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(R)-cyclosarin + H2O
?
-
-
-
?
(R)-sarin + H2O
?
-
-
-
?
(RS)-propan-2-yl methylphosphonofluoridate + H2O
isopropyl phosphate methylphosphonate + fluoride
(RS)-propan-2-yl methylphosphonofluoridate + H2O
propan-2-yl methylphosphonate + fluoride
i.e. sarin
-
-
?
(S)-cyclosarin + H2O
?
-
-
-
?
1,2,2-trimethylpropyl methylphosphonofluoridoate + H2O
1,2,2-trimethylpropyl methylphosphonate + fluoride + H+
-
-
-
?
1-methylethyl methylphosphonofluoridoate + H2O
1-methylethyl methylphosphonate + fluoride + H+
-
-
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
3,3-dimethylbutan-2-yl methylphosphonate + fluoride
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
Pinacolyl methylphosphonate + fluoride
i.e. soman
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
4-nitrophenyl-methyl(phenyl)phosphinate + H2O
?
4-nitrophenylisopropyl phenylphosphinate + H2O
?
-
at 22% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenylpropyl phenylphosphinate + H2O
?
-
at 24% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
chlorpyrifos + H2O
?
-
-
-
?
chlorpyrifos oxon + H2O
diethyl phosphate + 3,5,6-trichloropyridin-2-ol
coumaphos + H2O
?
-
-
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
cyclohexyl methylphosphonofluoridate + H2O
cyclohexyl methylphosphonate + fluoride
i.e. cyclosarin
-
-
?
cyclohexyl methylphosphonofluoridoate + H2O
cyclohexyl methylphosphonate + fluoride + H+
-
-
-
?
cyclohexylmethylphosphonofluoridate + H2O
cyclohexyl methylphosphonate + fluoride
i.e. cyclosarin
-
-
?
cyclohexylsarin + H2O
?
-
-
-
-
?
diazinon + H2O
?
-
-
-
-
?
diethyl fluorophosphate + H2O
diethyl phosphate + fluoride
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
diisopropyl phosphorofluoridate + H2O
diisopropyl phosphate + fluoride
ethyl dimethylamidocyanophosphate + H2O
ethyl hydrogen dimethylphosphoramidate + HCN
-
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
ethyl dimethylphosphoramidocyanidate + H2O
ethyl hydrogen dimethylphosphoramidate + HCN
i.e. tabun
-
-
?
ethyl N,N-dimethylphosphoramidocyanidate + H2O
ethyl N,N-dimethylphosphoramide + cyanide
-
i.e. tabun
-
-
?
fensulfothion + H2O
?
-
-
-
-
?
methyl parathion + H2O
?
-
-
-
-
?
mipafox + H2O
?
-
i.e. N,N'-diisopropyl phosphorodiamidofluoridate, poor substrate
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphonate + fluoride
O-cyclohexylmethylphosphonofluoridate + H2O
?
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate + H2O
?
-
an organophosphorous nerve agent
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
O-pinacolylmethylphosphonofluoridate + H2O
?
-
best substrate
-
-
?
p-nitrophenyl-soman + H2O
p-nitrophenol + soman
paraoxon + H2O
diethylphosphate + 4-nitrophenol
parathion + H2O
?
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
additional information
?
-
(RS)-propan-2-yl methylphosphonofluoridate + H2O
isopropyl phosphate methylphosphonate + fluoride
i.e. sarin
-
-
?
(RS)-propan-2-yl methylphosphonofluoridate + H2O
isopropyl phosphate methylphosphonate + fluoride
i.e. sarin
-
-
?
(S)-sarin + H2O
?
-
-
-
?
(S)-sarin + H2O
?
-
the calculated free energy barrier for hydrolysis of (S)-sarin by the mechanism for diiisopropyl fluorophosphate is highly unfavorable. Hydrolysis of (S)-sarin proceeds by a mechanism in which Asp229 could activate an intervening water molecule for nucleophilic attack on the substrate
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
3,3-dimethylbutan-2-yl methylphosphonate + fluoride
i.e. soman
-
-
?
3-[fluoro(methyl)phosphoryl]oxy-2,2-dimethylbutane + H2O
3,3-dimethylbutan-2-yl methylphosphonate + fluoride
i.e. soman
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
40% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
i.e. 4-nitrophenylethyl phenylphosphinate
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
at 46% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
Rangia cuneata (Mazur-type enzyme): better substrate than diisopropyl fluorophosphate
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
i.e. NPEPP
-
-
?
4-nitrophenyl-ethyl(phenyl)phosphinate + H2O
?
-
i.e. NPEPP
-
-
?
4-nitrophenyl-methyl(phenyl)phosphinate + H2O
?
-
at 49% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenyl-methyl(phenyl)phosphinate + H2O
?
-
i.e. 4-nitrophenylmethyl phenylphosphinate
-
-
?
4-nitrophenyl-methyl(phenyl)phosphinate + H2O
?
-
at 28% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
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
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
-
(+)isomer, pH 7.2, 1 mM MnCl2
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
-
(+)isomer, pH 7.2, 1 mM MnCl2
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
-
(+)isomer, pH 7.2, 1 mM MnCl2
-
-
?
cyclosarin + H2O
?
-
-
-
-
?
cyclosarin + H2O
?
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
reaction of EC 3.1.8.1
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
reaction of EC 3.1.8.1, paraoxonase
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
highly toxic structural analogue of G-class type of nerve agents
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
spectrophotometric determination with phenol red
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
best substrate of squid enzyme
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
The mechanism for hydrolysis of diisopropyl fluorophosphate involves nucleophilic attack by Asp229 on phosphorus to form a pentavalent intermediate. P-F bond dissociation then yields a phosphoacyl enzyme intermediate in the rate-limiting step. A water molecule, coordinated to the catalytic Ca2+, donates a proton to Asp121 and then attacks the tetrahedral phosphoacyl intermediate to liberate the diisopropyl phosphate product
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
room temperature, pH 7.5
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
at about 30% of O-pinacolylmethylphosphonofluoridate hydrolysis
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
binding analysis, overview
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
at about 5-10% of soman hydrolysis
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
an analogue molecule of G-type warfare agents
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. O,O-diisopropyl phosphorofluoridate
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
-
SMP30 is important in diisopropyl phosphofluoridate detoxification
-
-
?
