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(+)-cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
(1E)-but-1-en-1-yl dibutyl phosphate + H2O
dibutyl phosphate + ?
-
-
-
?
(RS)-propan-2-yl methylphosphonofluoridate + H2O
isopropyl phosphate methylphosphonate + fluoride
i.e. sarin
-
-
?
(S)-[2-(diethylamino)ethyl] O,O-diethyl phosphorothioate + H2O
diethyl phosphate + 2-(diethylamino)ethane-1-thiol
-
-
-
?
(S)-[2-(diethylamino)ethyl] O,O-dimethyl phosphorothioate + H2O
dimethyl phosphate + 2-(diethylamino)ethane-1-thiol
-
-
-
?
(S)-[2-(diethylamino)ethyl] O-(2-methylpropyl) methylphosphonothioate + H2O
2-methylpropyl methylphosphonate + 2-(diethylamino)ethane-1-thiol
-
-
-
?
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate + H2O
diethyl phosphate + 2-[di(propan-2-yl)amino]ethane-1-thiol
-
-
-
?
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-dimethyl phosphorothioate + H2O
dimethyl phosphate + 2-[di(propan-2-yl)amino]ethane-1-thiol
-
-
-
?
(S)-[2-[di(propan-2-yl)amino]ethyl] O-ethyl methylphosphonothioate + H2O
ethyl methylphosphonate + [di(propan-2-yl)amino]ethane-1-thiol
-
-
-
?
1,2,2-trimethylpropyl methylphosphonofluoridate + H2O
3,3-dimethylbutan-2-yl methylphosphonate + HF
-
-
-
-
?
1-methylethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl methylphosphonate + H2O
?
-
-
-
?
1-methylethyl 4-methyl-2-oxo-2H-chromen-7-yl methylphosphonate + H2O
?
-
-
-
?
1-methylethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen (1-methylpropyl)phosphonate
1-methylethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen methylphosphonate
1-methylpropyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylpropyl hydrogen methylphosphonate
1-palmitoyl-2-(5-oxo)valeroyl-sn-glycero-3-phosphocholine + H2O
lysophosphatidylcholine + ?
-
-
-
?
1-palmitoyl-2-(9-oxo)nonanoyl-sn-glycero-3-phosphocholine + 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-methoxycarbonyl-1-methylvinyl dimethyl phosphate + H2O
?
i.e. mevinphos
-
-
?
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
-
-
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
?
i.e. soman
-
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
Pinacolyl methylphosphonate + fluoride
i.e. soman
-
-
?
4-acetoxy acetophenone + 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
-
-
-
-
?
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate + H2O
4-acetylphenol + (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
-
-
-
?
4-acetylphenyl (R)-2-methylpropyl methylphosphonate + H2O
(R)-2-methylpropyl methylphosphonate + 4-acetylphenol
-
-
-
?
4-acetylphenyl (S)-2-methylpropyl methylphosphonate + H2O
(S)-2-methylpropyl methylphosphonate + 4-acetylphenol
-
-
-
?
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate + H2O
4-acetylphenol + 2-methylpropyl (R)-methylphosphonate
-
-
-
-
?
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate + H2O
4-acetylphenol + 2-methylpropyl (S)-methylphosphonate
-
-
-
-
?
4-acetylphenyl cyclohexyl (R)-methylphosphonate + H2O
4-acetylphenol + cyclohexyl (R)-methylphosphonate
-
-
-
-
?
4-acetylphenyl cyclohexyl (S)-methylphosphonate + H2O
4-acetylphenol + cyclohexyl (S)-methylphosphonate
-
-
-
-
?
4-acetylphenyl cyclohexyl methyl (R)-phosphate + H2O
cyclohexyl methyl (R)-phosphate + 4-acetylphenol
-
-
-
?
4-acetylphenyl cyclohexyl methyl (S)-phosphate + H2O
cyclohexyl methyl (S)-phosphate + 4-acetylphenol
-
-
-
?
4-acetylphenyl ethyl (R)-methylphosphonate + H2O
4-acetylphenol + ethyl (R)-methylphosphonate
-
-
-
-
?
4-acetylphenyl ethyl (S)-methylphosphonate + H2O
4-acetylphenol + ethyl (S)-methylphosphonate
-
-
-
-
?
4-acetylphenyl propan-2-yl (R)-methylphosphonate + H2O
4-acetylphenol + propan-2-yl (R)-methylphosphonate
-
-
-
-
?
4-acetylphenyl propan-2-yl (S)-methylphosphonate + H2O
4-acetylphenol + propan-2-yl (S)-methylphosphonate
-
-
-
-
?
4-carbamoylphenyl diethyl phosphate + H2O
dibutyl phosphate + ?
-
-
-
?
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 butanoate + H2O
4-nitrophenol + butanoate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl diethyl phosphate + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
4-nitrophenyl phenyl methylphosphonate + H2O
4-nitrophenol + phenyl hydrogen methylphosphonate
4-nitrophenyl phenyl methylphosphonate + H2O
phenyl hydrogen methylphosphonate + 4-nitrophenol
-
wild-type, 78% of the activity with propyl 4-nitrophenyl methylphosphonate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
4-nitrophenyl propan-2-yl methylphosphonate + H2O
propan-2-yl hydrogen methylphosphonate + 4-nitrophenol
-
wild-type, 57% of the activity with propyl 4-nitrophenyl methylphosphonate
-
-
?
4-nitrophenyl propyl methylphosphonate + H2O
4-nitrophenol + propyl hydrogen methylphosphonate
5-(thiobutyryl)butyrolactone + H2O
?
-
-
-
?
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
-
-
?
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
?
-
-
-
?
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
-
-
-
?
butan-2-yl 4-nitrophenyl methylphosphonate + H2O
butan-2-yl hydrogen methylphosphonate + 4-nitrophenol
-
wild-type, 50% of the activity with propyl 4-nitrophenyl methylphosphonate
-
-
?
cadusafos + H2O
O,O-diethylphosphorodithioate + phenol
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
chlorpyrifos + H2O
O,O-diethylphosphorothioate + 3,5,6-trichloropyridin-2-ol
chlorpyrifos oxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
chlorpyrifos oxon + H2O
?
-
-
-
?
chlorpyrifos oxon + H2O
diethyl phosphate + 3,5,6-trichloropyridin-2-ol
chlorpyrifos-oxon + H2O
3,5,6-trichloro-2-pyridinol + diethyl phosphate
-
-
-
?
chlorpyrifos-oxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
-
-
-
-
?
chlorpyrifos-oxon + H2O
?
chlorpyrifosoxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
-
-
-
?
chlorpyriphosoxon + H2O
?
-
-
-
-
?
chlortion + H2O
?
chlorthion is O,O-dimethyl O-(3-chloro-4-nitrophenyl) thionophosphate
-
-
?
CMP-coumarin + H2O
?
-
-
-
?
coroxon + H2O
?
-
-
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
coumaphos + H2O
3-chloro-4-methylumbelliferone + diethyl thiophosphate
coumaphos + H2O
O,O-diethylphosphorothioate + 3-chloro-4-methylumbelliferone
coumaphos + H2O
O,O-diethylphosphorothioate + 3-chloro-7-hydroxy-4-methyl-2H-chromen-2-one
cf. EC 3.1.8.2
-
-
?
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
-
-
-
?
cyclohexyl ethyl 4-nitrophenyl (R)-phosphate + H2O
cyclohexyl ethyl (R)-phosphate + 4-nitrophenol
-
-
-
?
cyclohexyl ethyl 4-nitrophenyl (S)-phosphate + H2O
cyclohexyl ethyl (S)-phosphate + 4-nitrophenol
-
-
-
?
cyclohexyl methyl 4-nitrophenyl (R)-phosphate + H2O
cyclohexyl methyl (R)-phosphate + 4-nitrophenol
-
-
-
?
cyclohexyl methyl 4-nitrophenyl (S)-phosphate + H2O
cyclohexyl methyl (S)-phosphate + 4-nitrophenol
-
-
-
?
cyclohexyl methyl phenyl (R)-phosphate + H2O
cyclohexyl methyl (R)-phosphate + phenol
-
-
-
?
cyclohexyl methyl phenyl (S)-phosphate + H2O
cyclohexyl methyl (S)-phosphate + phenol
-
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
cyclohexylmethylphosphonofluoridate + H2O
cyclohexyl methylphosphonate + fluoride
i.e. cyclosarin
-
-
?
cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
demeton-S methyl + H2O
2-ethylsulfanyl-ethanethiol + dimethyl phosphate
-
-
-
-
?
demeton-S-methyl + H2O
2-ethylsulfanyl-ethanethiol + dimethyl phosphate
-
-
-
-
?
diazinon + H2O
O,O-diethylphosphorothioate + ?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
diazoxon + H2O
6-methyl-2-(1-methylethyl)pyrimidin-4-ol + diethyl phosphate
-
-
-
-
ir
dibutyl 2,2,3,3-tetrafluorobutyl phosphate + H2O
dibutyl phosphate + ?
dibutyl 3,3-difluorobutyl phosphate + H2O
dibutyl phosphate + ?
dibutyl 4-acetophenyl phosphate + H2O
dibutyl phosphate + 4-hydroxyacetophenone
-
-
-
?
dibutyl 4-nitrophenyl phosphate + H2O
dibutyl phosphate + 4-nitrophenol
-
-
-
?
dibutyl phenyl phosphate + H2O
dibutyl phosphate + phenol
-
-
-
?
dichlorvos + H2O
2,2-dichloroethenol + dimethyl hydrogen phosphate
-
-
-
?
diethyl (3,5,6-trichloropyridin-2-yl) phosphate + H2O
?
diethyl 2,4,6-trifluorophenyl phosphate + H2O
diethyl phosphate + 2,4,6-trifluorophenol
-
-
-
?
diethyl 2,4-difluorophenyl phosphate + H2O
diethyl phosphate + 2,4-difluorophenol
-
-
-
?
diethyl 2,6-difluoro-4-nitrophenyl phosphate + H2O
diethyl phosphate + 2,6-difluoro-4-nitrophenol
-
-
-
?
diethyl 2-(dimethoxyphosphorylsulfanyl)butanedioate + H2O
?
i.e. malaoxon
-
-
?
diethyl 2-fluoro-4-nitrophenyl phosphate + H2O
diethyl phosphate + 2-fluoro-4-nitrophenol
-
-
-
?
diethyl 2-fluorophenyl phosphate + H2O
diethyl phosphate + 2-fluorophenol
-
-
-
?
diethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl phosphate + H2O
diethyl phosphate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one
-
-
-
?
diethyl 3-fluoro-4-nitrophenyl phosphate + H2O
diethyl phosphate + 3-fluoro-4-nitrophenol
best substrate
-
-
?
diethyl 3-fluorophenyl phosphate + H2O
diethyl phosphate + 4-fluorophenol
high activity
-
-
?
diethyl 4-acetophenyl phosphate + H2O
diethyl phosphate + 4-hydroxyacetophenone
-
-
-
?
diethyl 4-chlorophenyl phosphate + H2O
4-chlorophenol + diethyl phosphate
diethyl 4-chlorophenyl phosphate + H2O
diethyl phosphate + 4-chlorophenol
-
-
-
?
diethyl 4-chlorophenyl thiophosphate + H2O
4-chlorophenol + diethyl thiophosphate
-
-
-
?
diethyl 4-cyanophenyl phosphate + H2O
diethyl phosphate + 4-hydroxybenzonitril
-
-
-
?
diethyl 4-fluorophenyl phosphate + H2O
diethyl phosphate + 4-fluorophenol
-
-
-
?
diethyl 4-formylphenyl phosphate + H2O
diethyl phosphate + 4-formylphenol
-
-
-
?
diethyl 4-methoxyphenyl phosphate + H2O
diethyl phosphate + 4-methoxyphenol
-
-
-
?
diethyl 4-methylbenzylphosphonate + H2O
?
-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl phosphate
diethyl 4-nitrophenyl phosphate + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
p-nitrophenol + diethyl phosphate
-
-
-
-
?
diethyl pentafluoro-phenyl phosphate + H2O
diethyl phosphate + 2,3,4,5,6-pentafluorophenol
high activity
-
-
?
diethyl phenyl phosphate + H2O
diethyl phosphate + phenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
diethylumbelliferyl phosphate + H2O
diethylumbelliferol + phosphate
-
-
-
-
?
diisopropyl fluorophosphate + H2O
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
diisopropyl fluorophosphate + H2O
isopropanol + ?
-
-
-
?
diisopropylfluorophosphate + H2O
?
-
-
-
?
diisopropylfluorophosphate + H2O
diisopropyl phosphate + HF
dimefox + H2O
?
-
-
-
-
?
dimethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl phosphate + H2O
dimethyl phosphate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one
-
-
-
?
dimethyl 4-methyl-2-oxo-2H-chromen-7-yl phosphate + H2O
?
-
-
-
?
dimethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + dimethyl hydrogen phosphate
13.3% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
dimethyl 4-nitrophenyl phosphate + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl paraoxon + H2O
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
dyfonate + H2O
O,O-diethylphosphorothioate + 2-isopropyl-6-methylpyrimidin-4-ol
-
-
-
-
?
ethoprophos + H2O
?
-
-
-
-
?
ethyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl 1-methylethyl hydrogen phosphate
ethyl 2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl methylphosphonate + H2O
ethyl methylphosphonate + 7-hydroxy-4-(trifluoromethyl)-2H-1-benzopyran-2-one
-
-
-
?
ethyl 4-methyl-2-oxo-2H-chromen-7-yl methylphosphonate + H2O
ethyl methylphosphonate + 7-hydroxy-4-methyl-2H-1-benzopyran-2-one
-
-
-
?
ethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + ethyl hydrogen (1-methylpropyl)phosphonate
ethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + ethyl hydrogen methylphosphonate
ethyl 4-nitrophenyl methylphosphonate + H2O
ethyl hydrogen methylphosphonate + 4-nitrophenol
-
wild-type, 50% of the activity with propyl 4-nitrophenyl methylphosphonate
-
-
?
ethyl acetate + H2O
?
-
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
ethyl paraoxon + H2O
4-nitrophenol + diethyl phosphate
ethyl parathion + H2O
?
-
-
-
-
?
ethyl phenyl parathion
?
-
-
-
-
?
ethyl-paraoxon + H2O
?
the enzyme is a poor phosphotriesterase
-
-
?
fenamiphos + H2O
?
-
-
-
-
?
fenitrothion + H2O
?
-
-
-
?
fenitrothion + H2O
O,O-diethylphosphorothioate + 3-methyl-4-nitrophenol
-
-
-
?
fenitroxon + H2O
?
-
-
-
-
?
fensulfothion + H2O
?
-
-
-
?
fensulfothion + H2O
O,O-diethylphosphorothioate + 4-(methylsulfinyl)phenol
some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants
-
-
?
isopropyl methylphosphonofluoridate + H2O
propan-2-yl methylphosphonate + HF
-
-
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
malathion + H2O
O,O-diethylphosphorothioate + diethyl 2-mercaptosuccinate
low activity
-
-
?
methyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + methyl 1-methylethyl hydrogen phosphate
100% activity
-
-
?
methyl 4-nitrophenyl methylphosphonate + H2O
methyl hydrogen methylphosphonate + 4-nitrophenol
-
wild-type, 733% of the activity with propyl 4-nitrophenyl methylphosphonate
-
-
?
methyl 4-nitrophenyl phenyl (R)-phosphate + H2O
methyl phenyl (R)-phosphate + 4-nitrophenol
-
-
-
?
methyl 4-nitrophenyl phenyl (S)-phosphate + H2O
methyl phenyl (S)-phosphate + 4-nitrophenol
-
-
-
?
methyl 4-nitrophenyl propan-2-yl (R)-phosphate + H2O
methyl propan-2-yl (R)-phosphate + 4-nitrophenol
-
-
-
?
methyl 4-nitrophenyl propan-2-yl (S)-phosphate + H2O
methyl propan-2-yl (S)-phosphate + 4-nitrophenol
-
-
-
?
methyl 4-[(diethoxyphosphoryl)oxy]benzoate + H2O
dibutyl phosphate + ?
-
-
-
?
methyl bis(4-nitrophenyl) phosphate + H2O
methyl phosphate + 2 4-nitrophenol
-
-
-
?
methyl chlorpyrifos oxon + H2O
?
-
-
-
?
methyl chlorpyrifos thion + H2O
?
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
methyl paraoxon + H2O
?
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
methyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
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
-
-
?
mono(diethylphosphoryl)obidoxime + H2O
diethyl hydrogenphosphate + obidoxime
-
substrate is a potent inhibitor of human acetylcholinesterase
-
-
?
N,N-diethyl-2-(methyl-(2-methylpropoxy)phosphoryl)sulfanylethanamine + H2O
?
i.e. VR
-
-
?
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
-
-
?
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
-
-
?
O,O'-(diisobutyl)methylphosphonate + H2O
?
-
-
-
?
O,O,S-tributyl phosphorothioate + H2O
dibutyl phosphate + ?
-
-
-
?
O,O-diethyl fluorophosphate + H2O
diethylphosphate + fluoride
-
activity of EC 3.1.8.2
-
-
?
O,O-diethyl O-4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
O,O-diethyl O-[4-methyl-6-(propan-2-yl)pyrimidin-2-yl] phosphorothioate + H2O
O,O-diethyl phosphorothioate + 4-methyl-6-(propan-2-yl)pyrimidin-2-ol
-
i.e. diazinon
-
-
?
O,O-diethyl-S-[2-diethylaminoethyl]thiophosphate + H2O
?
i.e. amiton or VG
-
-
?
O,O-diethyl-S-[2-diisopropylaminoethyl]thiophosphate + H2O
?
i.e. diisopropyl-amiton
-
-
?
