem. Pharmacol.

69

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2005

Homo sapiens

15876422

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Modulation of paraoxonase (PON1) activity

Biochem. Pharmacol.

69

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2005

Homo sapiens

15670573

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Pasca, S.P.; Nemes, B.; Vlase, L.; Gagyi, C.E.; Dronca, E.; Miu, A.C.; Dronca, M.

High levels of homocysteine and low serum paraoxonase 1 arylesterase activity in children with autism

Life Sci.

78

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2006

Homo sapiens

16297937

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Kilic, S.S.; Aydin, S.; Kilic, N.; Erman, F.; Celik, I.

Serum arylesterase and paraoxonase activity in patients with chronic hepatitis

World J. Gastroenterol.

11

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2005

Homo sapiens (P27169), Homo sapiens

16437641

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Sumegova, K.; Blazicek, P.; Waczulikova, I.; Zitnanova, I.; Durackova, Z.

Activity of paraoxonase 1 (PON1) and its relationship to markers of lipoprotein oxidation in healthy Slovaks

Acta Biochim. Pol.

53

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2006

Homo sapiens (P27169)

17106515

677411

Juretic, D.; Motejlkova, A.; Kunovi?, B.; Reki?, B.; Flegar-Mestri?, Z.; Vuji?, L.; Mesi?, R.; Lukac-Bajalo, J.; Simeon-Rudolf, V.

Paraoxonase/arylesterase in serum of patients with type II diabetes mellitus

Acta Pharm.

56

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2006

Homo sapiens

16613735

677515

Walker, J.P.; Kimble, K.W.; Asher, S.A.

Photonic crystal sensor for organophosphate nerve agents utilizing the organophosphorus hydrolase enzyme

Anal. Bioanal. Chem.

389

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2007

Homo sapiens

17899031

677570

Saruhan, E.; Olgun, A.; Oztuerk, K.; Akman, S.; Erbil, M.K.

Age-related paraoxonase activity changes in Turkish population

Ann. N. Y. Acad. Sci.

1100

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2007

Homo sapiens

17460182

677884

Muacevic-Katanec, D.; Bradamante, V.; Poljicanin, T.; Reiner, Z.; Babic, Z.; Simeon-Rudolf, V.; Katanec, D.

Clinical study on the effect of simvastatin on paraoxonase activity

Arzneimittelforschung

57

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2007

Homo sapiens

18074758

677892

Santanam, N.; Parthasarathy, S.

Aspirin is a substrate for paraoxonase-like activity: implications in atherosclerosis

Atherosclerosis

191

272-275

2007

Homo sapiens (P27169), Homo sapiens

16793048

677893

Aslan, M.; Nazligul, Y.; Horoz, M.; Bolukbas, C.; Bolukbas, F.F.; Gur, M.; Celik, H.; Erel, O.

Serum paraoxonase-1 activity in Helicobacter pylori infected subjects

Atherosclerosis

196

270-274

2008

Homo sapiens

17125774

Rochu, D.; Chabriere, E.; Renault, F.; Elias, M.; Clery-Barraud, C.; Masson, P.

Stabilization of the active form(s) of human paraoxonase by human phosphate-binding protein

Biochem. Soc. Trans.

35

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2007

Homo sapiens

18031277

Nguyen, S.D.; Sok, D.E.

Preferable stimulation of PON1 arylesterase activity by phosphatidylcholines with unsaturated acyl chains or oxidized acyl chains at sn-2 position

Biochim. Biophys. Acta

1758

499-508

2006

Homo sapiens (P27169)

16674912

678464

Rochu, D.; Renault, F.; Clery-Barraud, C.; Chabriere, E.; Masson, P.

Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s)

Biochim. Biophys. Acta

1774

874-883

2007

Homo sapiens (P27169)

17556053

Sinan, S.; Kockar, F.; Arslan, O.

Novel purification strategy for human PON1 and inhibition of the activity by cephalosporin and aminoglikozide derived antibiotics

Biochimie

88

565-574

2006

Homo sapiens

16600468

679074

Forrest, S.R.; Elmore, B.B.; Palmer, J.D.