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
-
substrate of SMP30
-
-
?
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
-
-
-
?
diisopropyl phosphofluoridate + H2O
diisopropyl phosphate + fluoride
SMP30 is important in diisopropyl phosphofluoridate detoxification
-
-
?
diisopropyl phosphorofluoridate + H2O
diisopropyl phosphate + fluoride
-
pH 8.0, 25°C, 1 mM MgCl2
-
-
?
diisopropyl phosphorofluoridate + H2O
diisopropyl phosphate + fluoride
pH 8.0, 25°C, 1 mM MgCl2
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
ethyl dimethylphosphoramidocyanidate + H2O
?
i.e. tabun
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
-
i.e. cyclosarin
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
-
i.e. cyclosarin
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphate + fluoride
-
i.e. cyclosarin
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphonate + fluoride
-
no reaction with the (-)isomer O-cyclohexyl methylphosphonofluoridate
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphonate + fluoride
-
no reaction with the (-)isomer O-cyclohexyl methylphosphonofluoridate
-
-
?
O-cyclohexyl methylphosphonofluoridate + H2O
O-cyclohexyl methylphosphonate + fluoride
-
no reaction with the (-)isomer O-cyclohexyl methylphosphonofluoridate
-
-
?
O-cyclohexylmethylphosphonofluoridate + H2O
?
-
i.e. GF
-
-
?
O-cyclohexylmethylphosphonofluoridate + H2O
?
-
at 114% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
-
i.e. sarin
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
i.e. sarin
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
-
i.e. sarin
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
i.e. sarin
-
-
?
O-isopropylmethylphosphonofluoridate + H2O
O-isopropylmethylphosphate + fluoride
-
i.e. sarin
-
-
?
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
-
i.e. soman
-
-
?
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
i.e. soman
-
-
?
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
i.e. soman
-
-
?
O-pinacolyl methylphosphonofluoridate + H2O
O-pinacolyl methylphosphate + fluoride
-
i.e. soman
-
-
?
p-nitrophenyl-soman + H2O
p-nitrophenol + soman
-
the enzyme is immobilized on a photoluminescent porous silicon platform
soman is O-(2,3,3)-trimethylpropyl methylphosphonofluoridate
-
r
p-nitrophenyl-soman + H2O
p-nitrophenol + soman
-
the enzyme is immobilized on a photoluminescent porous silicon platform
soman is O-(2,3,3)-trimethylpropyl methylphosphonofluoridate
-
r
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
substrate are also 16 paraoxon analogs
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
-
-
-
?
phenyl acetate + H2O
phenol + acetate
pH 8.0, 25°C, 1 mM MgCl2
-
-
?
sarin + H2O
?
-
-
-
-
?
sarin + H2O
?
-
at 20% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
sarin + H2O
?
-
substrates are also p-nitrophenyl analogs of sarin, the enzyme exhibits a stereoselective preference for the R-P-enantiomers of sarin
-
-
?
sarin + H2O
?
-
i.e. O-isopropylmethylphosphonofluoridate
-
-
?
sarin + H2O
?
-
at 38% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
sarin + H2O
?
-
i.e. propyl-2-methane-fluorophosphonate
-
-
?
sarin + H2O
?
-
Mazur-type enzyme
-
-
?
sarin + H2O
?
-
i.e. O-isopropylmethylphosphonofluoridate
-
-
?
sarin + H2O
?
-
at 10% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
soman + H2O
?
-
-
-
-
?
soman + H2O
?
-
at 240% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
soman + H2O
?
-
i.e. O-pinacoyl methyl phosphonofluoridates
-
-
?
soman + H2O
?
-
substrates are also p-nitrophenyl analogs of soman, the enzyme exhibits a stereoselective preference for the R-P-enantiomers of soman
-
-
?
soman + H2O
?
-
10-20% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
soman + H2O
?
-
best substrate
-
-
?
soman + H2O
?
-
i.e. (3,3-dimethylbutyl)-2-methane-fluorophosphonate
-
-
?
soman + H2O
?
-
i.e. O-1,2,2-trimethylpropylmethylphosphono fluoride
-
-
?
soman + H2O
?
-
10% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
soman + H2O
?
-
i.e. O-1,2,2-trimethylpropylmethylphosphofluoridate
-
-
?
tabun + H2O
?
-
-
-
-
?
tabun + H2O
?
-
i.e. N,N-dimethylethylphosphoramidocyanidate, at 124% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
additional information
?
-
-
p-nitrophenyltriesters
-
-
?
additional information
?
-
-
not: 4-nitrophenylphosphonate, 4-nitrophenylphosphinorylcholine
-
-
?
additional information
?
-
-
not: 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
4-nitrophenylacetate, bis(4-nitrophenyl)phosphate, tris(4-nitrophenyl)phosphate
-
-
?
additional information
?
-
-
the natural substrates for enzyme are unknown, enzyme may, in nature, be used in peptide metabolism
-
-
?
additional information
?
-
-
the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity
-
-
?
additional information
?
-
-
the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX
-
-
?
additional information
?
-
-
OPH is able to degrade a broad list of some of the most toxic organophosphorous pesticides, such as paraoxon, and OP nerve agents including DFP, sarin, and soman
-
-
?
additional information
?
-
the enzyme also exhibits activity of EC 3.1.8.1, aryldialkylphosphatase, as well as of EC 3.1.8.2, diisopropyl-fluorophosphatase. Enzyme-substrate docking study, overview
-
-
?
additional information
?
-
-
the natural substrates for enzyme are unknown
-
-
?
additional information
?