O,O-diethyl-S-[2-dimethylaminoethyl]thiophosphate + H2O
?
i.e. dimethyl-amiton
-
-
?
O,O-diisopropyl-4-nitrophenyl phosphate + H2O
dipropan-2-yl hydrogen phosphate + 4-nitrophenol
-
-
-
-
?
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
?
-
-
-
?
O-(isobutyl)methylphosphonate + H2O
?
very low activity
-
-
?
O-ethyl O-4-nitrophenyl phenylphosphonothioate + H2O
?
-
-
-
?
O-ethyl S-(2-diisopropylaminoethyl) methylphosphonothioate + H2O
?
-
i.e. VX, a highly toxic organophosphorus nerve agent, stereospecific hydrolysis
-
-
?
O-ethyl S-(2-diisopropylaminoethyl)methylphosphonothioate + H2O
?
also called VX
-
-
?
O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate + H2O
?
-
-
-
?
O-ethyl-S-(2-di-n-propylaminoethyl)methylphosphonothiolate + H2O
?
i.e. n-propyl-VX
-
-
?
O-ethyl-S-(2-diethylaminoethyl)ethylphosphonothiolate + H2O
?
i.e. VE
-
-
?
O-ethyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VM
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)ethylphosphonothiolate + H2O
?
i.e. isopropyl-VE
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
O-ethyl-S-(2-dimethylaminoethyl)ethylphosphonothiolate + H2O
?
i.e. methyl-VE
-
-
?
O-ethyl-S-(2-dimethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. dimethyl-VX
-
-
?
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
-
-
?
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
-
-
?
O-isobutyl S-(2-N,N-diethylaminoethyl)methylphosphonothioate + H2O
?
also called VR
-
-
?
O-isobutyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid + H2O
?
-
hydrolysis is exclusively preferential for the P+ isomer. Glycosylation state of PON1 does not affect substrate stereoselectivity
-
-
?
O-isopropyl methylphosphonofluoridate + H2O
?
O-methyl O-(4-nitrophenyl) methylphosphonothioate + H2O
O-methyl-methylphosphonothionic acid + 4-nitrophenol
-
-
-
-
?
O-methyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. methyl-VM
-
-
?
O-n-butyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. CVX or Chinese VX
-
-
?
paraoxon + H2O
4-nitrophenol + di-ethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
paraoxon + H2O
4-nitrophenol + diethylphosphate
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
paraoxon + H2O
diethylphosphate + 4-nitrophenol
paraoxon ethylene + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
parathion + H2O
diethylthiophosphate + 4-nitrophenol
pentafluorophenyl diethyl phosphate + H2O
?
-
-
-
?
pentafluorophenyl diethyl phosphate + H2O
pentafluorophenol + diethyl phosphate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
phosalone + H2O
?
-
-
-
-
?
phosmet + H2O
N-hydroxymethyl-phthalimide + O,O-dimethyl dithiophosphate
-
-
-
-
?
phosphatidylcholine isoprostane + H2O
?
-
-
-
-
?
pirimiphos-methyloxon + H2O
?
propyl 4-nitrophenyl methylphosphonate + H2O
propyl hydrogen methylphosphonate + 4-nitrophenol
-
-
-
-
?
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin + H2O
?
-
-
-
-
?
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin + H2O
?
-
-
-
-
?
russian VX + H2O
methyl-phosphonothioic acid S-(2-diethylamino-ethyl) ester + 2-methylpropanol
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
O-ethyl hydrogen methylphosphonothioate + 2-[di(propan-2-yl)amino]ethanol
-
i.e. nerve agent VX
-
-
?
sarin + H2O
methyl-phosphonic acid monofluoride + isopropyl alcohol
sarin + H2O
methylphosphonofluoride acid + ?
soman + H2O
methyl-phosphonic acid monofluoride + 1,2,2-trimethylpropanol
soman + H2O
methylphosphonofluoride acid + 3,3-dimethylbutan-2-ol
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin + H2O
?
-
-
-
-
?
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin + H2O
?
-
-
-
-
?
tabun + H2O
cyanophosphonic acid dimethylamide + ethanol
trimethyl phosphate + H2O
?
-
-
-
?
VX + H2O
S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol
additional information
?
-
(+)-cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
wild type enzyme and mutant enzyme W263F hydrolyze the (+)-enantiomer approximately 3 and 4.5 times faster than the (-)-enantiomer
-
-
?
(+)-cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
wild type enzyme and mutant enzyme W263F hydrolyze the (+)-enantiomer approximately 3 and 4.5 times faster than the (-)-enantiomer
-
-
?
1-methylethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen (1-methylpropyl)phosphonate
6.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
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
33.1% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
1-methylethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen methylphosphonate
-
-
-
?
1-methylpropyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylpropyl hydrogen methylphosphonate
29.5% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
1-methylpropyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylpropyl hydrogen methylphosphonate
best substrate
-
-
?
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-chloro-4-methyl-2-oxo-2H-chromen-7-yl ethyl methylphosphonate + H2O
3-chloro-7-hydroxy-4-methyl-2H-chromen-2-one + ethyl methylphosphonate
-
-
-
?
4-nitrophenolate + H2O
?
-
-
-
-
?
4-nitrophenolate + H2O
?
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl phenyl methylphosphonate + H2O
4-nitrophenol + phenyl hydrogen methylphosphonate
45.2% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
4-nitrophenyl phenyl methylphosphonate + H2O
4-nitrophenol + phenyl hydrogen methylphosphonate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl propyl methylphosphonate + H2O
4-nitrophenol + propyl hydrogen methylphosphonate
58.5% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
4-nitrophenyl propyl methylphosphonate + H2O
4-nitrophenol + propyl hydrogen methylphosphonate
best substrate
-
-
?
acephate + H2O
?
-
-
-
-
?
acephate + H2O
?
-
-
-
-
?
acephate + H2O
?
-
-
-
-
?
cadusafos + H2O
O,O-diethylphosphorodithioate + phenol
-
-
-
-
?
cadusafos + H2O
O,O-diethylphosphorodithioate + phenol
-
-
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
a popular pesticide used in agricultural crop protection causes widespread contamination, degradation by evolutionary improved genetic OPH variants, e.g. variants B3561 and B1368, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
the wild-type enzyme shows 1000fold lower activity compared to substrate paraoxon, analysis of activity with chlorpyrifos of genetic variants, 22A11, A1030, A1467, B1368, B2136, and B3561, the wild-type shows extremely low activity while variants B3561 and B1368 show high activity, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
-
the wild-type enzyme shows lower activity compared to the activity of genetic variant 22A11, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
-
the wild-type enzyme shows lower activity compared to the activity of genetic variant 22A11, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
a popular pesticide used in agricultural crop protection causes widespread contamination, degradation by evolutionary improved genetic OPH variants, e.g. variants B3561 and B1368, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
the wild-type enzyme shows 1000fold lower activity compared to substrate paraoxon, analysis of activity with chlorpyrifos of genetic variants, 22A11, A1030, A1467, B1368, B2136, and B3561, the wild-type shows extremely low activity while variants B3561 and B1368 show high activity, overview
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
-
-
-
?
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
-
-
-
-
?
chlorpyrifos + H2O
?
-
-
-
?
chlorpyrifos + H2O
?
-
-
-
?
chlorpyrifos + H2O
O,O-diethylphosphorothioate + 3,5,6-trichloropyridin-2-ol
-
-
-
-
?
chlorpyrifos + H2O
O,O-diethylphosphorothioate + 3,5,6-trichloropyridin-2-ol
-
-
-
-
?
chlorpyrifos + H2O
O,O-diethylphosphorothioate + 3,5,6-trichloropyridin-2-ol
low activity, cf. EC 3.1.8.2
-
-
?
chlorpyrifos oxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
-
-
-
?
chlorpyrifos oxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
-
-
-
-
?
chlorpyrifos oxon + H2O
diethyl phosphate + 3,5,6-trichloropyridin-2-ol
-
-
-
?
chlorpyrifos oxon + H2O
diethyl phosphate + 3,5,6-trichloropyridin-2-ol
i.e. CPO, a metabolite of chlorpyrifos that is used as a pesticide in agriculture industry
-
-
?
chlorpyrifos-oxon + H2O
?
-
-
-
-
?
chlorpyrifos-oxon + H2O
?
-
-
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coroxon + H2O
diethyl phosphate + chlorferon
-
substrate is used for in vitro activity detection
-
-
?
coumaphos + H2O
3-chloro-4-methylumbelliferone + diethyl thiophosphate
-
-
-
-
?
coumaphos + H2O
3-chloro-4-methylumbelliferone + diethyl thiophosphate
-
-
-
?
coumaphos + H2O
3-chloro-4-methylumbelliferone + diethyl thiophosphate
-
-
-
-
?
coumaphos + H2O
?
-
-
-
-
?
coumaphos + H2O
?
-
-
-
-
?
coumaphos + H2O
O,O-diethylphosphorothioate + 3-chloro-4-methylumbelliferone
-
-
-
-
?
coumaphos + H2O
O,O-diethylphosphorothioate + 3-chloro-4-methylumbelliferone
-
-
-
-
?
CVX + H2O
?
-
i.e. diethylamino-ethyl-O-butyl methylphosphonothioate
-
-
?
CVX + H2O
?
-
i.e. diethylamino-ethyl-O-butyl methylphosphonothioate
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin, activity of 3.1.8.2
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
?
i.e. cyclosarin
-
-
?
cyclosarin + H2O
?
-
-
-
-
?
cyclosarin + H2O
?
-
-
-
?
cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
-
-
-
-
?
cyclosarin + H2O
methyl-phosphonic acid monofluoride + cyclohexanol
-
-
-
-
?
demethon-S + H2O
?
-
-
-
-
?
demethon-S + H2O
?
-
-
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
-
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
-
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
-
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
0.2 mM, 26% degradation over 24 h by whole cells
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
0.2 mM, 26% degradation over 24 h by whole cells
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
0.2 mM, 27% degradation over 24 h by whole cells
-
-
?
demeton-S + H2O
2-ethylsulfanyl-ethanethiol + diethyl phosphate
-
0.2 mM, 27% degradation over 24 h by whole cells
-
-
?
diazinon + H2O
?
-
0.2 mM, 24% degradation over 24 h by whole cells
-
-
?
diazinon + H2O
?
-
0.2 mM, 60% degradation over 24 h by whole cells
-
-
?
diazinon + H2O
O,O-diethylphosphorothioate + ?
-
-
-
-
?
diazinon + H2O
O,O-diethylphosphorothioate + ?
-
-
-
-
?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
-
-
-
?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
the homozygote wild type enzyme (QQ phenotype of Q192R) hydrolyzes diaxozon more rapidly than paraoxon
-
-
?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
the homozygote wild type enzyme shows highest activity towards diazoxon
-
-
?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
-
-
-
-
?
diazoxon + H2O
?
-
-
-
-
?
diazoxon + H2O
?
highest activity with diazoxon
-
-
?
diazoxon + H2O
?
-
-
-
-
?
dibutyl 2,2,3,3-tetrafluorobutyl phosphate + H2O
dibutyl phosphate + ?
-
-
-
?
dibutyl 2,2,3,3-tetrafluorobutyl phosphate + H2O
dibutyl phosphate + ?
low activity
-
-
?
dibutyl 3,3-difluorobutyl phosphate + H2O
dibutyl phosphate + ?
very low activity
-
-
?
dibutyl 3,3-difluorobutyl phosphate + H2O
dibutyl phosphate + ?
low activity
-
-
?
diethyl (3,5,6-trichloropyridin-2-yl) phosphate + H2O
?
i.e. chlorpyrifos-oxon
-
-
?
diethyl (3,5,6-trichloropyridin-2-yl) phosphate + H2O
?
i.e. chlorpyrifos-oxon or CPO
-
-
?
diethyl 4-chlorophenyl phosphate + H2O
4-chlorophenol + diethyl phosphate
-
-
-
?
diethyl 4-chlorophenyl phosphate + H2O
4-chlorophenol + diethyl phosphate
-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
15.1% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
low activity
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
i.e. paraoxon
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
i.e. paraoxon
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
diethyl paraoxon + H2O
?
-
-
-
-
?
diethyl paraoxon + H2O
?
-
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
both docking and molecular dynamics simulations suggest that the only way paraoxon can be accommodated in the PON1 active site is by pushing Y71 out of the active site, causing the active site loop to take on a partially open conformation
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
diethyl-parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
diisopropyl fluorophosphate + H2O
?
-
-
-
-
?
diisopropyl fluorophosphate + H2O
?
-
-
-
-
?
diisopropyl fluorophosphate + H2O
?
-
-
-
?
diisopropyl fluorophosphate + H2O
?
-
high concentration of purified human serum paraoxonase 1 (about 0.075 mg) is required to hydrolyze 0.002 mM diisopropyl fluorophosphates
-
-
?
diisopropyl fluorophosphate + H2O
?
-
-
-
-
?
diisopropyl fluorophosphate + H2O
?
-
high concentration of purified rabbit serum paraoxonase 1 (about 0.025 mg) is required to hydrolyze 0.002 mM diisopropyl fluorophosphates
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
reaction of EC 3.1.8.2
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
reaction of EC 3.1.8.2, highly toxic structural analogue of G-class type of nerve agents
-
-
?
diisopropylfluorophosphate + H2O
diisopropyl phosphate + HF
-
-
-
-
?
diisopropylfluorophosphate + H2O
diisopropyl phosphate + HF
-
-
-
-
?
diisopropylfluorophosphate + H2O
diisopropyl phosphate + HF
-
-
-
-
?
dimethoate + H2O
?
-
-
-
?
dimethoate + H2O
?
-
0.2 mM, 14% degradation over 24 h by whole cells
-
-
?
dimethoate + H2O
?
-
0.2 mM, 14% degradation over 24 h by whole cells
-
-
?
dimethoate + H2O
?
-
0.2 mM, 16% degradation over 24 h by whole cells
-
-
?
dimethoate + H2O
?
-
0.2 mM, 16% degradation over 24 h by whole cells
-
-
?
dimethyl paraoxon + H2O
?
-
-
-
-
?
dimethyl paraoxon + H2O
?
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
fluorimetric detection on solid medium
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
dimethyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
ethyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl 1-methylethyl hydrogen phosphate
18.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
ethyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl 1-methylethyl hydrogen phosphate
low activity
-
-
?
ethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + ethyl hydrogen (1-methylpropyl)phosphonate
14.7% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
ethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + ethyl hydrogen (1-methylpropyl)phosphonate
-
-
-
?
ethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + ethyl hydrogen methylphosphonate
29.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
ethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + ethyl hydrogen methylphosphonate
low activity
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
ethyl paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
ethyl paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
ethyl paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
ethyl paraoxon + H2O
?
-
-
-
-
?
ethyl paraoxon + H2O
?
-
-
-
?
malathion + H2O
?
-
-
-
-
?
malathion + H2O
?
-
-
-
-
?
malathion + H2O
?
-
-
-
?
malathion + H2O
?
-
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
-
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
-
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
0.2 mM, 89% degradation over 24 h by whole cells
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
0.2 mM, 89% degradation over 24 h by whole cells
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
0.2 mM, 95% degradation over 24 h by whole cells
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
0.2 mM, 95% degradation over 24 h by whole cells
-
-
?
malathion + H2O
O,O-diethyl phosphorothioate + diethyl 2-mercaptosuccinate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
weak activity
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
O,O-dimethyl O-4-nitrophenyl phosphate
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
-
the enzyme reaction also produces two protons, which lower the pH and establish a steady pH gradient
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethylphosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
-
-
-
?
methyl parathion + H2O
?
-
-
-
-
?
methyl parathion + H2O
?
-
-
-
-
?
methyl parathion + H2O
?
-
-
-
-
?
methyl parathion + H2O
?
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
i.e. O,O-dimethyl O-4-nitrophenyl phosphorothioate
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
i.e. O,O-dimethyl O-4-nitrophenyl phosphorothioate
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
-
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VX
-
-
?
O-isobutyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. VR or Russian VX
-
-
?
O-isobutyl-S-(2-diethylaminoethyl)methylphosphonothiolate + H2O
?
i.e. RVX, VR, or Russian VX
-
-
?
O-isopropyl methylphosphonofluoridate + H2O
?
i.e. sarin
-
-
?