Activity and lifetime of organophosphorous hydrolase (OPH) immobilized using layer-by-layer nano self-assembly on silicon microchannels

Catal. Today

120

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2006

Homo sapiens

-

679182

Sirivarasai, J.; Kaojarern, S.; Yoovathaworn, K.; Sura, T.

Paraoxonase (PON1) polymorphism and activity as the determinants of sensitivity to organophosphates in human subjects

Chem. Biol. Interact.

168

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2007

Homo sapiens (P27169), Homo sapiens

17532308

679262

Can Demirdoegen, B.; Tuerkanoglu, A.; Bek, S.; Sanisoglu, Y.; Demirkaya, S.; Vural, O.; Arinc, E.; Adali, O.

Paraoxonase/arylesterase ratio, PON1 192Q/R polymorphism and PON1 status are associated with increased risk of ischemic stroke

Clin. Biochem.

41

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2008

Homo sapiens (P27169)

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679293

Schulpis, K.H.; Karikas, G.A.; Bartzeliotou, A.; Papakonstantinou, E.D.; Kalogerakou, M.; Tsakiris, S.

The effect of diet on paraoxonase 1/arylesterase activities in patients with disorders of galactose metabolism

Clin. Endocrinol. (Oxf.)

67

687-692

2007

Homo sapiens (P27169)

17593248

679306

Isik, A.; Koca, S.S.; Ustundag, B.; Celik, H.; Yildirim, A.

Paraoxonase and arylesterase levels in rheumatoid arthritis

Clin. Rheumatol.

26

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2007

Homo sapiens (P27169)

16642406

679530

Catano, H.C.; Cueva, J.L.; Cardenas, A.M.; Izaguirre, V.; Zavaleta, A.I.; Carranza, E.; Hernandez, A.F.

Distribution of paraoxonase-1 gene polymorphisms and enzyme activity in a Peruvian population

Environ. Mol. Mutagen.

47

699-706

2006

Homo sapiens (P27169)

17078098

679634

Schulpis, K.H.; Bartzeliotou, A.; Tsakiris, S.; Gounaris, A.; Papassotiriou, I.

Serum paraoxonase/arylesterase activities in phenylketonuric patients on diet

Eur. J. Clin. Nutr.

61

803-808

2007

Homo sapiens (P27169), Homo sapiens

17203019

Yeung, D.T.; Smith, J.R.; Sweeney, R.E.; Lenz, D.E.; Cerasoli, D.M.

Direct detection of stereospecific soman hydrolysis by wild-type human serum paraoxonase

FEBS J.

274

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2007

Homo sapiens

17286579

681055

Renault, F.; Chabriere, E.; Andrieu, J.; Dublet, B.; Masson, P.; Rochu, D.

Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography

J. Chromatogr. B

836

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2006

Homo sapiens (P27169)

16595195

681264

Gaidukov, L.; Tawfik, D.S.

The development of human sera tests for HDL-bound serum PON1 and its lipolactonase activity

J. Lipid Res.

48

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2007

Homo sapiens (P27169), Homo sapiens

17435182

Park, C.H.; Nguyen, S.D.; Kim, M.R.; Jeong, T.S.; Sok, D.E.

Differential effect of lysophospholipids on activities of human plasma paraoxonase1, either soluble or lipid-bound

Lipids

41

371-380

2006

Homo sapiens (P27169)

16808151

Kanamori-Kataoka, M.; Seto, Y.

Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R)

Anal. Biochem.

385

94-100

2009

Homo sapiens (P27169), Homo sapiens

18952040

690495

Abd-Allah, G.M.; Mariee, A.D.

Nitrite-mediated inactivation of human plasma paraoxonase-1: possible beneficial effect of aromatic amino acids

Appl. Biochem. Biotechnol.

150

281-288

2008

Homo sapiens (P27169), Homo sapiens

18682903

Blum, M.M.; Timperley, C.M.; Williams, G.R.; Thiermann, H.; Worek, F.