-
-
not: 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
not: ATP
-
-
?
additional information
?
-
-
not: methanesulfonyl fluoride, phenylmethanesulfonyl fluoride, monofluorophosphate, iso-octamethylpyrophosphoramide (i.e. ios-OMPA)
-
-
?
additional information
?
-
-
the enzyme shows broad substrate specificity and is able to degrade organophosphorus compounds with P-O, P-CN, and P-F bonds and is the only enzyme known to cleave the P-S bond, which is characteristic of V-type nerve agents such as VX
-
-
?
additional information
?
-
-
additional substrate: dipeptide Gly-Pro, prolidase activity of enzyme
-
-
?
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
?
-
the enzyme is also active with substrates of EC 3.1.1.81, quorum-quenching N-acyl-homoserine lactonase, and EC 3.1.8.1, paraoxonase, hydrolyzing 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
-
-
?
additional information
?
-
-
the natural substrates for enzyme are unknown
-
-
?
additional information
?
-
-
enzyme is involved in the synthesis of isoethionate from cysteine
-
-
?
additional information
?
-
-
diisopropyl fluorophosphatase acts on a variety of organophosphorus compounds
-
-
?
additional information
?
-
-
The enzyme also acts as Ca2+-dependent phosphotriesterase. The hydrolytic reaction catalyzed by DFPase leads to the formation of a phosphate or phosphonate and a fluoride ion, resulting in detoxification of the organophosphorus agent. Presence of a phosphoenzyme intermediate in the reaction mechanism, which involves direct nucleophilic attack by Asp229 on the substrate, but no metal-assisted water activation, overview
-
-
?
additional information
?
-
diisopropyl-fluorophosphatase (DFPase) from Loligo vulgaris is highly stable and robust biocatalyst for the hydrolysis of various chemical warfare agents such as sarin, soman, tabun, but no natural substrate for DFPase has been identified to date
-
-
?
additional information
?
-
the diisopropylfluorophosphatase (DFPase) from the ganglion and brain of Loligo vulgaris acts on P-F bonds present in some organophosphorus pesticides (OPs)
-
-
?
additional information
?
-
-
the diisopropylfluorophosphatase (DFPase) from the ganglion and brain of Loligo vulgaris acts on P-F bonds present in some organophosphorus pesticides (OPs)
-
-
?
additional information
?
-
DFPase from Loligo vulgaris effectively catalyzes the hydrolysis of the bond between phosphorus and the fluoride (or cyanide) leaving group
-
-
?
additional information
?
-
DFPase from Loligo vulgaris effectively catalyzes the hydrolysis of the bond between phosphorus and the fluoride (or cyanide) leaving group
-
-
?
additional information
?
-
the enzyme is not hydrolytically active against compounds with P-O or P-S leaving group bonds, except for some soman derivatives, and shows no efficient hydrolytic activity against lactones or esters
-
-
?
additional information
?
-
the squid phosphotriesterase diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris shows relatively specific substrate preference, efficiently catalyzing the hydrolysis of diisopropyl fluorophosphate (DFP) and G-type nerve agents, including tabun (GA), sarin (GB), soman (GD), and cyclohexyl sarin (GF). The detoxification of the organophosphorous agent is achieved by the hydrolytic reaction producing a phosphate or phosphonate and a fluoride ion. The DFPase from squid central nervous system shows strong preference for the hydrolysis of P-F or P-CN bonds, which are absent in natural compounds
-
-
?
additional information
?
-
-
no activity of SMP30 with paraoxon, dihydrocoumarin, gamma-nonalactone, and delta-dodecanolactone
-
-
?
additional information
?
-
-
the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity
-
-
?
additional information
?
-
-
not: 4-nitrophenylphosphate
-
-
?
additional information
?
-
-
4-nitrophenylacetate, bis(4-nitrophenyl)phosphate, tris(4-nitrophenyl)phosphate
-
-
?
additional information
?
-
-
the ability of OPAA to cleave both G-type nerve agents comes from the hydroxide ion in the metal center that facilitates nucleophilic attack on either the carbonyl oxygen of the phosphorus center of organophosphorus nerve agents. The enzyme also shows prolidase activity
-
-
?
additional information
?
-
-
enzyme expression in liver decreases androgen-independently of aging
-
-
?
additional information
?
-
enzyme expression in liver decreases androgen-independently of aging
-
-
?
additional information
?
-
-
no activity of SMP30 with paraoxon, dihydrocoumarin, gamma-nonalactone, and delta-dodecanolactone
-
-
?
additional information
?
-
no activity of SMP30 with paraoxon, dihydrocoumarin, gamma-nonalactone, and delta-dodecanolactone
-
-
?
additional information
?
-
-
no activity with paraoxon, dihydrocoumarin, gamma-nonalactone and delta-dodecanolactone
-
-
?
additional information
?
-
no activity with paraoxon, dihydrocoumarin, gamma-nonalactone and delta-dodecanolactone
-
-
?
additional information
?
-
the substrates of enzyme OPH include organophosphate insecticides paraoxon, parathion, methylparathion, coumaphos, and diazinon, as well as potent nerve agents sarin, soman, and their analogue diisopropylfluorophosphate (DFP), cf. EC 3.1.8.1 and 3.1.8.2
-
-
?
additional information
?
-
-
no substrates are N-acetylvaline, N-acetylleucine, N-acetylmethionine or N-acetylalanine, sodium diphosphate, parathion, octamethylpyrophosphoramide (i.e. OMPA), triacetin, creatine phosphate, acetylcholine, butyrylcholine
-
-
?
additional information
?
-
-
not: ATP
-
-
?
additional information
?
-
-
Tetrahymena thermophila has 5 enzyme forms, some share characteristics of both the squid and the Mazur-type DFPase
-
-
?
additional information
?