O-isopropyl methylphosphonofluoridate + H2O
?
i.e. sarin
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
the enzyme prevents, independent of compound aging, the inhibition of acetylcholinesterase by paraoxon, and also by VX, sarin and soman, the latter are phosphyloxime products of acetlycholinesterase reaction with organophosphate inhibitors, overview
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
preferred substrate
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
652704, 664153, 665987, 702421, 707155, 707214, 708095, 709262, 709264, 709291, 709755, 714112, 714893, 714895, 715738, 715744, 716957, 728992, 750345, 750484, 750511, 752173 -
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
ir
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
best substrate
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
enzyme variant Q192: 1.3% of the activity with phenyl acetate (see EC 3.1.1.2), enzyme variant R192: 1% of the activity with phenyl acetate (see EC 3.1.1.2). Enzyme protein also shows activities of EC 3.1.1.25 and EC 3.1.1.2
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
human serum paraoxonase/arylesterase is an esterase with broad substrate specificity. It occurs in two genetically determined allozymic forms, type A and type B. These allozymes are the products of two allelic genes located at the paraoxonase locus on chromosome 7, which is closely linked to the gene for cystic fibrosis. Paraoxonase activity of the B type isozyme is considerably higher and stimulated more by 1 M NaCl than A-type paraoxonase. The ratio of paraoxonase activity to arylesterase activity of the B-isozyme is about 8, and that of the A isozyme about 1
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
i.e. O,O'-diethyl-4-nitrophenyl phosphothioate
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
0.2 mM, 12% degradation over 24 h by whole cells
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
0.2 mM, 12% degradation over 24 h by whole cells
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
0.2 mM, 35% degradation over 24 h by whole cells
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
0.2 mM, 35% degradation over 24 h by whole cells
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
the enzyme from Sulfolobus solfataricus has a low paraoxonase activity
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
i.e. diethyl-4-nitrophenyl-phosphate
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethylphosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethylphosphate
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethylphosphate
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethylphosphate
-
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
paraoxon is diethyl 4-nitrophenyl phosphate
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
high activity with enzyme mutant C258L/I261F/W263A
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl phosphate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl phosphate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
35205, 35210, 35218, 35219, 646500, 646504, 646507, 664153, 677411, 677570, 677884, 678489, 693321 -
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
highest activity
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
paraoxonase and arylesterase activities are significantly lower in a Helicobacter pylori positive group than in a Helicobacter pylori negative group, overview
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenylphosphate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
A-type paraoxonase shows 0.06% of the activity with phenyl acetate, B-type paraoxonase shows 2.5% of the activity with phenyl acetate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
higher activity towards paraoxon than towards phenyl acetate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
paraoxonase activity of PON1 is polymorphism dependent
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
PON1 activity determined towards the synthetic compounds paraoxon and phenyl acetate reflects no association with markers of oxidative stress
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
the enzyme exists in two genetically determined allozymic forms, and these A and B allozymes possess both paraoxonase and arylesterase activities. B-type esterase has relatively higher paraoxonase activity and is stimulated to a greater degree by 1 M NaCl than the A allozyme
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
the homozygote RR phenotype of Q192R shows highest activity towards paraoxon
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
Meles taxus
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
0.2% of the activity with phenyl acetate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
paraoxon is the best substrate for the purified arylesterase
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
engneered mutant strain, parathion metabolism, overview
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
engneered mutant strain, parathion metabolism, overview
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
?
parathion + H2O
4-nitrophenol + diethyl thiophosphate
-
-
-
?
parathion + H2O
?
-
-
-
-
?
parathion + H2O
?
-
-
-
-
?
parathion + H2O
?
-
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
-
-
-
-
?
parathion + H2O
diethylthiophosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl thiophosphate
-
-
?
parathion + H2O
diethylthiophosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl thiophosphate
-
-
?
parathion + H2O
diethylthiophosphate + 4-nitrophenol
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
arylesterase activity
-
-
?
pirimiphos-methyloxon + H2O
?
-
-
-
-
?
pirimiphos-methyloxon + H2O
?
-
-
-
-
?
russian VX + H2O
methyl-phosphonothioic acid S-(2-diethylamino-ethyl) ester + 2-methylpropanol
-
-
-
-
?
russian VX + H2O
methyl-phosphonothioic acid S-(2-diethylamino-ethyl) ester + 2-methylpropanol
-
-
-
-
?
sarin + H2O
?
-
-
-
-
?
sarin + H2O
?
-
efficient hydrolysis of sarin (11 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
sarin + H2O
?
-
efficient hydrolysis of sarin (11 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
sarin + H2O
methyl-phosphonic acid monofluoride + isopropyl alcohol
-
-
-
-
?
sarin + H2O
methyl-phosphonic acid monofluoride + isopropyl alcohol
-
-
-
-
?
sarin + H2O
methyl-phosphonic acid monofluoride + isopropyl alcohol
PON1 hydrolyzes sarin more effectively than paraoxon, sarin is o-isopropyl methylphosphonofluoridate
-
-
?
sarin + H2O
methylphosphonofluoride acid + ?
-
a highly toxic organophosphorus nerve agent, stereospecific hydrolysis
-
-
?
sarin + H2O
methylphosphonofluoride acid + ?
-
a highly toxic organophosphorus nerve agent
-
-
?
soman + H2O
?
-
-
-
-
?
soman + H2O
?
-
efficient hydrolysis of soman (3 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
soman + H2O
?
-
efficient hydrolysis of soman (3 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
soman + H2O
methyl-phosphonic acid monofluoride + 1,2,2-trimethylpropanol
-
-
-
-
?
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
-
-
?
soman + H2O
methylphosphonofluoride acid + 3,3-dimethylbutan-2-ol
PON1 hydrolyzes soman more effectively than paraoxon, soman is o-pinacolyl methylphosphonofluoridate
-
-
?
soman + H2O
methylphosphonofluoride acid + 3,3-dimethylbutan-2-ol
-
i.e. pinacolyl methylphosphonofluoridate, a highly toxic organophosphorus nerve agent
-
-
?
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
-
-
?
SP-CMP + H2O
?
SP-CMP is the toxic SP enantiomer of a GF surrogate in which the fluoride leaving group is replaced by a coumarin derivative
-
-
?
tabun + H2O
?
-
-
-
-
?
tabun + H2O
?
-
efficient hydrolysis of tabun (100 nM) is observed with about 0.025-0.04 units of paraoxonase 1. Tabun hydrolysis with paraoxonase 1 is about 30-60times and about 200-260times more efficient than that with sarin and soman, respectively
-
-
?
tabun + H2O
?
-
a highly toxic organophosphorus nerve agent
-
-
?
tabun + H2O
?
-
efficient hydrolysis of tabun (100 nM) is observed with about 0.025-0.04 units of paraoxonase 1. Tabun hydrolysis with paraoxonase 1 is about 30-60times and about 200-260times more efficient than that with sarin and soman, respectively
-
-
?
tabun + H2O
cyanophosphonic acid dimethylamide + ethanol
-
-
-
-
?
tabun + H2O
cyanophosphonic acid dimethylamide + ethanol
-
-
-
-
?
tabun + H2O
cyanophosphonic acid dimethylamide + ethanol
-
-
-
-
?
VR + H2O
?
-
i.e. diethylamino-ethyl-O-isobutyl methylphosphonothioate
-
-
?
VR + H2O
?
-
i.e. diethylamino-ethyl-O-isobutyl methylphosphonothioate
-
-
?
VX + H2O
?
-
i.e. diisopropylamino-ethyl-O-ethyl methylphosphonothioate
-
-
?
VX + H2O
?
-
i.e. O-ethyl S-[2-diisopropylaminoethyl]methylphosphonothiolate
-
-
?
VX + H2O
?
-
i.e. diisopropylamino-ethyl-O-ethyl methylphosphonothioate
-
-
?
VX + H2O
S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol
-
-
-
-
?
VX + H2O
S-[2-(diisopropylamino)ethyl]-methylphosphonothioic acid + ethanol
-
-
-
-
?
additional information
?
-
substrate binding modes and structure, overview
-
-
?
additional information
?
-
-
substrate binding modes and structure, overview
-
-
?
additional information
?
-
-
overview on substrate specificity
-
-
?
additional information
?
-
the enzyme is involved in detoxification of a broad range of organophosphorus pesticides and chemical warfare agents sarin and VX
-
-
?
additional information
?
-
-
OPH catalyzes hydrolysis of organophosphorus compounds, OPC15-20, to give phosphoric or alkylphosphonic acid derivatives, which is accompanied by a decrease in the pH of the reaction medium through release of two protons
-
-
?
additional information
?
-
the enzyme also exhibits activity of EC 3.1.8.2, diisopropyl-fluorophosphatase. Enzyme-substrate docking study, overview
-
-
?
additional information
?
-
-
the enzyme also exhibits activity of EC 3.1.8.2, diisopropyl-fluorophosphatase. Enzyme-substrate docking study, overview
-
-
?
additional information
?
-
wild-type PTE exhibits little stereoselectivity against the relatively small phosphonate center of O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX, but the elevated pKa of the thiol-leaving group provides a significant challenge for enzyme-catalyzed hydrolysis. Wild-type PTE has enzymatic activity for the hydrolysis of racemic VR similar to VX, but the larger isobutyl group attached to the phosphorus center results in a 25fold preference for the RP-enantiomer. Computational docking study of wild-type and mutant enzymes with the substrates
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl phenyl ethylphosphonate and 1-methylpropyl 4-nitrophenyl ethylphosphonate
-
-
?
additional information
?
-
-
substrate specificities of wild-type enzyme and genetic variants, overview
-
-
?
additional information
?
-
substrate specificity of wild-type and genetic variants, overview
-
-
?
additional information
?
-
-
substrate specificities of wild-type enzyme and genetic variants, overview
-
-
?
additional information
?
-
substrate specificity of wild-type and genetic variants, overview
-
-
?
additional information
?
-
-
overview on substrate specificity
-
-
?
additional information
?
-
-
isozyme PON2 has antioxidant properties, prevents low density lipoprotein lipid peroxidation and reverses the oxidation of mildly oxidized low density lipoproteins
-
-
?
additional information
?
-
-
PON1 is involved in metabolism of oxidized lipid compounds
-
-
?
additional information
?
-
-
polymorphism of enzyme and implications
-
-
?
additional information
?
-
-
isozyme PON1 is effective at reducing the activity of phospholipid oxidation products
-
-
?
additional information
?
-
-
the enzyme PON2 has antioxidant properties, prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of mildly oxidized LDL to induce monocyte chemotaxis
-
?
additional information
?
-
-
HDL-associated enzyme is a cardio- and vasoprotective enzyme
-
-
?
additional information
?
-
-
the enzyme associated to high-density lipoproteins HDL exhibits antioxidant function of particular physiological relevance, mechanism, compositional fluctuations of HDL effects the influence of the enzyme on cardiovascular risks, overview, PON1 content is reduced in human ApoAI deficiency disease
-
-
?
additional information
?
-
-
the enzyme efficiently hydrolyzes organophosphorus nerve agents
-
-
?
additional information
?
-
-
the enzyme is important in detoxification of organophosphorus compounds, structure and applications of organophosphorus compounds, clinical evidence of PON1, overview
-
-
?
additional information
?
-
the serum paraoxonase family contains detoxifying and anti-atherosclerotic enzymes
-
-
?
additional information
?
-
-
enzyme-HDL complex: interaction and structure analysis
-
-
?
additional information
?
-
-
no activity with dimefox, parathion, methyl parathion, and diisopropyl fluorophosphate, assay method evaluation of analogues with fluorescent leaving groups for screening and selection of the enzyme that efficiently hydrolyzes organophosphorus nerve agents, overview
-
-
?
additional information
?
-
the enzyme associates to HDL in the blood stream
-
-
?
additional information
?
-
polymorphisms allele frequency in relation to exposure of individuals to organophosphates, overview
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-
?
additional information
?
-
-
polymorphisms allele frequency in relation to exposure of individuals to organophosphates, overview
-
-
?
additional information
?
-
-
PON1 has a protective role e.g. against organophosphorous poisoning, but also against vascular diseases, PON1 has an anti-atherogenic activity
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-
?
additional information
?
-
PON1 hydrolyses esters, including organophosphates and lactones, and exhibits anti-atherogenic properties, the enzyme is associated to high-density-lipoprotein, bound together with the human phosphate binding protein
-
-
?
additional information
?
-
-
PON1 is a high-density lipoprotein-associated enzyme capable of hydrolyzing diverse substrates from organophosphate toxins to oxidized phospholipids, PON1 is linked with both the prevention of organophosphate poisoning and inhibition of atherosclerosis initiated by oxidatively modified low-density lipoprotein, overview, phenotypic distribution of the enzyme in individuals of both sexes and different age, overview
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-
?
additional information
?
-
-
the enzyme depends on high-density lipoprotein HDL as carrier and site of action, PON1 acts as an antioxidant preventing low-density lipoprotein peroxidation, overview
-
-
?
additional information
?
-
-
PON1 is a high-density lipoprotein-associated enzyme capable of hydrolyzing diverse substrates from organophosphate toxins to oxidized phospholipids
-
-
?
additional information
?
-
-
PON1 is associated to HDL and human phosphate-binding protein
-
-
?
additional information
?
-
-
residues Phe222 and His115 are important in organophosphorus substrate specificity and catalysis
-
-
?
additional information
?
-
-
high-density lipoprotein-associated paraoxonase possesses peroxidase-like activity that can contribute to the protective effect of paraoxonase against lipoprotein oxidation. The presence of paraoxonase in high-density lipoprotein may thus be a major contributor to the antiatherogenicity of this lipoprotein
-
-
?
additional information
?
-
PON1 hydrolyzes organophosphates, such as paraoxon, aromatic esters, for instance, phenyl acetate, and also lipid peroxidation products, and reduces the accumulation of them, PON1 prevents the acceleration of atherosclerosis, exhibits antioxidant ability, and assumes an antiatherogenic property. Negative correlation between the activity of PON1 and the level of lipid hydroperoxides in the rheumatoid arthritis patient group, overview
-
-
?
additional information
?
-
PON1 is a lipolactonase that associates with HDL-apolipoprotein A-I and thereby plays a role in the prevention of atherosclerosis
-
-
?
additional information
?
-
-
PON1 is a lipolactonase that associates with HDL-apolipoprotein A-I and thereby plays a role in the prevention of atherosclerosis
-
-
?
additional information
?
-
PON1 is not able to prevent macrophage oxidative stress, however, is able to retard macrophage-induced low-density lipoprotein oxidation
-
-
?
additional information
?
-
PON1 plays a key role in the protection of low density lipoproteins and high density lipoproteins from oxidation by hydrolyzing activated phospholipids and lipid peroxide products
-
-
?
additional information
?
-
-
PON1 plays a key role in the protection of low density lipoproteins and high density lipoproteins from oxidation by hydrolyzing activated phospholipids and lipid peroxide products
-
-
?
additional information
?
-
the active site of PON1 is characterized by two distinct binding regions, the hydrophobic binding site for arylesters/lactones and the paraoxon binding site for phosphotriesters
-
-
?
additional information
?
-
-
the active site of PON1 is characterized by two distinct binding regions, the hydrophobic binding site for arylesters/lactones and the paraoxon binding site for phosphotriesters
-
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?
additional information
?
-
the enzyme carried by high-density lipoprotein, exerts a protective effect against oxidative damage of cells and lipoproteins, modulating the susceptibility of high-density lipoprotein to atherogenic modifications and has an anti-inflammatory role, low PON1 activity is a risk factor for cardiovascular disease
-
-
?
additional information
?
-
the enzyme is located on high-density lipoprotein and prevents low-density-lipoprotein and high-density-lipoprotein oxidation both in vivo and in vitro through hydrolysis of lipid peroxides, the risk of ischemic stroke is related to the genotype of PON1 192RQ polymorphisms, overview
-
-
?
additional information
?
-
no activity with chlorpyrifos oxon and diazoxon
-
-
?
additional information
?
-
no activity with chlorpyrifos oxon and diazoxon
-
-
?
additional information
?
-
the overall substrate preference of cAMPP is methylphosphonates > ethylphosphonates >/= organophosphates
-
-
?
additional information
?
-
the enzyme does not hydrolyse 4-nitrophenyl phenyl ethylphosphonate and 1-methylpropyl 4-nitrophenyl ethylphosphonate
-
-
?
additional information
?
-
-
is resistant to chlorpyrifos
-
-
?
additional information
?
-
-
recombinant human paraoxoanase 1 cannot hydrolyze dimethyl paraoxon even at higher concentrations used
-
-
?
additional information
?
-
-
the stereochemical preference of the wild-type enzyme with chemical warfare agents is for the RP enantiomers
-
-
?
additional information
?
-
human paraoxonase 1 (h-PON1) can hydrolyze a variety of substrates. Interaction of recombinant PON1 proteins with lactones, overview
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-
?
additional information
?
-
-
human paraoxonase 1 (h-PON1) can hydrolyze a variety of substrates. Interaction of recombinant PON1 proteins with lactones, overview
-
-
?
additional information
?
-
human PON1 is a calcium-dependent promiscuous enzyme (phosphotriesterase, arylesterase and lactonase) with a wide range of substrates. Human PON1 is capable of hydrolyzing a broad range of organophosphorus compounds, including paraoxon, diisopropylfluorophosphate (DFP) and nerve agents such as sarin, soman and VX
-
-
?
additional information
?
-
PON1 shows very good adaptability in assay development with different substrates, PON1 substrate exhibit many degrees of freedom in docking simulations. The relative chemiluminescent efficiency for the five acridinium esters ranks as the following descreasing order: unsubstituted, 2,4-dimethylphenoxy-, 4-methylphenoxy-, 4-tertbutylphenoxy-, and chloro-acridinium ester. Selfhydrolysis of the five acridinium esters in Tris-HCl buffer, at pH 7.5 and 25°C is insignificant during 22 min, but between 1.03% and 27.17% after 12 weeks
-
-
?
additional information
?
-
-
the enzyme is also active with substrates of EC 3.1.1.81, quorum-quenching N-acyl-homoserine lactonase, and EC 3.1.8.2, diisopropyl-fluorophosphatase, hydrolyzing diisopropyl-fluorophosphates and phosphorus-halide and phosphorus-cyanide bonds in organophosphorus compounds. Measurement of N-oxodecanoyl-DL-homoserine lactone (3O-C10AHL)-hydrolyzing activity (EC 3.1.1.81) of recombinant h-PON1 enzymes is determined by using a recombinant quorum-sensing reporter Escherichia coli strain
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?
additional information
?
-
the enzyme is also active with substrates of EC 3.1.1.81, quorum-quenching N-acyl-homoserine lactonase, and EC 3.1.8.2, diisopropyl-fluorophosphatase, hydrolyzing diisopropyl-fluorophosphates and phosphorus-halide and phosphorus-cyanide bonds in organophosphorus compounds. Measurement of N-oxodecanoyl-DL-homoserine lactone (3O-C10AHL)-hydrolyzing activity (EC 3.1.1.81) of recombinant h-PON1 enzymes is determined by using a recombinant quorum-sensing reporter Escherichia coli strain
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-
?
additional information
?