Inhibitory potency against human acetylcholinesterase and enzymatic hydrolysis of fluorogenic nerve agent mimics by human paraoxonase 1 and squid diisopropyl fluorophosphatase

Biochemistry

47

5216-5224

2008

Homo sapiens (P27169), Homo sapiens

18396898

691845

Kotur-Stevuljevic, J.; Spasic, S.; Jelic-Ivanovic, Z.; Spasojevic-Kalimanovska, V.; Stefanovic, A.; Vujovic, A.; Memon, L.; Kalimanovska-Ostric, D.

PON1 status is influenced by oxidative stress and inflammation in coronary heart disease patients

Clin. Biochem.

41

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2008

Homo sapiens (P27169)

18634772

Alici, H.A.; Ekinci, D.; Beydemir, S.

Intravenous anesthetics inhibit human paraoxonase-1 (PON1) activity in vitro and in vivo

Clin. Biochem.

41

1384-1390

2008

Homo sapiens (P27169), Homo sapiens

18640108

691849

Schulpis, K.H.; Barzeliotou, A.; Papadakis, M.; Rodolakis, A.; Antsaklis, A.; Papassotiriou, I.; Vlachos, G.D.

Maternal chronic hepatitis B virus is implicated with low neonatal paraoxonase/arylesterase activities

Clin. Biochem.

41

282-287

2008

Homo sapiens (P27169), Homo sapiens

18035058

691850

Yildiz, A.; Gur, M.; Demirbag, R.; Yilmaz, R.; Akyol, S.; Aslan, M.; Erel, O.

Paraoxonase and arylesterase activities in untreated dipper and non-dipper hypertensive patients

Clin. Biochem.

41

779-784

2008

Homo sapiens (P27169), Homo sapiens

18355454

691852

Barim, A.O.; Aydin, S.; Colak, R.; Dag, E.; Deniz, O.; Sahin, I.

Ghrelin, paraoxonase and arylesterase levels in depressive patients before and after citalopram treatment

Clin. Biochem.

42

1076-1081

2009

Homo sapiens (P27169)

19272368

691855

Kasprzak, M.; Iskra, M.; Majewski, W.; Wielkoszynski, T.

Arylesterase and paraoxonase activity of paraoxonase (PON1) affected by ischemia in the plasma of patients with arterial occlusion of the lower limbs

Clin. Biochem.

42

50-56

2009

Homo sapiens (P27169)

18976644

691863

Garces, C.; Lopez-Simon, L.; Rubio, R.; Benavente, M.; Cano, B.; Ortega, H.; de Oya, M.

High-density lipoprotein cholesterol and paraoxonase 1 (PON1) genetics and serum PON1 activity in prepubertal children in Spain

Clin. Chem. Lab. Med.

46

809-813

2008

Homo sapiens (P27169)

18601602

691868

Kotani, K.; Kimura, S.; Tsuzaki, K.; Sakane, N.; Komada, I.; Schulze, J.; Gugliucci, A.

Reduced paraoxonase 1/arylesterase activity and its post-therapeutic increase in obstructive sleep apnea syndrome: A preliminary study

Clin. Chim. Acta

395

184-185

2008

Homo sapiens (P27169)

18503762

691995

van den Berg, S.W.; Jansen, E.H.; Kruijshoop, M.; Beekhof, P.K.; Blaak, E.; van der Kallen, C.J.; van Greevenbroek, M.M.; Feskens, E.J.

Paraoxonase 1 phenotype distribution and activity differs in subjects with newly diagnosed Type 2 diabetes (the CODAM Study)

Diabet. Med.

25

186-193

2008

Homo sapiens (P27169)

18290860

692445

Liu, Y.; Mackness, B.; Mackness, M.

Comparison of the ability of paraoxonases 1 and 3 to attenuate the in vitro oxidation of low-density lipoprotein and reduce macrophage oxidative stress

Free Radic. Biol. Med.

45

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2008

Homo sapiens (P27169)

18585453

692541

Camuzcuoglu, H.; Arioz, D.T.; Toy, H.; Kurt, S.; Celik, H.; Erel, O.