-
-
the natural substrates for enzyme are unknown
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.39
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
0.45
diazinon
-
pH not specified in the publication, temperature not specified in the publication
0.048 - 65.45
diisopropyl fluorophosphate
0.46
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
0.08
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
0.68
O-cyclohexyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.43
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
0.7 - 1.57
O-isopropylmethylphosphonofluoridate
0.5 - 2.48
O-pinacolyl methylphosphonofluoridate
0.24
parathion
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
0.048
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
2.12
diisopropyl fluorophosphate
mutant enzyme E37A/Y144A/R146A/T195M
2.72
diisopropyl fluorophosphate
wild-type, pH 7.5, 25°C, in nitrogen atmosphere
2.92
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 1-amino-2-propanol
2.95
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 2-amino-2-methyl-1-propanol
2.99
diisopropyl fluorophosphate
-
-
2.99
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
2.99
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 1 mM NaF
3.01
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme
3.08
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethanol
3.1
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y
3.15
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM monoethanolamine
3.18
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methanol
3.2
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y
3.2
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y
3.35
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM diethanolamine
3.38
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM glycerol
3.57
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 2 mM NaF
3.63
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
3.76
diisopropyl fluorophosphate
wild type enzyme
3.87
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 200 mM thiodipropanol and 1 mM NaF
3.93
diisopropyl fluorophosphate
mutant enzyme E37D/Y144A/R16A/T195M
3.97
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodiglycol
4
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y, with 300 mM triethanolamine
4.06
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol and 1 mM NaF
4.1
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethanolamine
4.17
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine and 300 mM ethanol
4.2
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y, with 300 mM triethanolamine
4.21
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triisopropanolamine
4.23
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 100 mM thiodipropanol and 1 mM NaF
4.3
diisopropyl fluorophosphate
-
pH 7.5, 22°C
4.32
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine and 300 mM ethanol
4.32
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM triethanolamine
4.41
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine and 300 mM ethanol
4.44
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine
4.45
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 3 mM NaF
4.45
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine and 300 mM ethanol
4.5
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y, with 300 mM triethanolamine
4.52
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine
4.54
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 200 mM thiodipropanol and 2 mM NaF
4.56
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine
4.58
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol and 2 mM NaF
4.61
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 3-amino-1-propanol
4.67
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine
4.7
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
4.77
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol
4.87
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 100 mM thiodipropanol and 2 mM NaF
4.89
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol and 3 mM NaF
5.04
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 200 mM thiodipropanol and 3 mM NaF
5.58
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 100 mM thiodipropanol and 3 mM NaF
23.36
diisopropyl fluorophosphate
wild-type, presence of 1 mM O,O-dicyclopentylphosphoroamidate, pH 7.5, 25°C, in nitrogen atmosphere
65.45
diisopropyl fluorophosphate
wild-type, presence of 3 mM O,O-dicyclopentylphosphoroamidate, pH 7.5, 25°C, in nitrogen atmosphere
0.7
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
1.57
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.5
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
2.48
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.058
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
1.27
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
2.48
soman
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
effects of pH, temperature and ionic strength on KM are studied
-
additional information
additional information
-
comparison of kinetic constants of paraoxon analogs
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetic analysis, substrate diisopropyl fluorophosphate in presence of aminoalcohol activators
-
additional information
additional information
reaction kinetics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
610
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
176
diazinon
-
pH not specified in the publication, temperature not specified in the publication
0.0115 - 2111
diisopropyl fluorophosphate
67
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
189
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
652
O-cyclohexyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.3
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
56 - 442
O-isopropylmethylphosphonofluoridate
5 - 151
O-pinacolyl methylphosphonofluoridate
630
parathion
-
pH not specified in the publication, temperature not specified in the publication
0.0115
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM glycerol
0.0117
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0123
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethanol
0.0123
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methanol
0.0142
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 3-amino-1-propanol
0.0148
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine
0.0151
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol
0.0155
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine and 300 mM ethanol
0.0163
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine
0.0178
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine and 300 mM ethanol
0.018
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine
0.0193
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine
0.0195
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 1-amino-2-propanol
0.0195
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine and 300 mM ethanol
0.0209
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM monoethanolamine
0.0211
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 2-amino-2-methyl-1-propanol
0.0216
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine and 300 mM ethanol
0.0295
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodiglycol
0.031
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y
0.0312
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM diethanolamine
0.0361
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triisopropanolamine
0.042
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethanolamine
0.0477
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM triethanolamine
0.048
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y
0.049
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y
0.142
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y, with 300 mM triethanolamine