-
the recombinant His6-tagged organophosphorus hydrolase (His6-OPH) shows catalytic activity in hydrolytic reactions with methylphosphonic acid (MPA) monoesters and diesters being decomposition products of R-VX nerve agent derivative (O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX), analysis of the mechanism of C-P bond cleavage in methylphosphonic acid by His6-OPH, overview. The recombinant enzyme His6-OPH is capable of degrading the key organophosphorus components of reaction masses (RMs) that are produced by chemical detoxification of R-VX, the RMs are multisubstrate mixtures for this enzyme, R-VX decomposition scheme. GC-MS analysis of phosphonates and methane
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-
?
additional information
?
-
-
the enzyme associated to high-density lipoproteins HDL exhibits antioxidant function of particular physiological relevance, mechanism, compositional fluctuations of HDL effects the influence of the enzyme on cardiovascular risks, overview
-
-
?
additional information
?
-
-
enzyme-HDL complex: interaction and structure analysis
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
molecular docking of substrates to wild-type and mutant enzymes using the crystal structure of PON1 (PDB ID 3SRG with resolution 2.19 A), overview. The enzyme also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate
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-
?
additional information
?
-
th enzyme is also active with the chromogenic lactone thiobutyl-gamma-butyric lactone (TBBL), cf. EC 3.1.1.81. It has both lactonase activity and paraoxonase activity. Empirical valence bond simulations of PON1-catalyzed hydrolyses of paraoxon and TBBL, overview
-
-
?
additional information
?
-
the mammalian serum paraoxonase 1 (PON1) is a calcium-dependent serum esterase which catalyzes the hydrolysis of a broad range of organic esters and organophosphorous (OP) compounds. PON1 is a lactonase with native substrates gamma- and delta-lactones which have long alkyl side chains, and PON1 possesses promiscuous OP hydrolase activity, particularly on paraoxon, which is attributed to its considerable plasticity of catalytic structure
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-
?
additional information
?
-
the mammalian serum paraoxonase 1 (PON1) is a calcium-dependent serum esterase which catalyzes the hydrolysis of a broad range of organic esters and organophosphorous (OP) compounds. PON1 is a lactonase with native substrates gamma- and delta-lactones which have long alkyl side chains, and PON1 possesses promiscuous OP hydrolase activity, particularly on paraoxon, which is attributed to its considerable plasticity of catalytic structure
-
-
?
additional information
?
-
-
improved degradation of organophosphorus pesticides by the engineered cell surface-expressed PON1 of transformeted strain JS444
-
-
?
additional information
?
-
-
improved degradation of organophosphorus pesticides by the engineered cell surface-expressed PON1 of transformeted strain JS444
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
enzyme additionally displays L-homoserine lactonase activity, EC 3.1.1.81
-
-
?
additional information
?
-
-
enzyme additionally displays L-homoserine lactonase activity, EC 3.1.1.81
-
-
?
additional information
?
-
-
enzyme additionally displays L-homoserine lactonase activity, EC 3.1.1.81
-
-
?
additional information
?
-
-
enzyme additionally displays L-homoserine lactonase activity, EC 3.1.1.81
-
-
?
additional information
?
-
-
a organophosphate-degrading enzyme
-
-
?
additional information
?
-
-
substrate specificity with organophosphorous compounds, overview
-
-
?
additional information
?
-
the enzyme possesses phosphotriesterase and a very high lactonase activity, structure-function relationship, overview
-
-
?
additional information
?
-
-
the enzyme possesses phosphotriesterase and a very high lactonase activity, structure-function relationship, overview
-
-
?
additional information
?
-
the phosphotriesterase-like lactonase enzyme is bifunctional showing lactonase (EC 3.1.1.81) and phosphotriesterase (EC 3.1.8.1 and 3.1.8.2) activities
-
-
?
additional information
?
-
substrate docking analysis. The C258 residue in the active site is involved in an interaction with the oxygen atom from the amide in the lactone analogue
-
-
?
additional information
?
-
the enzyme shows lactonase activity with N-(3-oxodecanoyl)-L-homoserine lactone, undecanoic-gamma-lactone, and undecanoic-delta-lactone, cf. EC 3.1.1.81
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-
?
additional information
?
-
-
the enzyme shows lactonase activity with N-(3-oxodecanoyl)-L-homoserine lactone, undecanoic-gamma-lactone, and undecanoic-delta-lactone, cf. EC 3.1.1.81
-
-
?
additional information
?
-
-
a organophosphate-degrading enzyme
-
-
?
additional information
?
-
-
substrate specificity with organophosphorous compounds, overview
-
-
?
additional information
?
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
additional information
?
-
-
organophosphate hydrolase interacts with Ton components and is targeted to the membrane only in the presence of the ExbB/ExbD complex
-
-
?
additional information
?
-
OPH is known to cleave the third ester linkage found in structurally diverse groups of organophosphorous compounds
-
-
?
additional information
?
-
-
OPH is known to cleave the third ester linkage found in structurally diverse groups of organophosphorous compounds
-
-
?
additional information
?
-
reactions are performed with soluble recombinant enzyme in solution or immobilized recombinant enzyme in calcium alginate gel
-
-
?
additional information
?
-
-
reactions are performed with soluble recombinant enzyme in solution or immobilized recombinant enzyme in calcium alginate gel
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-
?
additional information
?
-
phosphotriesterase from Sphingobium sp. TCM1 (Sb-PTE) possesses a rather broad substrate profile and is able to hydrolyze insecticides, plasticizers, and flame retardants that are not typically substrates for other enzymes of this class
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?
additional information
?
-
enzyme substrate specificity analysis, optimization of the assay method, overview. Sb-PTE is capable of hydrolyzing a wide range of organophosphate triester substrates. Broensted analysis, P-O bond cleavage is rate limiting for kcat and kcat/Km for the dibutyl series of substrates tested. The enzyme must be able to effectively protonate the leaving group for efficient catalysis, but the lack of loss of activity at high pH is inconsistent with a separate general acid serving this role, unless it occurs after the rate-limiting step. The absence of a solvent viscosity effect and the magnitude of the 18O-isotope effects are consistent with nucleophilic attack of hydroxide as the rate-limiting step during the hydrolysis of substrates by this enzyme
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-
?
additional information
?
-
multiple reaction products from the hydrolysis of chiral and prochiral organophosphate substrates, substrate specificity and differential hydrolysis of the prochiral substituents, analysis of the enantioselectivity, overview
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-
?
additional information
?
-
no hydrolysis: ethyl parathion. The enzyme also shows activity of 1,4-lactonase (EC 3.1.1.25) and arylesterase (EC 3.1.1.2)
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-
?
additional information
?
-
-
no hydrolysis: ethyl parathion. The enzyme also shows activity of 1,4-lactonase (EC 3.1.1.25) and arylesterase (EC 3.1.1.2)
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-
?
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0.088
(1E)-but-1-en-1-yl dibutyl phosphate
pH 9.0, 25°C
0.35 - 3.2
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
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
0.15 - 4
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
0.03 - 4.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
0.31
4-acetylphenyl cyclohexyl methyl (R)-phosphate
pH 8.5, 30°C
0.12
4-acetylphenyl cyclohexyl methyl (S)-phosphate
pH 8.5, 30°C
0.55
4-carbamoylphenyl diethyl phosphate
pH and temperature not specified in the publication
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
0.091 - 0.2
7-diethylphospho-6,8-difluor-4-methylumbelliferyl
0.032 - 0.51
chlorpyrifos
0.642
CMP-coumarin
pH 8.3, 25°C
0.071
Coumaphos
-
pH 7.2, 25°C
0.059
cyclohexyl ethyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
0.054
cyclohexyl ethyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
1.1
cyclohexyl methyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
0.053
cyclohexyl methyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
0.006
cyclohexyl methyl phenyl (R)-phosphate
pH 8.5, 30°C
1.2 - 23.31
demeton-S methyl
1.33
diazoxon
recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2
0.05 - 0.11
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
0.17
dibutyl 3,3-difluorobutyl phosphate
pH 9.0, 25°C
0.43
dibutyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
0.15
dibutyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
0.14
dibutyl phenyl phosphate
pH and temperature not specified in the publication
0.95
diethyl 2,4,6-trifluorophenyl phosphate
pH and temperature not specified in the publication
0.39
diethyl 2,4-difluorophenyl phosphate
pH and temperature not specified in the publication
1.1
diethyl 2,6-difluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
0.63
diethyl 2-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
1.3
diethyl 2-fluorophenyl phosphate
pH and temperature not specified in the publication
0.25
diethyl 3-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
0.27
diethyl 3-fluorophenyl phosphate
pH and temperature not specified in the publication
0.24
diethyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
0.41 - 7
diethyl 4-chlorophenyl phosphate
0.3 - 0.6
diethyl 4-chlorophenyl thiophosphate
0.67
diethyl 4-cyanophenyl phosphate
pH and temperature not specified in the publication
1.6
diethyl 4-fluorophenyl phosphate
pH and temperature not specified in the publication
1.2
diethyl 4-formylphenyl phosphate
pH and temperature not specified in the publication
0.44
diethyl 4-methoxyphenyl phosphate
pH and temperature not specified in the publication
0.083 - 1.9
diethyl 4-nitrophenyl phosphate
0.67 - 0.889
diethyl paraoxon
0.46
diethyl pentafluoro-phenyl phosphate
pH and temperature not specified in the publication
1.1
diethyl phenyl phosphate
pH and temperature not specified in the publication
0.0017 - 1.586
diethyl-paraoxon
0.0086
diethylumbelliferyl phosphate
-
pH 7.5, 25°C, recombinant mutant enzyme G137D
0.76
dimethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
0.5 - 1.3
dimethyl-paraoxon
2.1
ethyl paraoxon
-
at 35°C, pH 9.0
0.345
ethyl phenyl parathion
-
-
0.581
ethyl-paraoxon
pH 8.0, 70°C
0.061
methyl 4-nitrophenyl phenyl (R)-phosphate
pH 8.5, 30°C
0.25
methyl 4-nitrophenyl phenyl (S)-phosphate
pH 8.5, 30°C
2.3
methyl 4-nitrophenyl propan-2-yl (R)-phosphate
pH 8.5, 30°C
0.036
methyl 4-nitrophenyl propan-2-yl (S)-phosphate
pH 8.5, 30°C
1
methyl 4-[(diethoxyphosphoryl)oxy]benzoate
pH and temperature not specified in the publication
0.08
methyl bis(4-nitrophenyl) phosphate
pH 8.5, 30°C
0.05 - 2.79
methyl paraoxon
0.052 - 0.41
methyl parathion
0.073 - 1.22
methylparathion
4.6
O,O'-(diisobutyl)methylphosphonate
pH 10.5, 25°C, recombinant His6-tagged enzyme
0.085
O,O,S-tributyl phosphorothioate
pH 9.0, 25°C
1400
O-(isobutyl)methylphosphonate
pH 10.5, 25°C, recombinant His6-tagged enzyme
0.2
O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate
0.5
O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
4
pentafluorophenyl diethyl phosphate
pH 8.0
0.187
phosmet
-
pH 7.2, 25°C
0.15 - 5.87
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
additional information
additional information
-
0.35
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
0.6
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.65
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
0.73
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
0.76
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
0.8
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
0.87
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant wild-type enzyme
1
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
1.2
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
1.4
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
1.6
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
2.8
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
3.2
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
0.15
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
0.16
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
0.18
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
0.23
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
0.36
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
0.41
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
0.62
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.71
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
1.4
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
1.7
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
1.7
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
2
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
2.1
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
4
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
0.03
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
0.13
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
0.18
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
0.18
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
0.19
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
0.19
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
0.2
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
0.23
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
0.24
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
0.31
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
1.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
1.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
1.7
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
4.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
0.091
7-diethylphospho-6,8-difluor-4-methylumbelliferyl
-
pH 8.0, 37°C, recombinant isozyme L55R192 PON1
0.2
7-diethylphospho-6,8-difluor-4-methylumbelliferyl
-
pH 8.0, 37°C, recombinant isozyme L55Q192 PON1
0.032
chlorpyrifos
pH 8.0, 37°C, genetic variant B2136
0.131
chlorpyrifos
recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2
0.14
chlorpyrifos
pH 8.0, 37°C, genetic variant B3561
0.19
chlorpyrifos
pH 8.0, 37°C, genetic variant 22A11
0.22
chlorpyrifos
pH 8.0, 37°C, genetic variant B1368
0.26
chlorpyrifos
pH 8.0, 37°C, wild-type enzyme
0.27
chlorpyrifos
pH 8.0, 37°C, genetic variant A1467
0.51
chlorpyrifos
pH 8.0, 37°C, genetic variant A1030
0.236
demeton-S
-
pH 7.2, 25°C
1.9
demeton-S
mutant enzyme H257L, in tripart buffer (pH 8.0)
4.2
demeton-S
mutant enzyme H254R, in tripart buffer (pH 8.0)
4.4
demeton-S
wild type enzyme, in tripart buffer (pH 8.0)
6.1
demeton-S
-
at 35°C, pH 7.2
6.2
demeton-S
mutant enzyme H254R/H257L, in tripart buffer (pH 8.0)
7.6
demeton-S
mutant enzyme H254R/H257F, in tripart buffer (pH 8.0)
1.2
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
3.64
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
4.18
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
8.09
demeton-S methyl
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
23.31
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.05
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
0.11
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
0.41
diethyl 4-chlorophenyl phosphate
pH and temperature not specified in the publication
1.6
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
3.3
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
7
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
0.3
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
0.5
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
0.6
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
0.083
diethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
0.32
diethyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
0.34
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
0.74
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
1.9
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
0.67
diethyl paraoxon
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.772
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.889
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.0017
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
0.0036
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
0.0053
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
0.0053
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant H254Q/H257F
0.0054
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
0.0056
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
0.0067
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
0.0072
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.008
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
0.0092
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N
0.0092
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
0.011
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
0.021
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
0.022
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
0.025
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
0.033
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.081
diethyl-paraoxon
pH 9.0, 30°C, recombinant wild-type enzyme
0.107
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C, with 0.025% SDS
0.325
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C, with 0.025% SDS
0.38
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C
0.53
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
0.81
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
1.586
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C
0.5
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192N
0.9
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192I
0.9
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192K
0.9
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutants H115W
1.1
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192S
1.2
dimethyl-paraoxon
pH 8.0, 25°C, recombinant wild-type enzyme
1.2
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192A
1.3
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192W
0.16
malathion
25°C, pH 9.0
0.29
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.33
malathion
25°C, pH 9
0.351
malathion
-
pH 7.2, 25°C
0.41
malathion
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.67
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.82
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
1.16
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.05
methyl paraoxon
25°C, pH 9, mutant enzyme E14K
0.138
methyl paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
0.205
methyl paraoxon
-
pH 8.0, 70°C, recombinant enzyme
0.246
methyl paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.261
methyl paraoxon
25°C, pH 9, mutant enzyme Y34Q
0.27
methyl paraoxon
-
at 35°C, pH 9.0
0.278
methyl paraoxon
pH 8.3, 25°C
0.62
methyl paraoxon
25°C, pH 9, mutant enzyme E14K/Y34Q
1.4
methyl paraoxon
pH 9.0, 75°C
1.74
methyl paraoxon
25°C, pH 9, wild-type enzyme
2.14
methyl paraoxon
25°C, pH 9.0
2.79
methyl paraoxon
pH 8.0, 70°C
0.052
methyl parathion
-
pH 7.2, 25°C
0.12
methyl parathion
25°C, pH 9.0
0.272
methyl parathion
25°C, pH 9
0.36
methyl parathion
pH 9.1, 37°C, recombinant enzyme in presence of Co2+
0.41
methyl parathion
pH 9.1, 37°C, recombinant enzyme in absence of Co2+
0.073
methylparathion
-
pH 10.5, 20°C, recombinant His6-tagged OPH
0.21
methylparathion
-
pH 9.0, 20°C, native OPH
1.22
methylparathion
-
pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
0.2
O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate
mutant enzyme Q192R, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.2
O-ethyl S-2-diisopropylaminoethyl methylphosphonothiolate
wild type enzyme, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.005
paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.01
paraoxon
-
pH 10.5, 20°C, recombinant His6-tagged OPH
0.01
paraoxon
-
pH 10.5, 25°C, recombinant His6-tagged wild-type OPH
0.012
paraoxon
mutant H254R, pH 9.0, 25°C
0.016
paraoxon
-
pH 9.0, 20°C, native OPH
0.03
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K
0.033
paraoxon
-
pH 7.2, 25°C
0.035
paraoxon
wild-type enzyme
0.05
paraoxon
mutant enzyme H254R/H257F, in 20 mM CHES buffer (pH 9.0) at 25°C
0.06
paraoxon
-
pH 8.0, 70°C, recombinant enzyme
0.064
paraoxon
pH 8.0, 70°C, wild-type enzyme
0.07
paraoxon
mutant enzyme H254R/H257L, in 20 mM CHES buffer (pH 9.0) at 25°C
0.075
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W
0.08
paraoxon
-
pH 8.0, 37°C
0.085
paraoxon
pH 8.0, recombinant genetic variant G1A5
0.088
paraoxon
pH 8.0, recombinant genetic variant G3H8
0.089
paraoxon
pH 8.0, recombinant genetic variant G2E6
0.09
paraoxon
mutant enzyme H254R, in 20 mM CHES buffer (pH 9.0) at 25°C
0.094
paraoxon
pH 8.0, recombinant genetic variant G3C9
0.1
paraoxon
pH 8.0, recombinant genetic variant G2D6
0.1
paraoxon
wild type enzyme, in 20 mM CHES buffer (pH 9.0) at 25°C
0.104
paraoxon
-
pH 10.5, 25°C, 3-fluorotyrosine-containing recombinant His6-tagged OPH
0.12
paraoxon
wild-type enzyme, pH 9.0, 25°C
0.12
paraoxon
pH 8.0, recombinant genetic variant G1C4
0.12
paraoxon
-
pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
0.132
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.14
paraoxon
mutant E313A, pH 10.5, 25°C
0.15
paraoxon
mutant H115W/N133S, pH 10.5, 25°C
0.15
paraoxon
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.153
paraoxon
pH 8.0, 70°C, mutant enzyme W263F
0.16
paraoxon
wild-type, pH 10.5, 25°C
0.17
paraoxon
mutant N133S, pH 10.5, 25°C
0.18
paraoxon
mutant G11A and mutant G11S, pH 10.5, 25°C
0.19
paraoxon
mutant E314A and mutant G11C, pH 10.5, 25°C
