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(R)-cyclosarin + H2O
?
-
-
-
-
?
(R)-sarin + H2O
?
-
-
-
-
?
(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+
-
-
-
-
?
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
-
-
?
coumaphos + H2O
?
-
-
-
-
?
cyclohexyl methyl fluorophosphate + H2O
cyclohexyl methyl hydrogen phosphate + fluoride
cyclohexyl methylphosphonofluoridoate + H2O
cyclohexyl methylphosphonate + fluoride + H+
-
-
-
-
-
cyclohexylsarin + H2O
?
-
-
-
-
?
cyclosarin + H2O
?
-
-
-
-
?
diazinon + H2O
?
-
-
-
-
?
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 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
parathion + H2O
?
-
-
-
-
?
phenyl acetate + H2O
phenol + acetate
additional information
?
-
(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
-
?
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
-
-
?
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
-
-
?
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
-
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
-
-
646558, 646561, 680347, 690417, 694919, 701555, 701660, 703171, 704184, 713615, 729284 -
-
?
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
-
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
-
-
?
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

?
-
-
-
-
?
paraoxon + H2O
?
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
paraoxon + H2O
?
-
substrate are also 16 paraoxon analogs
-
-
?
paraoxon + H2O
?
-
-
-
-
?
paraoxon + H2O
?
-
-
-
-
?
paraoxon + H2O
?
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
paraoxon + H2O
?
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
-
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 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
?
-
-
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
?
-
-
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
?
-
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 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
2.99
diisopropyl fluorophosphate
-
-
2.99
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
3.76
diisopropyl fluorophosphate
-
wild type enzyme
3.93
diisopropyl fluorophosphate
-
mutant enzyme E37D/Y144A/R16A/T195M
4.3
diisopropyl fluorophosphate
-
pH 7.5, 22°C
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
-
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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
208 - 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
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
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H254R
-
the active site mutation results in increased activity with soman and VX
H275L
-
the active site mutation results in increased activity with soman and VX
H275V
-
the active site mutation results in increased activity with soman and VX
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
H219N
-
no effect on catalytic activity
H224N
-
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
D229N/N120D

-
no activity
D229N/N120D
-
catalytically inactive, no change in the calcium coordinating environment
H181N

-
20% loss of activity in comparison to wild-type enzyme
H181N
-
19% lower activity than the wild-type
H274N