0.182
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y, with 300 mM triethanolamine
0.217
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y, with 300 mM triethanolamine
9.69
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
20.35
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
208
diisopropyl fluorophosphate
-
pH 8, 35°C, effects of pH, temperature and ionic strength on kcat are studied
211
diisopropyl fluorophosphate
wild type enzyme
230
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
291
diisopropyl fluorophosphate
mutant enzyme E37A/Y144A/R146A/T195M
376
diisopropyl fluorophosphate
mutant enzyme E37D/Y144A/R16A/T195M
465
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
583
diisopropyl fluorophosphate
-
pH 7.5, 22°C
917
diisopropyl fluorophosphate
-
value above
2091
diisopropyl fluorophosphate
wild-type, presence of 3 mM O,O-dicyclopentylphosphoroamidate, pH 7.5, 25°C, in nitrogen atmosphere
2107
diisopropyl fluorophosphate
wild-type, pH 7.5, 25°C, in nitrogen atmosphere
2111
diisopropyl fluorophosphate
wild-type, presence of 1 mM O,O-dicyclopentylphosphoroamidate, pH 7.5, 25°C, in nitrogen atmosphere
56
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
442
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
5
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
151
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
6.11
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
3170
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1600
Coumaphos
-
pH not specified in the publication, temperature not specified in the publication
390
diazinon
-
pH not specified in the publication, temperature not specified in the publication
0.0031 - 9700
diisopropyl fluorophosphate
150
fensulfothion
-
pH not specified in the publication, temperature not specified in the publication
2400
methyl parathion
-
pH not specified in the publication, temperature not specified in the publication
959
O-cyclohexyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
0.045
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate
-
pH not specified in the publication, temperature not specified in the publication
80 - 282
O-isopropylmethylphosphonofluoridate
10 - 61
O-pinacolyl methylphosphonofluoridate
55000
paraoxon
-
pH not specified in the publication, temperature not specified in the publication
2600
parathion
-
pH not specified in the publication, temperature not specified in the publication
27
(R)-cyclosarin
mutant enzyme E37D/Y144A/R16A/T195M
130
(R)-cyclosarin
mutant enzyme E37A/Y144A/R146A/T195M
720
(R)-cyclosarin
wild type enzyme
24
(R)-sarin
mutant enzyme E37D/Y144A/R16A/T195M
45
(R)-sarin
mutant enzyme E37A/Y144A/R146A/T195M
47
(R)-sarin
wild type enzyme
17
(S)-cyclosarin
wild type enzyme
24
(S)-cyclosarin
mutant enzyme E37D/Y144A/R16A/T195M
490
(S)-cyclosarin
mutant enzyme E37A/Y144A/R146A/T195M
42
(S)-sarin
wild type enzyme
71
(S)-sarin
mutant enzyme E37D/Y144A/R16A/T195M
230
(S)-sarin
mutant enzyme E37A/Y144A/R146A/T195M
0.0031
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 3-amino-1-propanol
0.0032
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodipropanol
0.0033
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine
0.0034
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM glycerol
0.0035
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine
0.0035
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine and 300 mM ethanol
0.0039
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme
0.0039
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methanol
0.004
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM diethylamine and 300 mM ethanol
0.004
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethanol
0.004
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine
0.0044
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine
0.0045
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine and 300 mM ethanol
0.0052
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM methylamine and 300 mM ethanol
0.0066
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM monoethanolamine
0.0067
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 1-amino-2-propanol
0.0072
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM 2-amino-2-methyl-1-propanol
0.0074
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM thiodiglycol
0.0086
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triisopropanolamine
0.0093
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM diethanolamine
0.0098
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y
0.01
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethanolamine
0.011
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant wild-type enzyme, with 400 mM triethanolamine
0.0153
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y
0.016
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y
0.032
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant L140Y, with 300 mM triethanolamine
0.043
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y, with 300 mM triethanolamine
0.054
diisopropyl fluorophosphate
pH 8.0, 25°C, recombinant mutant F132Y/L140Y, with 300 mM triethanolamine
2.67
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1 wild-type enzyme
4.33
diisopropyl fluorophosphate
pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme
56
diisopropyl fluorophosphate
wild type enzyme
77
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
96
diisopropyl fluorophosphate
mutant enzyme E37D/Y144A/R16A/T195M
140
diisopropyl fluorophosphate
mutant enzyme E37A/Y144A/R146A/T195M
9700
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
80
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
282
O-isopropylmethylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
10
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
61
O-pinacolyl methylphosphonofluoridate
-
pH not specified in the publication, temperature not specified in the publication
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evolution
the phosphotriesterase activity development between PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, is investigated by using the hybrid density functional theory method B3LYP. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca2+ ion indirectly connecting the buried structural Ca2+ ion via hydrogen bonds in DFPase. It can reduce the plasticity of enzymatic structure, and possibly change the substrate preference from paraoxon (preferred substrate of PON1) to DFP (preferred substrate of DFPase), which implies an evolutionary transition from mono- to dinuclear catalytic centers, enzyme catalysis mechanism from an evolutionary perspective, overview
malfunction
insufficient organophosphate-hydrolyzing activity of native enzyme affirms the urgent need to develop improved variant(s) having enhanced organophosphate-hydrolyzing activity. Enzyme mutants show altered substrate specificity with increased activity against paraoxon and lactone substrates, overview
physiological function
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diisopropyl fluorophosphatase is a calcium-dependent phosphotriesterase that acts on a variety of highly toxic organophosphorus compounds, that act as inhibitors of acetylcholinesterase
physiological function
human paraoxonase 1 (h-PON1) is a serum enzyme that can hydrolyze a variety of substrates, including organophosphate (OP) compounds. PON1 can hydrolyze and inactivate a variety of organophosphate (OP) compounds, including certain OP pesticides and nerve agents (NAs). It is a potential candidate for the development of antidote against OP poisoning in humans. The enzyme possesses anti-inflammatory, anti-oxidative, anti-diabetic and quorum sensor-hydrolyzing activities, it is proposed that the lactonase activity of the enzyme is important for these defensive roles, cf. EC 3.1.1.81
physiological function