0.19
paraoxon
pH 10.5, 25°C, mutant enzyme H115W/N133S
0.25
paraoxon
pH 10.5, 25°C, wild-type enzyme
0.26
paraoxon
Zn2+-PTE, at pH 8.5 and 30°C
0.27
paraoxon
enzyme variant R192
0.271
paraoxon
-
pH 7.4, 37°C, type B paraoxonase
0.271
paraoxon
-
pH 8.0, 25°C, enzyme from phenotype B blood plasma
0.272
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/W263F
0.29
paraoxon
-
37°C, pH 10.0
0.29
paraoxon
-
native enzyme, in 50 mM borate buffer (pH 8.5, 0.1 mM CoCl2), at 25°C
0.3
paraoxon
mutant enzyme H257L, in 20 mM CHES buffer (pH 9.0) at 25°C
0.31
paraoxon
pH 8.5, 25°C, wild-type enzyme
0.32
paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
0.34
paraoxon
Co2+-PTE mutant H123N, at pH 8.5 and 30°C
0.345
paraoxon
surface-displayed recombinant enzyme from fresh cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C
0.347
paraoxon
surface-displayed recombinant enzyme from freeze-thawed cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C
0.36
paraoxon
Co2+-PTE mutant H123I, at pH 8.5 and 30°C
0.39
paraoxon
Co2+-PTE mutant H123A, at pH 8.5 and 30°C
0.4
paraoxon
-
37°C, pH 7.4
0.4
paraoxon
Co2+-PTE, at pH 8.5 and 30°C
0.41
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I261F
0.42
paraoxon
mutant H115W, pH 10.5, 25°C
0.43
paraoxon
pH 10.5, 25°C, mutant enzyme H115W
0.49 - 2
paraoxon
-
R192 isoenzyme, at pH 8.0 and 37°C
0.5
paraoxon
enzyme variant Q192
0.5
paraoxon
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
0.503
paraoxon
-
pH 7.4, 37°C, type A paraoxonase
0.503
paraoxon
-
pH 8.0, 25°C, enzyme from phenotype A blood plasma
0.51
paraoxon
pH 8.0, recombinant genetic variant G3A5
0.54
paraoxon
pH 8.0, wild-type enzyme
0.56
paraoxon
-
isozyme 192R, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
0.599
paraoxon
-
Q192 isoenzyme, at pH 8.0 and 37°C
0.75
paraoxon
pH 8.0, recombinant genetic variant G3G3
0.75
paraoxon
pH 8.0, mutant enzyme H134Q
0.8
paraoxon
recombinant enzyme
0.8
paraoxon
pH 8.0, recombinant genetic variant G2C2
0.8
paraoxon
pH 8.0, recombinant genetic variant G3H9
0.8
paraoxon
mutant H115W/R192Q, pH 8.0, 25°C
0.86
paraoxon
pH 8.0, wild-type enzyme
0.868
paraoxon
recombinant wild type enzyme, in 0.1 M Tris-HCl (pH 8.5), 2 M NaCl, and 2 mM CaCl2
0.9
paraoxon
pH 8.3, activity buffer
0.9
paraoxon
pH 8.3, activity buffer with 0.1% tergitol
0.9
paraoxon
mutant H115W, pH 8.0, 25°C
0.9
paraoxon
mutant H115W/R192K, pH 8.0, 25°C
0.94
paraoxon
wild type enzyme, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.96
paraoxon
-
isozyme 192Q, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
1.047
paraoxon
intracellular-expressed recombinant enzyme from fresh cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C
1.051
paraoxon
intracellular expressed recombinant enzyme from freeze-thawed cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C
1.1
paraoxon
pH 8.0, recombinant genetic variant G1B11
1.1
paraoxon
70°C, pH not specified in the publication
1.18
paraoxon
pH 8.0, mutant enzyme H115Q/H134Q
1.2
paraoxon
wild-type, pH 8.0, 25°C
1.2
paraoxon
mutant enzyme Q192R, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
1.2
paraoxon
pH 8.0, temperature not specified in the publication
1.2
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I98F/I261F
1.3
paraoxon
-
2 mM substrate, at pH 8.0 and 37°C
1.35
paraoxon
pH 8.0, mutant enzyme H115Q
1.42
paraoxon
pH 7.4, 25°C
1.5
paraoxon
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
1.63
paraoxon
-
pH 8.5, 37°C, enzyme form M2
1.69
paraoxon
-
37°C, pH 8.5
2
paraoxon
25°C, 0.1% SDS, pH not specified in the publication
2.36
paraoxon
pH 8.0, 70°C
2.5
paraoxon
pH 8.0, recombinant genetic variant G1A7
2.5
paraoxon
-
serum enzyme, pH 8.0, 37°C
2.69
paraoxon
-
pH 8.5, 37°C, enzyme form M1
3.27
paraoxon
70°C, pH 9.0
4.16
paraoxon
-
pH 8.0, 37°C
4.16
paraoxon
-
liver enzyme, pH 8.0, 37°C
4.2
paraoxon
25°C, 0.01% SDS, pH not specified in the publication
5.44
paraoxon
25°C, pH not specified in the publication, wild-type enzyme
24.25
paraoxon
25°C, pH 9.0
0.015
parathion
-
pH 10.5, 20°C, recombinant His6-tagged OPH
0.058
parathion
-
pH 7.2, 25°C
0.06
parathion
-
pH 9.0, 20°C, native OPH
0.434
parathion
pH 8.3, 25°C
0.6
parathion
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
1.5
parathion
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
1.7
parathion
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
1.4
phenyl acetate
-
pH 8.0, wild-type enzyme
3.5
phenyl acetate
-
pH 8.0, recombinant enzyme
0.15
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, pH 8.5, temperature not specified in the publication
5.87
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
mutant L271A/Y309A, pH 8.5, temperature not specified in the publication
0.074
sarin
mutant enzyme Q192R, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.21
sarin
wild type enzyme, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.27
soman
wild type enzyme, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
0.44
soman
mutant enzyme Q192R, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C
additional information
additional information
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-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
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kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
Km values of paraoxon hydrolysis with different metal ions in the active site
-
additional information
additional information
-
Km values of paraoxon hydrolysis with different metal ions in the active site
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
kinetic evaluation, mutant H254R
-
additional information
additional information
kinetics of the Zn-enzyme and the Cd-enzyme, wild-type and mutant, kinetic model, overview
-
additional information
additional information
-
kinetics of the Zn-enzyme and the Cd-enzyme, wild-type and mutant, kinetic model, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
-
first order kinetics
-
additional information
additional information
-
first order rate kinetics of the immobilized enzyme, overview
-
additional information
additional information
kinetic modelling, molecular dynamic docking studies and density functional theory calculations, overview
-
additional information
additional information
-
kinetic modelling, molecular dynamic docking studies and density functional theory calculations, overview
-
additional information
additional information
-
kinetics for diverse random mutant variants, overview
-
additional information
additional information
-
kinetics of recombinant His6-tagged wild-type OPH and 3-fluorotyrosine-containing recombinant His6-tagged OPH
-
additional information
additional information
-
classical Michaelis-Menten kinetics
-
additional information
additional information
classical Michaelis-Menten kinetics
-
additional information
additional information
classical Michaelis-Menten kinetics
-
additional information
additional information
classical Michaelis-Menten kinetics
-
additional information
additional information
heavy atom isotope effect measurements, competitive method
-
additional information
additional information
Michaelis-Menten kinetics, kinetic analysis of phosphotriesterase activity
-
additional information
additional information
reaction kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
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reaction kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
rhPON1-mediated hydrolyses of the acridinium esters obey first-order reaction kinetics, kinetic analysis of serum-catalyzed and recombinant enzyme-catalyzed hydrolysis of acridinium esters, detailed overview
-
additional information
additional information
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stopped-flow kinetics, Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.83
(1E)-but-1-en-1-yl dibutyl phosphate
pH 9.0, 25°C
1.1 - 51
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
5
1,2,2-trimethylpropyl methylphosphonofluoridate
-
-
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
0.41 - 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
17 - 174
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
3 - 166
4-acetylphenyl (S)-2-methylpropyl 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
0.36
4-acetylphenyl cyclohexyl methyl (R)-phosphate
pH 8.5, 30°C
0.38
4-acetylphenyl cyclohexyl methyl (S)-phosphate
pH 8.5, 30°C
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
0.8
4-carbamoylphenyl diethyl phosphate
pH and temperature not specified in the publication
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
0.28
CMP-coumarin
pH 8.3, 25°C
949
Coumaphos
-
pH 7.2, 25°C
2.5
cyclohexyl ethyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
2.8
cyclohexyl ethyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
6
cyclohexyl methyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
1.11
cyclohexyl methyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
0.38
cyclohexyl methyl phenyl (R)-phosphate
pH 8.5, 30°C
13.16 - 69.44
demeton-S methyl
0.045 - 0.36
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
0.043
dibutyl 3,3-difluorobutyl phosphate
pH 9.0, 25°C
2.5
dibutyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
7.5
dibutyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
4.4
dibutyl phenyl phosphate
pH and temperature not specified in the publication
71
diethyl 2,4,6-trifluorophenyl phosphate
pH and temperature not specified in the publication
13
diethyl 2,4-difluorophenyl phosphate
pH and temperature not specified in the publication
93
diethyl 2,6-difluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
40
diethyl 2-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
21
diethyl 2-fluorophenyl phosphate
pH and temperature not specified in the publication
107
diethyl 3-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
81
diethyl 3-fluorophenyl phosphate
pH and temperature not specified in the publication
0.6
diethyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
0.13 - 40
diethyl 4-chlorophenyl phosphate
1.1 - 2.4
diethyl 4-chlorophenyl thiophosphate
93
diethyl 4-cyanophenyl phosphate
pH and temperature not specified in the publication
78
diethyl 4-fluorophenyl phosphate
pH and temperature not specified in the publication
31
diethyl 4-formylphenyl phosphate
pH and temperature not specified in the publication
2.5
diethyl 4-methoxyphenyl phosphate
pH and temperature not specified in the publication
6.5 - 2500
diethyl 4-nitrophenyl phosphate
4.3 - 16.2
diethyl paraoxon
167
diethyl pentafluoro-phenyl phosphate
pH and temperature not specified in the publication
71
diethyl phenyl phosphate
pH and temperature not specified in the publication
0.104 - 2230
diethyl-paraoxon
1.3
diethylumbelliferyl phosphate
-
pH 7.5, 25°C, recombinant mutant enzyme G137D
698
dihydrocoumarin
-
recombinant PON3
41
diisopropylfluorophosphate
-
-
9.1
dimethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
0.1 - 10.7
dimethyl-paraoxon
0.24
ethyl acetate
pH 8.0, genetic variant PON1 G2E6
0.115
ethyl paraoxon
-
at 35°C, pH 9.0
0.00108
ethyl-paraoxon
pH 8.0, 70°C
56
isopropylmethylphosphonofluoridate
-
-
6.3
methyl 4-nitrophenyl phenyl (R)-phosphate
pH 8.5, 30°C
0.6
methyl 4-nitrophenyl phenyl (S)-phosphate
pH 8.5, 30°C
5
methyl 4-nitrophenyl propan-2-yl (R)-phosphate
pH 8.5, 30°C
2.05
methyl 4-nitrophenyl propan-2-yl (S)-phosphate
pH 8.5, 30°C
3.2
methyl 4-[(diethoxyphosphoryl)oxy]benzoate
pH and temperature not specified in the publication
9
methyl bis(4-nitrophenyl) phosphate
pH 8.5, 30°C
0.00783 - 342
methyl paraoxon
0.0011 - 1152
methyl parathion
2300
methylparathion
-
pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
0.42
O,O,S-tributyl phosphorothioate
pH 9.0, 25°C
0.1
O-isobutyl-S-[2-(diethylamino)ethyl]methylphosphonothioic acid
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
0.6 - 678
pentafluorophenyl diethyl phosphate
771
phosmet
-
pH 7.2, 25°C
0.55 - 11.72
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
0.167 - 4.95
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
0.007 - 0.15
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
0.15 - 0.5
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
1.83 - 6.467
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
additional information
additional information
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-
1.1
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant wild-type enzyme
3 - 6
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
5.1
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
6.1
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
8.6
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
13
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
14
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
16
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
19
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
22
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
23
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
31
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
51
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.27
2,4-dinitrophenyl diethyl phosphate
pH 8.0
9160
2,4-dinitrophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.062
2,6-difluorophenyl diethyl phosphate
pH 8.0
950
2,6-difluorophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
10.2
3,5-dinitrophenyl diethyl phosphate
pH 8.0
1477
3,5-dinitrophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.178
3-cyanophenyl diethyl phosphate
pH 8.0
1610
3-cyanophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.0011
3-fluorophenyl diethyl phosphate
pH 8.0
656
3-fluorophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.076
3-nitrophenyl diethyl phosphate
pH 8.0
840
3-nitrophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.41
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
2
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.2
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
3.4
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
8.5
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.21
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.45
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.62
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
1.5
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.016
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.12
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
2.1
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.9
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
17
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
45
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
46
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
50
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
55
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
57
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
58
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
72
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
84
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
100
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
101
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
122
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
160
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
174
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
3 - 6
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
8.1
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
8.7
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
14
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
21
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
25
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
29
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
33
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
40
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
51
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
53
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
56
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
159
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
166
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
20
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
37
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
51
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
93
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
110
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
12
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
22
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
50
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
100
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.81
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
5.9
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
93
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
150
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
0.14
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
5.1
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
19
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
7.3
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
14
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
110
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
130
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
150
4-acetylphenyl ethyl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
110
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
190
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
290
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
410
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
670
4-acetylphenyl ethyl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
18
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
100
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
120
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
250
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
7.4
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
15
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
40
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
92
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
370
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.0008
4-chlorophenyl diethyl phosphate
pH 8.0
848
4-chlorophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.4
4-cyanophenyl diethyl phosphate
pH 8.0
7495
4-cyanophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
0.44
4-diethyl phosphate acetophenone
pH 8.0
8080
4-diethyl phosphate acetophenone
pH 8.0, genetic variant PON1 G2E6
0.47
4-diethyl phosphate benzaldehyde
pH 8.0
12620
4-diethyl phosphate benzaldehyde
pH 8.0, genetic variant PON1 G2E6
4.8
4-nitrophenyl diethyl phosphate
pH 8.0
10520
4-nitrophenyl diethyl phosphate
pH 8.0, genetic variant PON1 G2E6
2.2
chlorpyrifos
pH 8.0, 37°C, wild-type enzyme
73.8
chlorpyrifos
pH 8.0, 37°C, wild-type enzyme
1430
chlorpyrifos
pH 8.0, 37°C, genetic variant A1467
2610
chlorpyrifos
pH 8.0, 37°C, genetic variant A1030
3540
chlorpyrifos
pH 8.0, 37°C, genetic variant B2136
20100
chlorpyrifos
pH 8.0, 37°C, genetic variant 22A11
21500
chlorpyrifos
pH 8.0, 37°C, genetic variant B1368
30900
chlorpyrifos
pH 8.0, 37°C, genetic variant B3561
0.0006
demeton-S
-
at 35°C, pH 7.2
3.3
demeton-S
mutant enzyme H257L, in tripart buffer (pH 8.0)
3.5
demeton-S
wild type enzyme, in tripart buffer (pH 8.0)
32
demeton-S
mutant enzyme H254R, in tripart buffer (pH 8.0)
34
demeton-S
mutant enzyme H254R/H257F, in tripart buffer (pH 8.0)
50
demeton-S
mutant enzyme H254R/H257L, in tripart buffer (pH 8.0)
650
demeton-S
-
pH 7.2, 25°C
13.16
demeton-S methyl
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
14.62
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
45.95
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
48.27
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
69.44
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.045
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
0.36
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
0.13
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
0.23
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
0.36
diethyl 4-chlorophenyl phosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
40
diethyl 4-chlorophenyl phosphate
pH and temperature not specified in the publication
1.1
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
2.2
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
2.4
diethyl 4-chlorophenyl thiophosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
6.5
diethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
32
diethyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
2060
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
2300
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
2500
diethyl 4-nitrophenyl phosphate
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
4.3
diethyl paraoxon
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
5.7
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
16.2
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.104
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
0.202
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
6.91
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C
8.6
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C, with 0.025% SDS
15
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
31.7
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C, with 0.025% SDS
33
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
35
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
38
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
41
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant H254Q/H257F
48
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
58
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N
66
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
71.05
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C
85
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
103
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
108
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
116
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
131
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
446
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
456
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