-
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

-
chemical modification of Tyr, Cys, Arg, Lys, Glu and Asp, this residues are not critical for catalysis
additional information
-
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
-
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
-
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
-
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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Cohen, J.A.; Warringa, M.G.P.J.
Purification and properties of dialkylfluorophosphatase
Biochim. Biophys. Acta
26
29-39
1957
Sus scrofa
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Hoskin, F.C.G.; Long, R.J.
Purification of a DFP-hydrolyzing enzyme from squid head ganglion
Arch. Biochem. Biophys.
150
548-555
1972
Aplysia sp., Doryteuthis pealeii, Octopus sp., Peltodoris nobilis, Sepiidae, Spisula solidissima
brenda
DeFrank, J.J.; Cheng, T.C.
Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate
J. Bacteriol.
173
1938-1943
1991
Alteromonas sp.
brenda
Cheng, T.C.; Harvey, S.P.; Stroup, A.N.
Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina
Appl. Environ. Microbiol.
59
3138-3140
1993
Pseudoalteromonas undina
brenda
Wang, F.; Xiao, M.; Mu, S.
Purification and properties of a diisopropyl-fluorophosphatase from squid Todarodes pacificus steenstrup
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8
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1993
Todarodes pacificus
brenda
Kopec-Smith, K.; Deschamps, J.R.; Loomis, L.D.; Ward, K.B.
A partial primary structure of squid hepatopancreas organophosphorus acid anhydrolase
Chem. Biol. Interact.
87
49-54
1993
Doryteuthis pealeii
brenda
Landis, W.G.; Anderson, R.S.; Chester, N.A.; Durst, H.D.; Haley, M.V.; Johnson, D.W.; Tauber, R.M.
The organophosphate acid anhydrases of the protozoan, Tetrahymena thermophila, and the clam, Rangia cuneata
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1989
Rangia cuneata, Sus scrofa, Tetrahymena thermophila
-
brenda
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Alternative substrates and an inhibitor of the organophosphate acid anhydrase activities of the protozoan, Tetrahymena thermophila
Comp. Biochem. Physiol. C
92
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1989
Sus scrofa, Tetrahymena thermophila
-
brenda
Landis, W.G.; Haley, M.V.; Johnson, D.W.
Kinetics of the DFPase activity in Tetrahymena thermophila
J. Protozool.
33
216-218
1986
Tetrahymena thermophila
brenda
Hoskin, F.C.G.; Prusch, R.D.
Characterization of a DFP-hydrolyzing enzyme in squid posterior salivary gland by use of Soman, DFP and manganous ion
comp. Biochem. Physiol. C
75
17-20
1983
Loligo sp., Rattus norvegicus
brenda
Garden, J.M.; Hause, S.K.; Hoskin, F.C.G.; Roush, A.H.
Comparison of DFP-hydrolyzing enzyme purified from head ganglion and hepatopancreas of squid (Loligo pealei) by means of isoelectric focusing
Comp. Biochem. Physiol. C
52
95-98
1975
Doryteuthis pealeii
brenda
Hoskin, F.C.G.
Squid nerve type DFPase. Molecular structures
Jerus. Symp. Quantum Chem. Biochem.
7
209-211
1974
Loligo sp.
-
brenda
Koepke, J.; Scharff, E.I.; Lucke, C.; Ruterjans, H.; Fritzsch, G.
Atomic resolution crystal structure of squid ganglion DFPase
Acta Crystallogr. Sect. D
58
1757-1759
2002
Loligo sp.
brenda
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Crystallization and preliminary X-ray crystallographic analysis of DFPase from Loligo vulgaris
Acta Crystallogr. Sect. D
57
148-149
2001
Loligo vulgaris
brenda
Cheng, T.C.; Harvey, S.P.; Chen, G.L.
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62
1636-1641
1996
Alteromonas sp.
brenda
Hill, C.M.; Li, W.S.; Cheng, T.C.; DeFrank, J.J.; Raushel, F.M.
Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin
Bioorg. Chem.
29
27-35
2001
Alteromonas sp.
brenda
Hartleib, J.; Ruterjans, H.
High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris
Protein Expr. Purif.
21
210-219
2001
Loligo vulgaris
brenda
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Insights into the reaction mechanism of the diisopropyl fluorophosphatase from Loligo vulgaris by means of kinetic studies, chemical modification and site-directed mutagenesis
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1546
312-324
2001
Loligo vulgaris
brenda
Hill, C.M.; Wu, F.; Cheng, T.C.; DeFrank, J.J.; Raushel, F.M.
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10
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2000
Alteromonas sp.
brenda
Hoskin, F.C.; Walker, J.E.; Mello, C.M.
Organophosphorus acid anhydrolase in slime mold, duckweed and mung bean: a continuing search for a physiological role and a natural substrate
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119-120
399-404
1999
Dictyostelium discoideum, Landoltia punctata, no activity in Lemna minor, Vigna radiata
brenda
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57
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Alteromonas sp.
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Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme
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44
9022-9033
2005
Loligo vulgaris, Loligo vulgaris (Q7SIG4)
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851-853
2005
Alteromonas sp., Alteromonas sp. JD6.5
brenda
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Stereospecificity in the enzymatic hydrolysis of cyclosarin (GF)
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Alteromonas sp., Alteromonas sp. JD6.5, Pseudoalteromonas haloplanktis
-
brenda
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Mus musculus, Rattus norvegicus (Q03336), Rattus norvegicus
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Dual activities of human prolidase
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20
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Homo sapiens
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Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris
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63
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2007
Loligo vulgaris
brenda
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Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism
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Loligo vulgaris (Q7SIG4)
brenda
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Loligo vulgaris
brenda
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106
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2009
Loligo vulgaris (Q7SIG4)
brenda
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66
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Loligo vulgaris (Q7SIG4)
brenda
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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
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Loligo vulgaris
brenda
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A strategy for the production of soluble human senescence marker protein-30 in Escherichia coli
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393
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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
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187
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2010
Loligo vulgaris (Q7SIG4)
brenda
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Loligo vulgaris (Q7SIG4)
brenda
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Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase
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49
547-559
2010
Alteromonas sp. (Q44238), Alteromonas sp. JD6.5 (Q44238)
brenda
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Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase)
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66
1131-1138
2010
Loligo vulgaris
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Hydrolysis of organophosphorus compounds by microbial enzymes
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89
35-43
2011
Alteromonas sp., Alteromonas sp. JD6.5, Brevundimonas diminuta, Flavobacterium sp., Pseudoalteromonas haloplanktis, Pseudoalteromonas undina
brenda
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Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots
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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.
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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
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118
4479-4489
2014
Loligo vulgaris (Q7SIG4)
brenda