the enzyme efficiently catalyze the hydrolysis of the substrate diisopropyl fluorophosphate and a wide range of organophosphorus nerve agents, including soman, sarin, and tabun
physiological function
the squid phosphotriesterase diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris shows relatively specific substrate preference, efficiently catalyzing the hydrolysis of diisopropyl fluorophosphate (DFP) and G-type nerve agents, including tabun (GA), sarin (GB), soman (GD), and cyclohexyl sarin (GF). The detoxification of the organophosphorous (OP) agent is achieved by the hydrolytic reaction producing a phosphate or phosphonate and a fluoride ion
additional information
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organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
additional information
-
organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
additional information
-
organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
additional information
-
organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
additional information
-
organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
additional information
the OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions. The native enzyme structure reveals the presence of a well-defined nonproteinaceous density in the active site, which might be due to a bound glycolate, which is isosteric with a glycine product. All three glycolate oxygens coordinate the two Mn2+ atoms
additional information
h-PON1 is a polymorphic enzyme. Molecular docking analysis, homology modelling, overview
additional information
in detoxification of nerve gas compounds or pesticides in the human body, due to non-human origin of the enzyme, immunological reactions occur when it is injected into body. In order to using DFPase as in vivo detoxifying agent, some manipulations to augment of its efficiency and to decrease of immunogenic problems are needed. Modifications such as PEGylation is one of the possible solutions to conquer these problems
additional information
residue Asp229 plays a role in the coordination variation of calcium during the reaction. Quantum mechanical/molecular mechanical umbrella sampling simulations displays that the hydrolysis of diisopropyl fluorophosphate (DFP) and (S)-sarin processes by DFPase presents two different reaction pathways involving nucleophilic attack by Asp229 or an activated water on phosphorus. Modeling of active site and reaction mechanism with nucleophile Asp229 and coordinating Ca2+, detailed overview. Optimized geometries for the intermediates, transition state, and product for the hydrolysis step of DFPase
additional information
residue Asp229 plays a role in the coordination variation of calcium during the reaction. Quantum mechanical/molecular mechanical umbrella sampling simulations displays that the hydrolysis of diisopropyl fluorophosphate (DFP) and (S)-sarin processes by DFPase presents two different reaction pathways involving nucleophilic attack by Asp229 or an activated water on phosphorus. Modeling of active site and reaction mechanism with nucleophile Asp229 and coordinating Ca2+, detailed overview. Optimized geometries for the intermediates, transition state, and product for the hydrolysis step of DFPase
additional information
the metal-substituted catalysts generates the activated water molecules that initiate nucleophilic attack on the phosphorus atom of the substrate, resulting in the cleavage of phosphoester bond and the release of leaving group
additional information
the phosphotriesterase diisopropyl fluorophosphatase (DFPase) is a calcium-dependent beta-propeller protein. PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, seem to employ similar catalytic mechanisms as phosphotriesterase, due to their structural similarities of active sites. The attacking nucleophile for phosphotriester hydrolysis is identified to be an activated water molecule, with the nucleophile attacking the phosphorus center. The E53Q and D269N mutants in PON1 both possess measurable lactonase and paraoxonase activity, and mutation studies combined with related molecular dynamics simulations suggest that the water activated by Glu53 and Asp269 is the most likely attacking nucleophile. Analysis of the rate-determining reaction step of the organophosphorus compound hydrolysis catalyzed both by DFPase and PON1. Structure-function relationship, overview. Active site structure of DFPase (PDB ID 2GVW) and substrate docking
additional information
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organophosphorus hydrolase, OPH, contains a two-oxygen bridging mechanism in the active site suggesting subtle differences compared to organophosphorus acid anhydrolase, OPAA. OPAAs exhibit higher soman activities, whereas OPHs have higher activity against the organophosphorus pesticide paraoxon
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additional information
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the OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions. The native enzyme structure reveals the presence of a well-defined nonproteinaceous density in the active site, which might be due to a bound glycolate, which is isosteric with a glycine product. All three glycolate oxygens coordinate the two Mn2+ atoms
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H254R
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the active site mutation results in increased activity with soman and VX
H275L
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the active site mutation results in increased activity with soman and VX
H275V
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the active site mutation results in increased activity with soman and VX
H115W/R192K
site-directed mutagenesis, the mutant shows altered substrate specificity compared to wild-type
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
L55M
natural polymorphism, the polymorphism at the 55th position of h-PON1 does not affect the catalytic properties of the enzyme
R192E
natural polymorphism, polymorphism at position 192 plays an important role in determining the substrate specificity and catalytic efficiency of the enzyme
Asp229/Asn120
site-directed mutagenesis, the mutant shows impaired catalytic activity or decreased substrate binding affinity
Asp229/Asn175
site-directed mutagenesis, the mutant shows impaired catalytic activity or decreased substrate binding affinity
D121E
the mutant displays 87% activity compared to the wild type enzyme
D229N
enzymatically inactive
D229N/N175D
catalytically inactive, no change in the calcium coordinating environment
D232S
3% higher activity than the wild-type
E21Q/N120D
catalytically inactive
E21Q/N120D/N175D/D229N
the mutations lead to a loss of calcium binding and enzymatic activity
E21Q/N175D
catalytically inactive
E37A/Y144A/R146A/T195M
the mutant shows increased turnover number and kcat/Km for diisopropyl fluorophosphate compared to the wild type enzyme
E37D/Y144A/R16A/T195M
the mutant shows increased turnover number and kcat/Km for diisopropyl fluorophosphate compared to the wild type enzyme
F173A
84% lower activity than the wild-type
F173L
28% lower activity than the wild-type
F173S
68% lower activity than the wild-type
F173V
46% lower activity than the wild-type
F173W
19% lower activity than the wild-type
F173Y
53% lower activity than the wild-type
F314A
3% higher activity than the wild-type
Glu21/Asn120
site-directed mutagenesis, the mutant shows impaired catalytic activity or decreased substrate binding affinity
Glu21/Asn175
site-directed mutagenesis, the mutant shows impaired catalytic activity or decreased substrate binding affinity
H219N
-
no effect on catalytic activity
H224N
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115% activity in comparison to wild-type enzyme
H248N
-
no effect on catalytic activity
H287A
90% lower activity than the wild-type