545
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
2230
diethyl-paraoxon
pH 9.0, 30°C, recombinant wild-type enzyme
0.1
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192I
0.2
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192S
0.9
dimethyl-paraoxon
pH 8.0, 25°C, recombinant wild-type enzyme
3.8
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192N
4.2
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192W
6
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutants H115W
7.7
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192A
10.7
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192K
0.00089
malathion
25°C, pH 9.0
2.55
malathion
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
23.01
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
40.63
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
44.92
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
73.29
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
160
malathion
-
pH 7.2, 25°C
0.00783
methyl paraoxon
-
at 35°C, pH 9.0
0.3
methyl paraoxon
25°C, pH 9, mutant enzyme E14K
0.31
methyl paraoxon
pH 8.3, 25°C
0.42
methyl paraoxon
25°C, pH 9, mutant enzyme Y34Q
0.86
methyl paraoxon
25°C, pH 9, mutant enzyme E14K/Y34Q
1.25
methyl paraoxon
pH 8.0, 70°C
1.3
methyl paraoxon
-
pH 8.0, 70°C, recombinant enzyme
2.71
methyl paraoxon
25°C, pH 9.0
7.4
methyl paraoxon
25°C, pH 9, wild-type enzyme
7.75
methyl paraoxon
pH 9.0, 75°C
14.05
methyl paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
342
methyl paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
0.0011
methyl parathion
25°C, pH 9.0
9.7
methyl parathion
25°C, pH 9
1152
methyl parathion
-
pH 7.2, 25°C
0.0008
paraoxon
pH 8.0
0.007
paraoxon
pH 8.0, recombinant genetic variant G1A7
0.009
paraoxon
pH 8.0, recombinant genetic variant G1B11
0.036
paraoxon
pH 8.0, recombinant genetic variant G2C2
0.04
paraoxon
pH 8.0, recombinant genetic variant G3A5
0.11
paraoxon
pH 8.0, recombinant genetic variant G3G3
0.13
paraoxon
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.14
paraoxon
pH 8.0, recombinant genetic variant G3H9
0.14
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K
0.17
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
0.24
paraoxon
pH 8.0, 70°C, wild-type enzyme
0.24
paraoxon
-
pH 8.0, 70°C, recombinant enzyme
0.45
paraoxon
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
0.54
paraoxon
pH 8.0, recombinant genetic variant G1C4
0.68
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W
0.79
paraoxon
70°C, pH not specified in the publication
0.87
paraoxon
pH 8.0, recombinant genetic variant G2E6
0.89
paraoxon
pH 8.0, temperature not specified in the publication
0.9
paraoxon
wild-type, pH 8.0, 25°C
0.98
paraoxon
pH 8.0, recombinant genetic variant G2D6
1
paraoxon
pH 8.0, mutant enzyme H115Q
1.09
paraoxon
pH 8.0, recombinant wild-type PON1 genetic variant G2E6
1.1
paraoxon
pH 8.0, recombinant genetic variant G3C9
1.16
paraoxon
pH 8.0, recombinant genetic variant G1A5
1.2
paraoxon
pH 8.0, recombinant genetic variant G3H8
1.42
paraoxon
25°C, pH not specified in the publication, wild-type enzyme
1.63
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/W263F
2.2
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I261F
2.29
paraoxon
pH 8.0, 70°C
2.7
paraoxon
25°C, 0.01% SDS, pH not specified in the publication
3
paraoxon
pH 8.0, wild-type enzyme
3.3
paraoxon
pH 8.3, activity buffer
3.7
paraoxon
pH 8.3, activity buffer with 0.01 mM apolipoprotein apoA-I rHDL
3.7
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I98F/I261F
3.76
paraoxon
pH 8.0, 70°C, mutant enzyme W263F
3.8
paraoxon
mutant H115W/R192Q, pH 8.0, 25°C
3.98
paraoxon
70°C, pH 9.0
4.2
paraoxon
pH 8.0, wild-type enzyme
4.7
paraoxon
pH 8.0, mutant enzyme H115Q/H134Q
4.8
paraoxon
recombinant enzyme
5.7
paraoxon
-
pH 7.4, 37°C, type A paraoxonase
5.8
paraoxon
pH 8.3, activity buffer with 0.1% tergitol
6
paraoxon
mutant H115W, pH 8.0, 25°C
8.52
paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
10.7
paraoxon
mutant H115W/R192K, pH 8.0, 25°C
10.98
paraoxon
-
pH 7.4, 37°C, type B paraoxonase
12.59
paraoxon
25°C, pH 9.0
12.7
paraoxon
pH 8.0, mutant enzyme H134Q
14.31
paraoxon
25°C, 0.1% SDS, pH not specified in the publication
50
paraoxon
Co2+-PTE mutant H123I, at pH 8.5 and 30°C
125
paraoxon
-
pH 10.5, 25°C, 3-fluorotyrosine-containing recombinant His6-tagged OPH
390
paraoxon
Co2+-PTE mutant H123A, at pH 8.5 and 30°C
450
paraoxon
mutant enzyme H254R/H257F, in 20 mM CHES buffer (pH 9.0) at 25°C
597
paraoxon
recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C
640
paraoxon
mutant enzyme H254R/H257L, in 20 mM CHES buffer (pH 9.0) at 25°C
750
paraoxon
mutant H254R, pH 9.0, 25°C
780
paraoxon
pH 8.5, recombinant wild-type enzyme-MBP fusion protein
1200
paraoxon
mutant enzyme H254R, in 20 mM CHES buffer (pH 9.0) at 25°C
1280
paraoxon
pH 8.5, recombinant genetic variants 1.5E-MBP fusion protein
1290
paraoxon
Zn2+-PTE, at pH 8.5 and 30°C
1336
paraoxon
-
pH 7.2, 25°C
1430
paraoxon
pH 8.5, recombinant genetic variants 1.6F-MBP fusion protein
1610
paraoxon
Co2+-PTE mutant H123N, at pH 8.5 and 30°C
2150
paraoxon
pH 8.5, recombinant genetic variants 2.S5-MBP fusion protein
2280
paraoxon
wild-type enzyme
2280
paraoxon
pH 9.0, recombinant wild-type enzyme
3400
paraoxon
-
pH 8.0, 30°C
4010
paraoxon
Co2+-PTE, at pH 8.5 and 30°C
5100
paraoxon
-
pH 10.5, 25°C, recombinant His6-tagged wild-type OPH
6900
paraoxon
wild type enzyme, in 20 mM CHES buffer (pH 9.0) at 25°C
8000
paraoxon
mutant enzyme H257L, in 20 mM CHES buffer (pH 9.0) at 25°C
10500
paraoxon
wild-type enzyme, pH 9.0, 25°C
11700
paraoxon
-
pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
0.12
parathion
pH 8.3, 25°C
300
parathion
recombinant wild-type enzyme bound to Cd2+ and Zn2+, pH 9.0, 30°C
600
parathion
recombinant wild-type enzyme bound to Cd2+, pH 9.0, 30°C
720
parathion
recombinant wild-type enzyme bound to Zn2+, pH 9.0, 30°C
1098
parathion
-
pH 7.2, 25°C
0.6
pentafluorophenyl diethyl phosphate
pH 8.0
678
pentafluorophenyl diethyl phosphate
about, pH 8.0, genetic variant PON1 G2E6
89
phenyl acetate
-
recombinant PON3
552
phenyl acetate
pH 8.0, recombinant genetic variant G1C4
562
phenyl acetate
pH 8.0, recombinant genetic variant G2D6
789
phenyl acetate
pH 8.0, recombinant genetic variant G3C9
833
phenyl acetate
pH 8.0, recombinant genetic variant G1A5
965
phenyl acetate
pH 8.0, recombinant genetic variant G2E6
1018
phenyl acetate
pH 8.0, recombinant genetic variant G3H8
1236
phenyl acetate
pH 8.0, recombinant wild-type PON1
0.55
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
11.72
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
0.167
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
4.95
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
0.007
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, pH 8.5, temperature not specified in the publication
0.15
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
mutant L271A/Y309A, pH 8.5, temperature not specified in the publication
15
sarin
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
39
sarin
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
90
sarin
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
120
sarin
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
300
sarin
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.2
soman
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.6
soman
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
9.1
soman
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
25
soman
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
89
soman
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.15
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
0.5
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
1.83
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
6.467
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9.43
(1E)-but-1-en-1-yl dibutyl phosphate
pH 9.0, 25°C
1.264 - 85
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
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
21.4 - 333.3
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
5.55 - 883.3
4-acetylphenyl (S)-2-methylpropyl 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
1.16
4-acetylphenyl cyclohexyl methyl (R)-phosphate
pH 8.5, 30°C
3.17
4-acetylphenyl cyclohexyl methyl (S)-phosphate
pH 8.5, 30°C
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
1.45
4-carbamoylphenyl diethyl phosphate
pH and temperature not specified in the publication
0.438
CMP-coumarin
pH 8.3, 25°C
42.37
cyclohexyl ethyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
51.85
cyclohexyl ethyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
5.45
cyclohexyl methyl 4-nitrophenyl (R)-phosphate
pH 8.5, 30°C
20.94
cyclohexyl methyl 4-nitrophenyl (S)-phosphate
pH 8.5, 30°C
63.33
cyclohexyl methyl phenyl (R)-phosphate
pH 8.5, 30°C
0.00083
cyclosarin
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
0.0000983
demeton-S
-
at 35°C, pH 7.2
1.63 - 40.23
demeton-S methyl
0.9 - 3.27
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
0.25
dibutyl 3,3-difluorobutyl phosphate
pH 9.0, 25°C
5.81
dibutyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
50
dibutyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
31.4
dibutyl phenyl phosphate
pH and temperature not specified in the publication
1.1
dichlorvos
pH 8.0, 37°C, enzyme administered in monkeys in vivo
74.7
diethyl 2,4,6-trifluorophenyl phosphate
pH and temperature not specified in the publication
33.3
diethyl 2,4-difluorophenyl phosphate
pH and temperature not specified in the publication
84.54
diethyl 2,6-difluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
63.5
diethyl 2-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
16.15
diethyl 2-fluorophenyl phosphate
pH and temperature not specified in the publication
428
diethyl 3-fluoro-4-nitrophenyl phosphate
pH and temperature not specified in the publication
300
diethyl 3-fluorophenyl phosphate
pH and temperature not specified in the publication
2.5
diethyl 4-acetophenyl phosphate
pH and temperature not specified in the publication
97.6
diethyl 4-chlorophenyl phosphate
pH and temperature not specified in the publication
138.8
diethyl 4-cyanophenyl phosphate
pH and temperature not specified in the publication
48.75
diethyl 4-fluorophenyl phosphate
pH and temperature not specified in the publication
25.8
diethyl 4-formylphenyl phosphate
pH and temperature not specified in the publication
5.68
diethyl 4-methoxyphenyl phosphate
pH and temperature not specified in the publication
0.91 - 100
diethyl 4-nitrophenyl phosphate
1.8 - 7.3
diethyl paraoxon
363.04
diethyl pentafluoro-phenyl phosphate
pH and temperature not specified in the publication
64.54
diethyl phenyl phosphate
pH and temperature not specified in the publication
0.2 - 27531
diethyl-paraoxon
151.16
diethylumbelliferyl phosphate
-
pH 7.5, 25°C, recombinant mutant enzyme G137D
11.97
dimethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
0.11 - 11.89
dimethyl-paraoxon
0.05467 - 25
ethyl paraoxon
0.00186
ethyl-paraoxon
pH 8.0, 70°C
103.28
methyl 4-nitrophenyl phenyl (R)-phosphate
pH 8.5, 30°C
2.4
methyl 4-nitrophenyl phenyl (S)-phosphate
pH 8.5, 30°C
2.17
methyl 4-nitrophenyl propan-2-yl (R)-phosphate
pH 8.5, 30°C
56.94
methyl 4-nitrophenyl propan-2-yl (S)-phosphate
pH 8.5, 30°C
3.2
methyl 4-[(diethoxyphosphoryl)oxy]benzoate
pH and temperature not specified in the publication
112.5
methyl bis(4-nitrophenyl) phosphate
pH 8.5, 30°C
0.029 - 102
methyl paraoxon
0.0091 - 0.036
methyl parathion
4.94
O,O,S-tributyl phosphorothioate
pH 9.0, 25°C
0.867
O,O-diethyl fluorophosphate
-
pH 8.0, 25°C, enzyme administered in mice in vivo
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
617 - 767
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
883 - 933
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
0.00486 - 0.0249
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
0.283
SP-CMP
pH 8.0, 25°C, enzyme administered in mice in vivo
1.05 - 6.7
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
13.6 - 25
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
0.767
Tabun
-
pH 8.0, 25°C, enzyme administered in mice in vivo
1.264
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant wild-type enzyme
4.0625
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
4.357
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
5.375
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
11.071
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
14.571
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
19
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
21.053
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
21.539
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
28.75
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
30
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
30.137
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
85
(S)-[2-[di(propan-2-yl)amino]ethyl] O,O-diethyl phosphorothioate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
0.003
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.058
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.22
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
1.3
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
2.3
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
0.016
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.13
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.2
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.49
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
0.59
4-acetylphenyl (2R)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.0011
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.0032
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.0067
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
0.25
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
1.7
4-acetylphenyl (2S)-3,3-dimethylbutan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
21.4
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
25
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
32.7
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
34.375
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
49.4
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
61
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
81.7
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
94.1
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
124.3
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
158.3
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
162.9
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
255.6
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
313
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
333.3
4-acetylphenyl (R)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
5.55
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant wild-type enzyme
9.3
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
17.1
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
34
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
38.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
42.6
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
110.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
112
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
143.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
166.67
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
180
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
290
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant H254Q/H257F
294.4
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
535.5
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
883.3
4-acetylphenyl (S)-2-methylpropyl methylphosphonate
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
1.5
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
13
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
180
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
760
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
850
4-acetylphenyl 2-methylpropyl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.099
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
9.5
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
34
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
73
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
180
4-acetylphenyl 2-methylpropyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
0.25
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
1.9
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
16
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
21
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
28
4-acetylphenyl cyclohexyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
0.00094
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
0.021
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
0.1
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
5.8
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
28
4-acetylphenyl cyclohexyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
1.5
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.4
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
75
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
490
4-acetylphenyl ethyl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
520
4-acetylphenyl ethyl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
130
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
150
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
160
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
220
4-acetylphenyl ethyl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
1200
4-acetylphenyl ethyl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
1.8
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
2.5
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
110
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
520
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
580
4-acetylphenyl propan-2-yl (R)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
3.1
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C
5.9
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C
6.2
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C
27
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C
110
4-acetylphenyl propan-2-yl (S)-methylphosphonate
-
mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C
1.63
demeton-S methyl
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
1.97
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
3.5
demeton-S methyl
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
19.08
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
40.23
demeton-S methyl
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.9
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
3.27
dibutyl 2,2,3,3-tetrafluorobutyl phosphate
pH 9.0, 25°C
0.91
diethyl 4-nitrophenyl phosphate
pH 9.0, 75°C
78.31
diethyl 4-nitrophenyl phosphate
pH 8.5, 30°C
100
diethyl 4-nitrophenyl phosphate
pH and temperature not specified in the publication
1.8
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
6.5
diethyl paraoxon
-
recombinant enzyme, in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
7.3
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
0.2
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
0.25
diethyl-paraoxon
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
18.19
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C
44.8
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C
80.4
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 25°C, with 0.025% SDS
97.5
diethyl-paraoxon
recombinant enzyme mutant C258L/I261F/W263A, pH 8.5, 65°C, with 0.025% SDS
1920
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F
4925
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F
6304
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N
6786
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L
7736
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant H254Q/H257F
8824
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N
9722
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
9818
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F
11806
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
12222
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L
14239
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
14500
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
16515
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
19434
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
20727
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L
21239
diethyl-paraoxon
pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
27531
diethyl-paraoxon
pH 9.0, 30°C, recombinant wild-type enzyme
0.11
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192I
0.18
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192S
0.75
dimethyl-paraoxon
pH 8.0, 25°C, recombinant wild-type enzyme
3.23
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192W
6.42
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192A
6.67
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutants H115W
7.6
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192N
11.89
dimethyl-paraoxon
pH 8.0, 25°C, recombinant mutant H115W/R192K
0.05467
ethyl paraoxon
-
at 35°C, pH 9.0
1.2
ethyl paraoxon
-
at pH 8.0 and 23°C
1.4
ethyl paraoxon
-
with 50% (v/v) glycerol, at pH 8.0 and -18°C
25
ethyl paraoxon
-
at pH 8.0 and 70°C
0.0056
malathion
25°C, pH 9.0
1.88
malathion
25°C, pH 9
6.21
malathion
-
wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
19.83
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
49.54
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
109.4
malathion
-
mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
154.9
malathion
-
mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C
0.029
methyl paraoxon
-
at 35°C, pH 9.0
0.443
methyl paraoxon
pH 8.0, 70°C
1.1
methyl paraoxon
pH 8.3, 25°C
1.27
methyl paraoxon
25°C, pH 9.0
1.4
methyl paraoxon
25°C, pH 9, mutant enzyme E14K/Y34Q
1.6
methyl paraoxon
25°C, pH 9, mutant enzyme Y34Q
4.26
methyl paraoxon
25°C, pH 9, wild-type enzyme
5.57
methyl paraoxon
pH 9.0, 75°C
6
methyl paraoxon
25°C, pH 9, mutant enzyme E14K
102
methyl paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