Serum paraoxonase and arylesterase activities in patients with epithelial ovarian cancer

Gynecol. Oncol.

112

481-485

2009

Homo sapiens (P27169), Homo sapiens

19101714

692732

Rock, W.; Rosenblat, M.; Miller-Lotan, R.; Levy, A.P.; Elias, M.; Aviram, M.

Consumption of wonderful variety pomegranate juice and extract by diabetic patients increases paraoxonase 1 association with high-density lipoprotein and stimulates its catalytic activities

J. Agric. Food Chem.

56

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2008

Homo sapiens (P27169)

18759451

693321

Pasca, S.P.; Dronca, E.; Nemes, B.; Kaucsar, T.; Endreffy, E.; Iftene, F.; Benga, I.; Cornean, R.; Dronca, M.

Paraoxonase 1 activities and polymorphisms in autism spectrum disorders

J. Cell. Mol. Med.

14

600-607

2010

Homo sapiens

18624774

693354

Stoltz, D.A.; Ozer, E.A.; Taft, P.J.; Barry, M.; Liu, L.; Kiss, P.J.; Moninger, T.O.; Parsek, M.R.; Zabner, J.

Drosophila are protected from Pseudomonas aeruginosa lethality by transgenic expression of paraoxonase-1

J. Clin. Invest.

118

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2008

Homo sapiens (P27169)

18704198

693357

Aksoy, H.; Aksoy, A.N.; Ozkan, A.; Polat, H.

Serum lipid profile, oxidative status, and paraoxonase 1 activity in hyperemesis gravidarum

J. Clin. Lab. Anal.

23

105-109

2009

Homo sapiens (P27169)

19288455

693517

Jaichander, P.; Selvarajan, K.; Garelnabi, M.; Parthasarathy, S.

Induction of paraoxonase 1 and apolipoprotein A-I gene expression by aspirin

J. Lipid Res.

49

2142-2148

2008

Homo sapiens (P27169), Mus musculus (P52430)

18519978

694369

Wills, A.M.; Landers, J.E.; Zhang, H.; Richter, R.J.; Caraganis, A.J.; Cudkowicz, M.E.; Furlong, C.E.; Brown, R.H.

Paraoxonase 1 (PON1) organophosphate hydrolysis is not reduced in ALS

Neurology

70

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2008

Homo sapiens (P27169)

18347314

Stevens, R.C.; Suzuki, S.M.; Cole, T.B.; Park, S.S.; Richter, R.J.; Furlong, C.E.

Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning

Proc. Natl. Acad. Sci. USA

105

12780-12784

2008

Homo sapiens (P27169)

18711144

Hu, X.; Jiang, X.; Lenz, D.E.; Cerasoli, D.M.; Wallqvist, A.

In silico analyses of substrate interactions with human serum paraoxonase 1

Proteins

75

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2009

Homo sapiens (P27169), Homo sapiens

18951406

695193

Richter, R.J.; Jarvik, G.P.; Furlong, C.E.

Paraoxonase 1 (PON1) status and substrate hydrolysis

Toxicol. Appl. Pharmacol.

235

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2009

Homo sapiens (P27169)

19071155

Hsu, Y.T.; Su, C.Y.; Du, H.C.; Jao, S.C.; Li, W.S.

Evaluation of organophosphorus chemicals-degrading enzymes: a comparison of Escherichia coli and human cytosolic aminopeptidase P

Chem. Biodivers.

5

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2008

Escherichia coli (P15034), Homo sapiens (Q9NQW7)

18649306

Nguyen, S.D.; Hung, N.D.; Cheon-Ho, P.; Ree, K.M.; Dai-Eun, S.

Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1)

Biochim. Biophys. Acta

1790

155-160

2009

Homo sapiens

19103263

707155

Popa, C.; van Tits, L.J.; Barrera, P.; Lemmers, H.L.; van den Hoogen, F.H.; van Riel, P.L.; Radstake, T.R.; Netea, M.G.; Roest, M.; Stalenhoef, A.F.