H287D
99% lower activity than the wild-type
H287F
36% lower activity than the wild-type
H287L
21% lower activity than the wild-type
H287Q
54% lower activity than the wild-type
H287W
34% lower activity than the wild-type
H287Y
57% lower activity than the wild-type
M148A
26% lower activity than the wild-type
N120D
96% lower activity than the wild-type
N120D/N175D/D229N
the mutations lead to a loss of calcium binding and enzymatic activity
N175D
98% lower activity than the wild-type
N237S
4% lower activity than the wild-type
Q304F
50% lower activity than the wild-type
Q304W
3% lower activity than the wild-type
Q77W
6% higher activity than the wild-type
Q77Y
6% lower activity than the wild-type
R146S
45% lower activity than the wild-type
S271A
34% higher activity than the wild-type
S271A/D232S
19% lower activity than the wild-type
T195A
60% lower activity than the wild-type
T195L
11% lower activity than the wild-type
T195V
3% lower activity than the wild-type
Y144S
8% higher activity than the wild-type
F132Y
site-directed mutagenesis, the mutant exhibits a 3fold increased activity with diisopropyl fluorophosphate compared to wild-type
F132Y/ L140Y
site-directed mutagenesis, the mutant exhibits a several folds increased activity with diisopropyl fluorophosphate compared to wild-type
L140Y
site-directed mutagenesis, the mutant exhibits a 5fold increased activity with diisopropyl fluorophosphate compared to wild-type
D229N/N120D
no activity
D229N/N120D
catalytically inactive, no change in the calcium coordinating environment
H181N
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20% loss of activity in comparison to wild-type enzyme
H181N
19% lower activity than the wild-type
H274N
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slight loss of activity in comparison to wild-type enzyme using pH Stat measurements, no alteration is observed with fluoride assay
H274N
7% lower activity than the wild-type
H287N
-
96% loss of activity in comparison to wild-type enzyme
H287N
96% lower activity than the wild-type
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 are 2fold less efficient with N,N-diethyl substrates and 5fold less efficient with N,N-dimethyl substrates
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
additional information
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
additional information
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chemical modification of Tyr, Cys, Arg, Lys, Glu and Asp, this residues are not critical for catalysis
additional information
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preparation of bicontinuous microemulsions made of sugar surfactants as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, scattering experiments. DFPase still has high activity in this complex reaction medium, overview
additional information
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reengineering of DFPase through rational design to bind and productively orient the more toxic SP stereoisomers of the nerve agents sarin and cyclosarin, creating a modified enzyme with enhanced overall activity and significantly increased detoxification properties
additional information
intracellular production of organophosphorus pesticides (OPs)-degrading enzymes or the use of native bacteria and fungi leads to a low degradation rate of OPs due to a mass transfer issue which reduces the overall catalytic efficiency. To overcome this challenge, DFPase is expressed on the surface of Escherichia coli for the first time by employing the N-terminal domain of the ice nucleation protein (InaV-N) as an anchoring motif. The recombinant DFPase is successfully located on the outer membrane and shows a significant ability for the biodegradation of diisopropylfluorophosphate (DFP) with a specific activity of 500 U/mg of wet cell weight. The recombinant cells can also degrade chlorpyrifos. No enzyme activity is measured by the fluoride ion-selective electrode in the control sample, inner membrane fraction, or cytoplasm fraction of pET-28a-InaV-N-DFPase cells. High potential of the InaV-N anchoring domain to produce an engineered bacterium that can be used in the bioremediation of pesticide-contaminated environments
additional information
-
intracellular production of organophosphorus pesticides (OPs)-degrading enzymes or the use of native bacteria and fungi leads to a low degradation rate of OPs due to a mass transfer issue which reduces the overall catalytic efficiency. To overcome this challenge, DFPase is expressed on the surface of Escherichia coli for the first time by employing the N-terminal domain of the ice nucleation protein (InaV-N) as an anchoring motif. The recombinant DFPase is successfully located on the outer membrane and shows a significant ability for the biodegradation of diisopropylfluorophosphate (DFP) with a specific activity of 500 U/mg of wet cell weight. The recombinant cells can also degrade chlorpyrifos. No enzyme activity is measured by the fluoride ion-selective electrode in the control sample, inner membrane fraction, or cytoplasm fraction of pET-28a-InaV-N-DFPase cells. High potential of the InaV-N anchoring domain to produce an engineered bacterium that can be used in the bioremediation of pesticide-contaminated environments
additional information
the kinetic measurements of enzyme mutants show that the double mutants Glu21/Asn120, Glu21/Asn175, Asp229/Asn120, and Asp229/Asn175 have impaired catalytic activity or decreased substrate binding affinity although their structures provide unchanged calcium coordination environment proving signification of suitable electrostatic effect of the active site for binding and catalysis
additional information
the kinetic measurements of enzyme mutants show that the double mutants Glu21/Asn120, Glu21/Asn175, Asp229/Asn120, and Asp229/Asn175 have impaired catalytic activity or decreased substrate binding affinity although their structures provide unchanged calcium coordination environment proving signification of suitable electrostatic effect of the active site for binding and catalysis
additional information
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construction of SMP30 knockout mice showing no activity with diisopropyl phosphofluoridate in livers, the liver of the mutant mice is far more susceptible to cytotoxicity of diisopropyl phosphofluoridate
additional information
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preparation of a direct conjugation of organophosphorus acid anhydrolase with CdS quantum dots via arrested precipitation within the enzyme matrix. The bio-conjugate not only retains enzyme conformational structure but also retains enzyme activity and is effective at detecting diisopropyl fluorophosphate at the micromolar level. Purification of the conjugates by gel filtration. Circular dichroism spectrometric and high resolution transmission electron microscope conjugate structure analysis, overview
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Loligo sp.
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Loligo vulgaris (Q7SIG4)
brenda
Blum, M.M.; Tomanicek, S.J.; John, H.; Hanson, B.L.; Rueterjans, H.; Schoenborn, B.P.; Langan, P.; Chen, J.C.
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction
Acta Crystallogr. Sect. F
66
379-385
2010
Loligo vulgaris (Q7SIG4)
brenda
Gaeb, J.; Melzer, M.; Kehe, K.; Wellert, S.; Hellweg, T.; Blum, M.M.
Monitoring the hydrolysis of toxic organophosphonate nerve agents in aqueous buffer and in bicontinuous microemulsions by use of diisopropyl fluorophosphatase (DFPase) with 1H-31P HSQC NMR spectroscopy
Anal. Bioanal. Chem.
396
1213-1221
2010
Loligo vulgaris
brenda
Choi, M.S.; Saxena, A.; Chilukuri, N.
A strategy for the production of soluble human senescence marker protein-30 in Escherichia coli
Biochem. Biophys. Res. Commun.
393
509-513
2010
Homo sapiens
brenda
Blum, M.M.; Chen, J.C.