0.0091
methyl parathion
25°C, pH 9.0
0.036
methyl parathion
25°C, pH 9
0.02167
paraoxon
-
PON1/human phosphate binding protein (1:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
0.26
paraoxon
25°C, pH not specified in the publication
0.3
paraoxon
-
in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4
0.33
paraoxon
-
PON1/human phosphate binding protein (9:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
0.367
paraoxon
pH 8.0, 25°C, enzyme administered in rats in vivo
0.52
paraoxon
25°C, pH 9.0
0.64
paraoxon
25°C, 0.01% SDS, pH not specified in the publication
0.7
paraoxon
wild-type, pH 8.0, 25°C
0.7
paraoxon
70°C, pH not specified in the publication
0.87
paraoxon
25°C, pH not specified in the publication, mutant enzyme Y34Q
0.97
paraoxon
pH 8.0, 70°C
1.07
paraoxon
pH 8.0, 70°C, mutant enzyme W263Q
1.11
paraoxon
-
isozyme 192Q, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
1.22
paraoxon
70°C, pH 9.0
1.3
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q
1.53
paraoxon
-
recombinant PON1, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C
2.2
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/W263Q
2.45
paraoxon
pH 8.0, 70°C, mutant enzyme W263F
3.05
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I98F/I261F
3.67
paraoxon
-
isozyme 192R, in 100 mM Tris-HCl (pH 8.5), 1 mM CaCl2, 37°C
3.75
paraoxon
pH 8.0, 70°C, wild-type enzyme
4.5
paraoxon
25°C, pH not specified in the publication, mutant enzyme E14K
4.6
paraoxon
mutant H115W/R192Q, pH 8.0, 25°C
5.4
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/I261F
6.02
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W/W263F
6.6
paraoxon
mutant H115W, pH 8.0, 25°C
7.14
paraoxon
25°C, 0.1% SDS, pH not specified in the publication
9.01
paraoxon
pH 8.0, 70°C, mutant enzyme Y97W
10.7
paraoxon
mutant H115W/R192K, pH 8.0, 25°C
23.33
paraoxon
-
pH 8.0, 38°C, enzyme administered in mice in vivo
26.6
paraoxon
-
pH 8.5, 70°C, Mn2+-containing enzyme
140
paraoxon
Co2+-PTE mutant H123I, at pH 8.5 and 30°C
1000
paraoxon
Co2+-PTE mutant H123A, at pH 8.5 and 30°C
4700
paraoxon
Co2+-PTE mutant H123N, at pH 8.5 and 30°C
5000
paraoxon
Zn2+-PTE, at pH 8.5 and 30°C
10000
paraoxon
Co2+-PTE, at pH 8.5 and 30°C
0.281
parathion
pH 8.3, 25°C
0.367
parathion
pH 8.0, 25°C, enzyme administered in rats in vivo
1.1
parathion
pH 8.0, 25°C, enzyme administered in rats in vivo
617
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
767
RP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
883
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
933
RP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
0.00486
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, pH 8.5, temperature not specified in the publication
0.0249
S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate
-
mutant L271A/Y309A, pH 8.5, temperature not specified in the publication
1.05
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
6.7
SP-O-ethyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
13.6
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
25
SP-O-n-propyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin
-
mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C
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A204C/T234C
site-directed mutagenesis, Ala204 and Thr234 are located on the alpha-helices and gamma turn, respectively, thermostability of the mutant enzyme is increased compared to the wild-type, due to increased rigidity
A80V/F132V/K185R/H254Q/H257Y/I274N
site-directed mutagenesis
A80V/F132V/K185R/H254Q/H257Y/I274N/S308L
site-directed mutagenesis, the mutant combines expression-enhancing mutations (A80V/K185R/I274N) with additional changes in the active site to achieve a high kcat/Km for the hydrolysis of the SP-enantiomer of ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX. Three-dimensional structure, overview
A80V/I106C/F132V/K185R/H254Q/H257Y/I274N
site-directed mutagenesis
A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L
site-directed mutagenesis
A80V/I106G/F132V/K185R/H254Q/H257Y/I274N
site-directed mutagenesis
A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L
site-directed mutagenesis
C24S
site-directed mutagenesis, mutation of the invariant cysteine residue in the lipobox motif of the OPH signal peptide
D233A
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
D233N
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
D301A
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
D301N
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
F132V/H254Q/H257F
site-directed mutagenesis
F132V/H254Q/H257F/S308L
site-directed mutagenesis
G74C/A78C
site-directed mutagenesis, Gly74 and Ala78 are located on the gamma turn and beta-turn, respectively, which link gamma turn and beta-turn adjacent together, thermostability of the mutant enzyme is decreased compared to the wild-type, due to increased flexibility
H123A
KM remains unaffected, whereas kcat decreases 2.5fold. Alters the bacterial expression yield of Co2+-PTE and Ki for Zn(OH)2 inhibition
H123I
KM remains unaffected, whereas kcat decreases 10fold. Alters the bacterial expression yield of Co2+-PTE and Ki for Zn(OH)2 inhibition
H123N
KM remains unaffected, whereas kcat decreases 80fold. Alters the bacterial expression yield of Co2+-PTE and Ki for Zn(OH)2 inhibition
H254A
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
H254N
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
H254Q/H257F
site-directed mutagenesis, the mutant exhibits a 100fold improvement for the hydrolysis of O-ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX, relative to the wild-type enzyme
H254R/H257F
the mutant enzyme shows reduced activity towards paraoxon and increased activity towards demeton-S compared to the wild type enzyme
H254R/H257L
the variant has higher turnover numbers for the chemical warfare agents O-ethyl S-diisopropyl aminomethyl methylphosphonothioate and O-isobutyl S-N,N-diethylaminoethyl methylphosphonothioate compared to the wild type enzyme, the demeton-S activity is over 14times higher as that of the wild type enzyme
H257L
the mutant enzyme shows increased activity towards paraoxon and reduced activity toward demeton-S compared to the wild type enzyme
I106A/F132A/H254Y
-
stereoselectivity of enzyme toward chiral phosphorous center of substrate is reversed
I106C
site-directed mutagenesis
I106C/F132V/H254Q/H257F
site-directed mutagenesis
I106C/F132V/H254Q/H257F/S308L
site-directed mutagenesis, the mutant shows a similar catalytic efficiency for the hydrolysis of ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX, as mutant H254Q/H257F, but a 3fold improvement in kcat
I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
site-directed mutagenesis, the mutant has a kcat value for ethyl-S-(2-diisopropylaminoethyl)methylphosphonothiolate, i.e. VX, that is enhanced by 150fold relative to wild-type PTE. Three-dimensional structure, overview
I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F
site-directed mutagenesis
I106G
site-directed mutagenesis
I106G/F132V/H254Q/H257F/S308L
site-directed mutagenesis
I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L
site-directed mutagenesis
L308S
site-directed mutagenesis
T128C/ E124C
site-directed mutagenesis, thermostability and kcat of the mutant enzyme are increased compared to the wild-type
T128C/ E153C
site-directed mutagenesis, Thr128 and Glu153 are located on the beta-sheet and alpha-helices, respectively, thermostability of the mutant enzyme is increased compared to the wild-type, due to increased rigidity
A14T/A80V/K185R/H257Y/I274N
-
random saturation mutagenesis, variant 2H2, increased activity and altered kinetics compared to the wild-type enzyme
A80V/I274N/K185R
-
site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
A80V/S365P
-
random saturation mutagenesis, variant 2H2, increased activity and altered kinetics compared to the wild-type enzyme
H257Y
-
random saturation mutagenesis, variant 6D4, increased activity and altered kinetics compared to the wild-type enzyme
I274N
-
random saturation mutagenesis, variant 5A6, increased activity and altered kinetics compared to the wild-type enzyme
I274N/K185R
-
site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
K185E
-
site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
K185R
-
site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
L182S/V310A
-
random saturation mutagenesis, variant 2F6, increased activity and altered kinetics compared to the wild-type enzyme
R153L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R153W
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
185X
-
construction of diverse mutants with polymorphism at residue 185 showing altered activities with substrate methyl parathion and paraoxon, overview
A14T/A80V/K185R
naturally occurring OPH genetic variant B1368, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A14T/A80V/K185R/H254R/I274N
naturally occurring OPH genetic variant B2136, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A14T/A80V/K185R/H257Y/I274N
A14T/A80V/K185R/I274N
naturally occurring OPH genetic variant A1030, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A14T/L17P/A80V/V116I/K185R/A203T/I274N/P342S
naturally occurring OPH genetic variant B3561, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A14T/R67H/A80V/L87S/Q148R/K185R
naturally occurring OPH genetic variant A1467, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A80V
-
OPH genetic variant 2H2, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
H257Y
-
OPH genetic variant 6D4, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
I274N
-
OPH genetic variant 5A6, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
I274N/H257Y
-
OPH genetic variant 21E1, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
A14T/A80V/K185R
-
naturally occurring OPH genetic variant B1368, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
-
A14T/A80V/K185R/H257Y/I274N
-
naturally occurring OPH genetic variant 22A11, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
-
A14T/A80V/K185R/I274N
-
naturally occurring OPH genetic variant A1030, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
-
A14T/R67H/A80V/L87S/Q148R/K185R
-
naturally occurring OPH genetic variant A1467, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
-
A80V
-
OPH genetic variant 2H2, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
-
H257Y
-
OPH genetic variant 6D4, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
-
I274N
-
OPH genetic variant 5A6, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
-
I274N/H257Y
-
OPH genetic variant 21E1, site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
-
A80V/F132C/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
A80V/F132D/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with VX, demethon-S methyl and malathion compared to the wild type enzyme
A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S
A80V/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
A80V/K185R/D208G/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S
-
the mutant displays a 77fold improvement in the specific activity against malathion, and exhibits only about 10% of the specific activity against VX compared to the wild type enzyme
G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
L271/Y309A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, 2fold increase in reactivity with substrate demeton-S-methyl
L271A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, similar soluble expression
L271A/Y309A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, exhibits a 150fold higher catalytic efficiency for V-type nerve agents such as S-(2-[di(propan-2-yl)amino]ethyl)O-ethyl methylphosphonothioate than the wild-type
T172A/L271A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, decrease in activity
T172A/L271A/Y309A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, decrease in activity
T172A/Y309A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, 2fold increase in reactivity with substrate demeton-S-methyl
Y309A
-
mutant based on expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, increase in soluble expression
A80V/F132C/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
-
A80V/F132D/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
-
A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with VX, demethon-S methyl and malathion compared to the wild type enzyme
-
A80V/K185R/D208G/H257W/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
-
A80V/K185R/D208G/I274N/R319S
-
the mutant shows increased specific activity with demethon-S methyl and malathion compared to the wild type enzyme
-
C283A
-
retains enzymatic activity, not inactivated by p-hydroxymercuribenzoate
C283S
-
retains enzymatic activity, not inactivated by p-hydroxymercuribenzoate
C284A
mutant with 20fold reduced paraoxonase activity
D183N
the mutant disfavors paraoxon binding due to its charged nature and possible electrostatic repulsion with the phosphate group of paraoxon
F132G
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
F222A
site-directed mutagenesis, inactive mutant
G60A
-
the mutant shows increased catalytic efficiency with sarin and soman compared to the wild type enzyme
H114N
-
catalytically inactive
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/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/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/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
H133N
-
catalytically inactive
H134Q
activity with paraoxon is 602% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 38% of wild-type 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
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
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
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
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
L69V
the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme
L69V/V369A
the mutant shows increased paraoxon binding affinity compared to the wild type enzyme
R180T
the mutant enzyme exhibits 180fold increased ethyl paraoxon-hydrolyzing activity compared to the wild type enzyme
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
R192V
site-directed mutagenesis
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
S193P
the mutation increases phosphotriesterase activity of PON1
S308G
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
V346A
the mutant shows a 4-16fold increase in PON1 activity compared to the wild type enzyme
D229N/N120D
-
site-directed mutagenesis, the mutation reorientates the electrostatic environment around the catalytic calcium, inactive mutant
D229N/N175D
-
site-directed mutagenesis, the mutation reorientates the electrostatic environment around the catalytic calcium, inactive mutant
E21Q/N120D
-
site-directed mutagenesis, inactive mutant
E21Q/N175D
-
site-directed mutagenesis, inactive mutant
G137D
-
the naturally occurring mutation (Gly137Asp) in alpha-esterase 7 (LcalphaE7) results in acquisition of organophosphate hydrolase activity and confers resistance to organophosphate insecticides. The Gly137Asp mutation does not significantly alter the geometry of the LcalphaE7 catalytic triad or oxyanion hole, organophosphorous substrate binding structure compared to wild-type, overview. The pH-dependence of the rate-determining dephosphorylation step of the reaction by mutant G137D is not altered compared to the wild-type enzyme
PON1
-
the mutant is less able to detoxify diazoxon
D269N
site-directed mutagenesis, the mutant possesses measurable lactonase and paraoxonase activity
D270X
site-directed mutagenesis, mutation of the residue stabilizes the PON1-paraoxon substrate binding reducing the leaving group elimination rate. Effects of Asn270 mutation on enzymatic structure, overview
E53Q
site-directed mutagenesis, the mutant possesses measurable lactonase and paraoxonase activity
H115W/T332S
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
H115W/T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
H115W/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74A
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
I74F
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W/T332S
site-directed mutagenesis, the mutant shows very highly increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W/V346A
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
I74F/T332S
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74L
site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type
I74V
site-directed mutagenesis, the mutant shows slightly reduced activity with diethyl-paraoxon compared to wild-type
I74W
site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type
L69A
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
L69I
site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type
T332A
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
T332S
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
T332V
site-directed mutagenesis, almost inactive mutant
V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
Y71A
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71F
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71G
site-directed mutagenesis, the mutant shows reduced lactonase and paraoxonase activities compared to the wild-type enzyme, the mutant shows an increased active site volume compared to the wild-type
Y71M
site-directed mutagenesis, the mutant shows reduced lactonase and paraoxonase activities compared to the wild-type enzyme, the mutant shows an increased active site volume compared to the wild-type
Y71W
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71X
site-saturation library screening. The impact of Y71 mutational substitutions on PON1's lactonase activity is minimal, whereas the kcat for the paraoxonase activity is negatively perturbed by up to 100fold, suggesting greater mutational robustness of the native activity. Additionally, while these substitutions modulate PON1's active site shape, volume, and loop flexibility, their largest effect is in altering the solvent accessibility of the active site by expanding the active site volume, allowing additional water molecules to enter. This effect is markedly more pronounced in the organophosphatase activity than the lactonase activity. Differential effect of mutating Y71 on the native and promiscuous activities of PON1, detailed overview
C105S
mutant shows 24.0% activity compared to the wild type enzyme
C107S
mutant shows 30.8% activity compared to the wild type enzyme
C129S
mutant shows 3.6% activity compared to the wild type enzyme
C258A
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
C258L
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
D141T
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
D251N
mutant shows 0.6% activity compared to the wild type enzyme
F46L/C258A/W263M/I280T
site-directed mutagenesis, mutant alphasA6, the mutant shows altered substrate specificity compared to the wild-type enzyme
H281N
mutant shows 19.4% activity compared to the wild type enzyme
I767T
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
L130P
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
L228M
site-directed mutagenesis
L72I/Y99F/I122L/L228M/F229S/W263L
site-directed mutagenesis, mutant alphasC6, the mutant shows altered substrate specificity compared to the wild-type enzyme
S156A
mutant shows 0.012% activity compared to the wild type enzyme
V27A/D141T
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
V27A/I76T/Y97W/Y99F/L130P/L226V
site-directed mutagenesis, mutant alphasB5, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263I
site-directed mutagenesis, mutant alphasB5 W263I, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263L
site-directed mutagenesis, mutant alphasB5 W263L, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/I76T/Y97W/Y99F/L130P/L226V/W263M
site-directed mutagenesis, mutant alphasB5 W263M, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A/Y97W/L228M/W263M
site-directed mutagenesis, the mutant alphasD6 enzyme demonstrates a large increase in catalytic efficiencies compared to the wild-type enzyme, with increases of 2210fold, 163fold, 58fold, and 16fold against methyl-parathion, malathion, ethyl-paraoxon, and methyl-paraoxon, respectively
V27A/Y97W/Y99F
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
W263L
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263N
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263Q
kcat/Km for paraoxon is 3.5fold lower than wild-type value
Y97W/I261F
kcat/Km for paraoxon is 1.4fold higher than wild-type value
Y97W/I98F/I261F
kcat/Km for paraoxon is 1.2fold higher than wild-type value
Y97W/W263F
kcat/Km for paraoxon is 1.6fold higher than wild-type value
Y97W/W263Q
kcat/Km for paraoxon is 1.7fold lower than wild-type value
Y99F
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263Q
-
kcat/Km for paraoxon is 3.5fold lower than wild-type value
-
Y97W
-
kcat/Km for paraoxon is 2.4fold higher than wild-type value
-
Y97W/I261F
-
kcat/Km for paraoxon is 1.4fold higher than wild-type value
-
Y97W/W263Q
-
kcat/Km for paraoxon is 1.7fold lower than wild-type value
-
R91A/R96F
site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant
R91A/R96G
site-directed mutagenesis, substitution of the protein-interacting arginines
R91F/R96F
site-directed mutagenesis, substitution of the protein-interacting arginines, inactive mutant
R91F/R96G
site-directed mutagenesis, substitution of the protein-interacting arginines
E14K
Tm-value for the mutant enzyme is 6°C lower than wild-type Tm-value. The efficiency of methyl paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
E14K/Y34Q
Tm-value for the mutant enzyme is 4°C lower than wild-type Tm-value. The efficiency of methyl paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
Y34Q
Tm-value for the mutant enzyme is 8°C lower than wild-type Tm-value. The efficiency of methyl paraoxon hydrolysis is similar for wild-type and the mutants, whereas the mutants exhibit higher catalytic efficiency against ethyl-paraoxon than the wild-type. The mutants exhibit a heavily reduced N-acyl-homoserine lactonase-, delta-lactonase- and gamma-lactonase activity
H115W
-