Anti-inflammatory therapy with tumour necrosis factor alpha inhibitors improves high-density lipoprotein cholesterol antioxidative capacity in rheumatoid arthritis patients

Ann. Rheum. Dis.

68

868-872

2009

Homo sapiens

18635596

Samra, Z.Q.; Shabir, S.; Rehmat, Z.; Zaman, M.; Nazir, A.; Dar, N.; Athar, M.A.

Synthesis of cholesterol-conjugated magnetic nanoparticles for purification of human paraoxonase 1

Appl. Biochem. Biotechnol.

162

671-686

2010

Homo sapiens

19902382

Otto, T.C.; Kasten, S.A.; Kovaleva, E.; Liu, Z.; Buchman, G.; Tolosa, M.; Davis, D.; Smith, J.R.; Balcerzak, R.; Lenz, D.E.; Cerasoli, D.M.

Purification and characterization of functional human paraoxonase-1 expressed in Trichoplusia ni larvae

Chem. Biol. Interact.

187

388-392

2010

Homo sapiens

20176005

Gencer, N.; Arslan, O.

Purification human PON1Q192 and PON1R192 isoenzymes by hydrophobic interaction chromatography and investigation of the inhibition by metals

J. Chromatogr. B

877

134-140

2009

Homo sapiens

19084484

Renault, F.; Carus, T.; Clery-Barraud, C.; Elias, M.; Chabriere, E.; Masson, P.; Rochu, D.

Integrative analytical approach by capillary electrophoresis and kinetics under high pressure optimized for deciphering intrinsic and extrinsic cofactors that modulate activity and stability of human paraoxonase (PON1)

J. Chromatogr. B

878

1346-1355

2010

Homo sapiens, synthetic construct

19945920

Ekinci, D.; Beydemir, S.

Effect of some analgesics on paraoxonase-1 purified from human serum

J. Enzyme Inhib. Med. Chem.

24

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2009

Homo sapiens

19548782

709584

Fairchild, S.Z.; Peterson, M.W.; Hamza, A.; Zhan, C.G.; Cerasoli, D.M.; Chang, W.E.

Computational characterization of how the VX nerve agent binds human serum paraoxonase 1

J. Mol. Model.

17

97-109

2011

Homo sapiens

20379755

709755

Camuzcuoglu, H.; Toy, H.; Cakir, H.; Celik, H.; Erel, O.

Decreased paraoxonase and arylesterase activities in the pathogenesis of future atherosclerotic heart disease in women with gestational diabetes mellitus

J. Womens Health (Larchmt)

18

1435-1439

2009

Homo sapiens

19698032

714045

Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Doctor, B.P.; Nambiar, M.P.

Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1

Biochem. Biophys. Res. Commun.

403

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2010

Oryctolagus cuniculus, Homo sapiens

21040699

714112

Valiyaveettil, M.; Alamneh, Y.; Rezk, P.; Biggemann, L.; Perkins, M.W.; Sciuto, A.M.; Doctor, B.P.; Nambiar, M.P.

Protective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs

Biochem. Pharmacol.

81

800-809

2011

Oryctolagus cuniculus, Homo sapiens

21219877

Tsai, P.C.; Bigley, A.; Li, Y.; Ghanem, E.; Cadieux, C.L.; Kasten, S.A.; Reeves, T.E.; Cerasoli, D.M.; Raushel, F.M.

Stereoselective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase

Biochemistry

49

7978-7987

2010

Homo sapiens

20701311

714759

Moghtaderi, A.; Hashemi, M.; Dabiri, S.; Moazeni-Roodi, A.; Hosseini, M.

Serum paraoxonase and arylesterase activities in patients with lacunar infarction: a case control study

Clin. Biochem.

44

288-292

2011

Homo sapiens

21167145

714893

Hashemi, M.; Kordi-Tamandani, D.M.; Sharifi, N.; Moazeni-Roodi, A.; Kaykhaei, M.A.; Narouie, B.; Torkmanzehi, A.

Serum paraoxonase and arylesterase activities in metabolic syndrome in Zahedan, southeast Iran

Eur. J. Endocrinol.