Structural characterization of the catalytic calcium-binding site in diisopropyl fluorophosphatase (DFPase)-Comparison with related beta-propeller enzymes
Chem. Biol. Interact.
187
373-379
2010
Loligo vulgaris (Q7SIG4)
brenda
Melzer, M.; Chen, J.C.; Heidenreich, A.; Gaeb, J.; Koller, M.; Kehe, K.; Blum, M.M.
Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design
J. Am. Chem. Soc.
131
17226-17232
2009
Loligo vulgaris (Q7SIG4)
brenda
Vyas, N.K.; Nickitenko, A.; Rastogi, V.K.; Shah, S.S.; Quiocho, F.A.
Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase
Biochemistry
49
547-559
2010
Alteromonas sp. (Q44238), Alteromonas sp. JD6.5 (Q44238)
brenda
Chen, J.C.; Mustyakimov, M.; Schoenborn, B.P.; Langan, P.; Blum, M.M.
Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase)
Acta Crystallogr. Sect. D
66
1131-1138
2010
Loligo vulgaris
brenda
Theriot, C.M.; Grunden, A.M.
Hydrolysis of organophosphorus compounds by microbial enzymes
Appl. Microbiol. Biotechnol.
89
35-43
2011
Alteromonas sp., Pseudoalteromonas undina, Brevundimonas diminuta, Flavobacterium sp., Pseudoalteromonas haloplanktis, Alteromonas sp. JD6.5
brenda
Zhao, L.; Gattas-Asfura, K.M.; Xu, J.; Patel, R.A.; Dadlani, A.; Sillero-Mahinay, M.; Cushmore, M.; Rastogi, V.K.; Shah, S.S.; Leblanc, R.M.
Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots
Chem. Commun. (Camb. )
47
7242-7244
2011
Pseudomonas aeruginosa
brenda
Wellert, S.; Tiersch, B.; Koetz, J.; Richardt, A.; Lapp, A.; Holderer, O.; Gaeb, J.; Blum, M.M.; Schulreich, C.; Stehle, R.; Hellweg, T.
The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity
Eur. Biophys. J.
40
761-774
2011
Loligo vulgaris
brenda
Belinskaya, T.; Pattabiraman, N.; diTargiani, R.; Choi, M.; Saxena, A.
Differences in amino acid residues in the binding pockets dictate substrate specificities of mouse senescence marker protein-30, human paraoxonase1, and squid diisopropylfluorophosphatase
Biochim. Biophys. Acta
1824
701-710
2012
Loligo vulgaris (Q7SIG4)
brenda
Wymore, T.; Field, M.J.; Langan, P.; Smith, J.C.; Parks, J.M.
Hydrolysis of DFP and the nerve agent (S)-sarin by DFPase proceeds along two different reaction pathways: Implications for engineering bioscavengers
J. Phys. Chem. B
118
4479-4489
2014
Loligo vulgaris (Q7SIG4)
brenda
Latifi, A.M.; Karami, A.; Khodi, S.
Efficient surface display of diisopropylfluorophosphatase (DFPase) in E. coli for biodegradation of toxic organophosphorus compounds (DFP and Cp)
Appl. Biochem. Biotechnol.
177
624-636
2015
Loligo vulgaris (Q7SIG4), Loligo vulgaris
brenda
Tripathy, R.K.; Aggarwal, G.; Bajaj, P.; Kathuria, D.; Bharatam, P.V.; Pande, A.H.
Towards understanding the catalytic mechanism of human paraoxonase 1 experimental and in silico mutagenesis studies
Appl. Biochem. Biotechnol.
182
1642-1662
2017
Homo sapiens (P27169)
brenda
Goldsmith, M.; Eckstein, S.; Ashani, Y.; Greisen, P.; Leader, H.; Sussman, J.L.; Aggarwal, N.; Ovchinnikov, S.; Tawfik, D.S.; Baker, D.; Thiermann, H.; Worek, F.
Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro
Arch. Toxicol.
90
2711-2724
2016
Brevundimonas diminuta (P0A434)
brenda
Allahyari, H.; Latifi, A.
Diisopropyl-fluorophosphatase as a catalytic bioscavenger
J. Appl. Biotechnol. Rep.
3
477-482
2016
Loligo vulgaris (Q7SIG4)
-
brenda
Zhang, H.; Yang, L.; Ma, Y.Y.; Zhu, C.; Lin, S.; Liao, R.Z.
Theoretical studies on catalysis mechanisms of serum paraoxonase 1 and phosphotriesterase diisopropyl fluorophosphatase suggest the alteration of substrate preference from paraoxonase to DFP
Molecules
23
1660
2018
Loligo vulgaris (Q7SIG4)
brenda
Li, D.; Zhang, Y.; Song, H.; Lu, L.; Liu, D.; Yuan, Y.
Aminoalcohol-induced activation of organophosphorus hydrolase (OPH) towards diisopropylfluorophosphate (DFP)
PLoS ONE
12
e0169937
2017
Sphingobium fuliginis (P0A433)
brenda
Yun, H.; Yu, J.; Kim, S.; Lee, N.; Lee, J.; Lee, S.; Kim, N.D.; Yu, C.; Rho, J.
Expression and purification of biologically active recombinant human paraoxonase 1 from a Drosophila S2 stable cell line
Protein Expr. Purif.
131
34-41
2017
Homo sapiens (P27169)
brenda
Xu, C.; Yang, L.; Yu, J.; Liao, R.
What roles do the residue Asp229 and the coordination variation of calcium play of the reaction mechanism of the diisopropyl-fluorophosphatase? A DFT investigation
Theoret. Chem. Accounts
135
1-11
2016
Loligo vulgaris (Q7SIG4)
-
brenda
Xu, C.; Yang, L.; Yu, J.; Liao, R.
What roles do the residue Asp229 and the coordination variation of calcium play of the reaction mechanism of the diisopropyl-fluorophosphatase? A DFT investigation
Theoret. Chem. Accounts
135
138
2016
Loligo vulgaris (Q7SIG4)
-
brenda