as the wild-type, preference for the three RP isomers of the O-alkyl methylphosphonyl-3-cyano-7-hydroxy-4-methylcoumarin analogs, regardless of the size of the alkyl group
H254R
site-directed mutagenesis, the mutation increases the mutants activity with substrate demeton-S, a VX analogue, 4fold and decreases the activity with paraoxon 14fold as well as activity towards diisopropyl phosphorofluoridate, a sarin analogue, 183fold compared to the wild-type enzyme
H254R
the mutant enzyme is not completely denatured by urea concentrations up to 8.5 M even after incubation for 24 h, the mutant is more stable than the wild type enzyme and shows increased activity with demeton-S 9times over that of the wild type enzyme
Y309F
site-directed mutagenesis
Y309F
site-directed mutagenesis, structure and kinetics of the mutant enzyme with different bound metal ions compared to the wild-type enzyme, overview
R153A
-
prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153A
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R153L/R370L
-
prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153L/R370L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R153W/R370L
-
hydrolyses the (S)-enantiomer of O-methoxy-p-nitrophenyl methylphosphonate significantly faster than the (R)-isomer. Prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153W/R370L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R370L
-
prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R370L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
W88L
-
prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
W88L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
A14T/A80V/K185R/H257Y/I274N
naturally occurring OPH genetic variant 22A11, the variant shows altered kinetics with chlorpyrifos compared to the wild-type enzyme
A14T/A80V/K185R/H257Y/I274N
-
OPH genetic variant 22A11, constructed by site directed mutagenesis, the variant shows altered kinetics compared to the wild-type enzyme
A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S
-
the specific activity of the mutant is improved 26, 35 and 42fold against VX, malathion and demeton-S methyl, respectively, compared to the wild type
A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S
-
mutant constructed fo expression of soluble and active enzyme
C284D
no enzymic activity
C284D
site-directed mutagenesis, inactive mutant
D269E
no enzymic activity
D269E
site-directed mutagenesis, inactive mutant
D54N
no enzymic activity
D54N
site-directed mutagenesis, inactive mutant
E313A
slightly decreased activity
E313A
site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme
E314A
enzymic activity similar to wild-type
E314A
site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme
F222D
no enzymic activity
F222D
site-directed mutagenesis, inactive mutant
F222D
the mutation abolishes both esterase and PON activity of PON1
F222Y
site-directed mutagenesis, the mutant enzyme shows altered kinetics compared to the wild-type enzyme
F222Y
hydrolysis of phenyl acetate, but not of paraoxon
F222Y
increased activity with phenyl acetate, no activity with paraoxon
F222Y
the mutation abolishes the PON activity of PON1 but retains the esterase activity with a 1.5fold increase in KM for phenyl acetate
G11A
site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme
G11A
slightly enhanced activity with phenyl acetate and paraoxon
G11C
site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme
G11C
slightly enhanced activity with phenyl acetate and paraoxon
G11S
site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme
G11S
slightly enhanced activity with phenyl acetate and paraoxon
H115W
site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme
H115W
no enzymic activity with phenyl acetate, increased activity with paraoxon
H115W
no hydrolysis of phenyl acetate, but hydrolysis of paraoxon. Phenyl acetate can act as an inhibitor
H115W
activity with paraoxon is 195% of wild-type activity, activity with 7-diethylphosphoro-3-cyanocoumarin is 234% of wild-type activity
H115W
the mutant shows a 2fold increase in PON1 activity compared to the wild type enzyme
H115W
significant increase in the rate of catalysis, no effect on the affinity of the substrate
H115W/N133S
site-directed mutagenesis, the mutant enzyme shows reduced activity and altered kinetics compared to the wild-type enzyme
H115W/N133S
no enzymic activity with phenyl acetate, slightly decreased activity with paraoxon
H115W/N133S
no hydrolysis of phenyl acetate, but hydrolysis of paraoxon
H115W/R192K
site-directed mutagenesis
H115W/R192K
further increases in the paraoxon hydrolyzing activity of the enzyme
H115W/R192K
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview
H115W/R192K
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
H115W/R192K
the mutant enzyme exhibits considerably increased organophosphate-hydrolyzing activity compared to the wild type enzyme
H115W/R192Q
mutation R192Q eleiminates the effect of mutation H115W
H115W/R192Q
site-directed mutagenesis, the mutant shows altered substrate specificity and activity compared to the wild-type, overview
H134W
no enzymic activity
H134W
site-directed mutagenesis, inactive mutant
H134Y
no enzymic activity
H134Y
site-directed mutagenesis, inactive mutant
H285D
no enzymic activity
H285D
site-directed mutagenesis, inactive mutant
H285Y
no enzymic activity
H285Y
site-directed mutagenesis, inactive mutant
L55M
naturally occuring polymorphism, allele frequency in relation to exposure of individuals to organophosphates, overview
L55M
the mutant shows low enzymatic activity
L55M
the polymorphism accounts for 73% of PON1 activity
L55M
natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme
L69F
no enzymic activity
L69F
site-directed mutagenesis, inactive mutant
N133S
enzymic activity similar to wild-type
N133S
site-directed mutagenesis, the mutant enzyme shows slightly altered kinetics compared to the wild-type enzyme
N168E
no enzymic activity
N168E
site-directed mutagenesis, inactive mutant
N224A
no enzymic activity
N224A
site-directed mutagenesis, inactive mutant
Q192R
naturally occuring polymorphism, allele frequency in relation to exposure of individuals to organophosphates, overview
Q192R
a naturally occuring polymorphism, 192QQ, 192RR or 192QR, that reduces PON1 activity and increases the risk of ischemic stroke, genotyping and phenotyping, allele frequency, the paraoxonase/arylesterase activity ratio is unaltered
Q192R
the homozygote phenotype has significant lower PON1 activity towards paraoxon and diazoxon than the wild type enzyme
Q192R
the mutant hydrolyzes paraoxon approximately 9times as efficiently as the wild type enzyme and is significantly more efficient in hydrolyzing chlorpyrifos oxon
Q192R
the mutant hydrolyzes paraoxon with a high enzyme activity
Q192R
the mutant shows lower Vmax and kcat/Km values for soman and sarin than the wild type enzyme
Q192R
the mutation is associated with sporadic amyotrophic lateral sclerosis
Q192R
the polymorphism accounts for 69% of PON1 activity, the 192RR genotype carriers have the highest PON1 activity, whereas the the 192QQ genotype carriers have the lowest activity, with the heterozygote 192Q/R having intermediate activity
Q192R
there are substrate-dependent differences among PON1 Q192R isoforms, the Q variant has a higher diazoxonase activity, whereas paraoxonase activity predominates in the R variant
Q192R
-
the mutant exhibits significantly lower homocysteine-thiolactone/creatinine levels and has 2.6 and 3.3fold greater catalytic efficiency with homocysteine-thiolactone and paraoxon, respectively, than the wild type enzyme
Q192R
-
the mutation is related to vascular disease and variation in the enzyme activity
R192Q
site-directed mutagenesis
R192Q
a naturally occuring polymorphism, 192QQ, 192RR or 192QR, that reduces PON1 activity and increases the risk of ischemic stroke, genotyping and phenotyping, allele frequency, the paraoxonase/arylesterase activity ratio is unaltered
R192Q
the polymorphic residue R192Q interacts with the leaving group of paraoxon, suggesting it plays an important role in the proper positioning of this substrate in the active site
V304A
no enzymic activity
V304A
site-directed mutagenesis, inactive mutant
V346L
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
V346L
site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type
C258L/I261F/W263A
site-directed mutagenesis, in vitro evolution, the mutant activity is promiscuous. The combination of C258L, I261F, and W263A mutations in the SsoPox triple mutant improves the hydrolytic specific activity in terms of kcat/KM toward paraoxon 12fold, the kcat 294fold compared to wild-type SsoPox, while the KM value increases
C258L/I261F/W263A
site-directed mutagenesis, mutant alphasA1, the mutant shows altered substrate specificity compared to the wild-type enzyme
C258L/I261F/W263A
site-directed mutagenesis, mutant SsoPox 3 M
V27A
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
V27A
site-directed mutagenesis, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
W263F
kcat/Km for paraoxon is 6.5fold higher than wild-type value
W263F
mutant is able to convert paraoxon to 4-nitrophenol
W263F
site-directed mutagenesis, the W263 residue is previously demonstrated to be involved in the formation of an hydrophobic channel for the substrate leaving group, the mutant enzyme shows increased phosphotriesterase activity compared to the wild-type
W263I
site-directed mutagenesis, active site mutant, the mutant shows altered substrate specificity compared to the wild-type enzyme
W263I
-
the mutant has increased lactonase and phosphotriesterase activities compared to the wild type
Y97W
site-directed mutagenesis
Y97W
kcat/Km for paraoxon is 2.4fold higher than wild-type value
W263F
-
mutant is able to convert paraoxon to 4-nitrophenol
-
W263F
-
kcat/Km for paraoxon is 6.5fold higher than wild-type value
-
additional information
-
construction of a 3-fluorotyrosine-containing enzyme by replacement of Tyr residues, Tyr292, Tyr239, and Tyr248 residues are completely replaced by the fluorinated analogue, while the Tyr156 residue is replaced by 90%, overview, the substitution extends substantially the pH range of action of the fluorine-substituted enzyme compared with the unsubstituted one, the mutant shows increased pH and temperature stability, but reduced activity
additional information
a PTE mutant dubbed C23 is engineered, exhibiting reversed stereoselectivity and high catalytic efficiency (kcat/KM) for the hydrolysis of the toxic enantiomers of nerve agents VX, CVX, and VR. The other mutants A53, IV-A1, IV-H3, B141, and RD1-G83 are less effective, activities and mutant-substrate docking, overview. The only exception is IV-A1 with amiton. Most variants are highly efficient when hydrolyzing N,N-diisopropyl substrates and were 2fold less efficient with N,N-di-ethyl substrates and 5fold less efficient with N,N-di-methyl substrates
additional information
-
a PTE mutant dubbed C23 is engineered, exhibiting reversed stereoselectivity and high catalytic efficiency (kcat/KM) for the hydrolysis of the toxic enantiomers of nerve agents VX, CVX, and VR. The other mutants A53, IV-A1, IV-H3, B141, and RD1-G83 are less effective, activities and mutant-substrate docking, overview. The only exception is IV-A1 with amiton. Most variants are highly efficient when hydrolyzing N,N-diisopropyl substrates and were 2fold less efficient with N,N-di-ethyl substrates and 5fold less efficient with N,N-di-methyl substrates
additional information
appropriate amino acid pairs for the introduction of disulfide bridge to improve protein thermostability are selected, engineering of de novo disulfide bridges is explored as a means to increase the thermal stability of enzymes in the rational method of protein engineering. Circular dichroism (CD) spectrometry and intrinsic fluorescence experiments are applied to evaluate the structural changes of mutants compared to the wild-type after introducing disulfide bridge
additional information
computational docking study of wild-type and mutant enzymes with the toxic substrates
additional information
generation of opd null mutants, strain DS010
additional information
-
generation of opd null mutants, strain DS010
additional information
-
enzyme variants with improved degradation of methyl parathion by DNA shuffling
additional information
-
construction of diverse mutant variants by saturation mutagenesis, e.g. mutant 22A11, sequencing of randomly chosen mutants, the mutants show increased activity and altered kinetics compared to the wild-type enzyme, overview
additional information
analysis of stucture, and activity and kinetics with chlorpyrifos of genetic variants, 22A11, A1030, A1467, B1368, B2136, and B3561, overview
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construction of genetic variants of OPH wild-type enzyme with altered sbstrate specificities, overview
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construction of genetic variants of OPH wild-type enzyme with altered sbstrate specificities, overview
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additional information
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analysis of stucture, and activity and kinetics with chlorpyrifos of genetic variants, 22A11, A1030, A1467, B1368, B2136, and B3561, overview
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additional information
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analysis of PON1 polymorphisms, e.g. at residue Q192R, overview
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naturally occurring polymorphism Q192R
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naturally occurring polymorphism Q192R
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increased activity and lifetime of OPH immobilized using layer-by-layer nano self-assembly on silicon microchannels, the polycation used is poly(ethylenimine), the polyanion used is poly(styrenesulfonate), method development and optimization, overview
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the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus
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the presence of a (His)6-tag at the N-terminus and at both the N- and C-termini decreases the enzymatic activity of the recombinant protein. The activity is unaffected by the presence of a (His)6-tag at its C-terminus
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development of a recombinant production method for the enzyme in Escherichia coli, which can be used for the industrial scale production of rh-PON1 enzymes. The catalytic properties of the refolded enzymes are similar to their soluble counterparts
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development of a recombinant production method for the enzyme in Escherichia coli, which can be used for the industrial scale production of rh-PON1 enzymes. The catalytic properties of the refolded enzymes are similar to their soluble counterparts
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generation of wild-type-like-G3C9-derived PON1 variants 2D8, IIG1, VIID2 and PG11
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h-PON1 is a polymorphic enzyme. A random mutagenesis approach is used to increase the organophosphate (OP)-hydrolyzing activity of recombinant enzyme h-PON1. The mutants not only show a 10-340fold increased OP-hydrolyzing activity against different OP substrates but also exhibit differential lactonase and arylesterase activities, molecular docking studies, overview. Random mutagenesis using Escherichia coli XL-1 Red mutator strain. All mutations result in a considerable decrease in the delta-valerolactone-hydrolyzing activity of the enzyme
additional information
h-PON1 is a polymorphic enzyme. A random mutagenesis approach is used to increase the organophosphate (OP)-hydrolyzing activity of recombinant enzyme h-PON1. The mutants not only show a 10-340fold increased OP-hydrolyzing activity against different OP substrates but also exhibit differential lactonase and arylesterase activities, molecular docking studies, overview. Random mutagenesis using Escherichia coli XL-1 Red mutator strain. All mutations result in a considerable decrease in the delta-valerolactone-hydrolyzing activity of the enzyme
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nanocapsulation of enzyme into enzyme-polyelectrolyte complexes leads to its expected stabilisation and significant improvement of Km and Ksi with methylphosphonic acid
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the catalytic efficiency of the recombinant human paraoxonase 1 fused to human immunoglobulin Fc domain, i.e. recombinant PON1-hFc, towards diisopropyl fluorophosphate (DFP) and paraoxon hydrolysis is 1.63 and 1.24fold higher, respectively, than the recombinant human wild-type PON1
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replacement of the catalytic serine with the diethylphosphoserine from the structure of the phosphorylated wild-type enzyme (PDB ID 4FNM), molecular dynamics simulations
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modulating the active site hydrophobicity is a key element in facilitating the evolution of organophosphatase activity. Molecular dynamics simulations of wild-type and mutant PON1 enzymes, detailed overview
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transformation of strain JS444 with a surface anchor system derive from Pseudomonas syringae leads to cell surface-taregeted expression of the enzyme reducing the limitations on substrate uptake, the engineered cells show improved degradation of organophosphorus pesticides and 4-nitrophenol, evaluation, overview
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transformation of Pseudomnas putida with the opd gene and the 4-nitrophenyl PNP operon allows the engineered organism to utilize parathion as sole source of carbon and energy, overview
additional information
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transformation of strain JS444 with a surface anchor system derive from Pseudomonas syringae leads to cell surface-taregeted expression of the enzyme reducing the limitations on substrate uptake, the engineered cells show improved degradation of organophosphorus pesticides and 4-nitrophenol, evaluation, overview
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additional information
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transformation of Pseudomnas putida with the opd gene and the 4-nitrophenyl PNP operon allows the engineered organism to utilize parathion as sole source of carbon and energy, overview
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additional information
evolution of a lactonase into a phosphotriesterase, semi-rational engineering approach is used to design an efficient and thermostable organophosphate hydrolase, starting from enzyme SsoPox from Sulfolobus solfataricus as a lactonase scaffold. In particular, by in vitro evolution of the SsoPox ancillary promiscuous activity, the triple mutant C258L/I261F/W263A is obtained which, retaining its inherent stability, shows an enhancement of its hydrolytic activity on paraoxon up to 300fold. The mutant is tested in formulations of different solvents (methanol or ethanol) or detergents (SDS or a commercial soap) for the cleaning of pesticide-contaminated surfaces. Construction of a chimeric gene ssopox-pte by insertion of 16 conserved residues of pte gene in the ssopox sequence. Recombination by DNA StEP between ssopox-pte chimera and ssopox gene
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optimization of enzyme production scale-up for establishment of an industrial purification process using SsoPox C258L/I261F/W263A mutant enzyme SsoPox 3 M, set up of high cell density fermentation strategies
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the lactonase SsoPox is engineered for higher phosphotriesterase activity using structure-based combinatorial libraries. By comparing structures of enzymes with similar topology, it is possible to redesign, using modelling tools, the active site cavity of SsoPox to mimic as closely as possible that of enzyme BdPTE from Brevundimonas diminuta. Some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. Structure-based identification of mutations, structure-activity analysis of wild-type and mutant enzymes, overview. Construction of SsoPox monovariants alphasA1, alphasA6, alphasB5, alphasC6 and alphasD6
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the lactonase SsoPox is engineered for higher phosphotriesterase activity using structure-based combinatorial libraries. By comparing structures of enzymes with similar topology, it is possible to redesign, using modelling tools, the active site cavity of SsoPox to mimic as closely as possible that of enzyme BdPTE from Brevundimonas diminuta. Some enzyme mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. Structure-based identification of mutations, structure-activity analysis of wild-type and mutant enzymes, overview. Construction of SsoPox monovariants alphasA1, alphasA6, alphasB5, alphasC6 and alphasD6
additional information
exbD and tonB genes of Sphingobium fuliginis are amplified wild-type strain ATCC 27551 from different plasmids, overview
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exbD and tonB genes of Sphingobium fuliginis are amplified wild-type strain ATCC 27551 from different plasmids, overview
additional information
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optimization of enzyme production scale-up for establishment of an industrial purification process using wild-type SacPox enzyme, set up of high cell density fermentation strategies. The enzyme is employable in cleaning organophosphates from different surfaces like glass, tissues, and fruits, also in presence of surfactants and even when dissolved in tap water
additional information
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variant 3B3 hydrolyzes almost exclusively the RP isomer whereas variant 3D8 is capable of hydrolyzing both RP and SP enantiomers. Variant 3B3 displays even greater stereo-specificity towards the RP enantiomers as the wild-type and mutant H115W
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