164

219-222

2011

Homo sapiens

21059866

714895

Cayir, K.; Bilici, M.; Tekin, S.; Kara, F.; Turkyilmaz, A.; Yildirim, A.

Serum paraoxonase and arylesterase activities in esophageal cancer: A controlled study

Eur. J. Gen. Med.

7

398-403

2010

Homo sapiens

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Bayrak, A.; Bayrak, T.; Demirpence, E.; Kilinc, K.

Differential hydrolysis of homocysteine thiolactone by purified human serum (192)Q and (192)R PON1 isoenzymes

J. Chromatogr. B

879

49-55

2011

Homo sapiens

21123122

715738

Duygu, F.; Tekin Koruk, S.; Aksoy, N.

Serum paraoxonase and arylesterase activities in various forms of hepatitis B virus infection

J. Clin. Lab. Anal.

25

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2011

Homo sapiens

21919063

715744

Kockar, F.; Sinan, S.; Yildirim, H.; Arslan, O.

Differential effects of some antibiotics on paraoxonase enzyme activity on human hepatoma cells (HepG2) in vitro

J. Enzyme Inhib. Med. Chem.

25

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2010

Homo sapiens

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Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Farag, H.A.; Agrawal, P.; Doctor, B.P.; Nambiar, M.P.

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Homo sapiens

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Homo sapiens (P27169), Homo sapiens

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Homo sapiens

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Tekin Koruk, S.; Aksoy, N.; Hamidanoglu, M.; Karsen, H.; Unlu, S.; Bilinc, H.

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Homo sapiens

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Homo sapiens

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New chemiluminescent substrates of paraoxonase 1 with improved specificity synthesis and properties

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Homo sapiens (P27169)

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Transcriptional regulation of human paraoxonase 1 by nuclear receptors

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Homo sapiens (P27169)

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Homo sapiens

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Arulkumar, M.; Vijayan, R.; Penislusshiyan, S.; Sathishkumar, P.; Angayarkanni, J.; Palvannan, T.

Alteration of paraoxonase, arylesterase and lactonase activities in people around fluoride endemic area of Tamil Nadu, India

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Homo sapiens

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Millenson, M.E.; Braun, J.M.; Calafat, A.M.; Barr, D.B.; Huang, Y.T.; Chen, A.; Lanphear, B.P.; Yolton, K.

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Homo sapiens (P27169)

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The effect of divalent metal chelators and cadmium on serum phosphotriesterase, lactonase and arylesterase activities of paraoxonase 1

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Homo sapiens

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Kahveci, H.; Laloglu, F.; Kilic, O.; Ciftel, M.; Yildirim, A.; Orbak, Z.; Ertekin, V.; Laloglu, E.

Serum paraoxonase and arylesterase values as antioxidants in healthy premature infants at fasting and posprandial times

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Homo sapiens

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Cebi, A.; Akgun, E.; Esen, R.; Demir, H.; Cifci, A.

The activities of serum paraoxonase and arylesterase and lipid profile in acute myeloid leukemia preliminary results

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Homo sapiens

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Zargari, M.; Sharafeddin, F.; Mahrooz, A.; Alizadeh, A.; Masoumi, P.

The common variant Q192R at the paraoxonase 1 (PON1) gene and its activity are responsible for a portion of the altered antioxidant status in type 2 diabetes

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Homo sapiens

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Perla-Kajan, J.; Borowczyk, K.; Glowacki, R.; Nygard, O.; Jakubowski, H.

Paraoxonase 1 Q192R genotype and activity affect homocysteine thiolactone levels in humans

FASEB J.

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Homo sapiens

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Toward understanding the catalytic mechanism of human paraoxonase 1 site-specific mutagenesis at position 192

PLoS ONE

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Homo sapiens (P27169), Homo sapiens

26829396

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Bajaj, P.; Tripathy, R.K.; Aggarwal, G.; Pande, A.H.

Expression and purification of biologically active recombinant human paraoxonase 1 from inclusion bodies of Escherichia coli

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Homo sapiens (P27169), Homo sapiens

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