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Enzyme Nomenclature
Information on EC 3.1.8.2 - diisopropyl-fluorophosphatase
for references in articles please use BRENDA:EC3.1.8.2
Word Map on EC 3.1.8.2
- 3.1.8.2
- dfpase
-
organophosphorus
- dfp
- degradation
- squid
- sarin
-
loligo
- diisopropylfluorophosphate
- phosphotriesterases
- paraoxon
- environmental protection
-
opaas
- vx
- methylphosphonofluoridate
-
bioscavenger
-
polyurethane
- cyclosarin
-
bioplastics
-
warfare
- prolidase
- alteromonas
-
water-filled
- analysis
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.1.8.2
-
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RECOMMENDED NAME
GeneOntology No.
diisopropyl-fluorophosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
enzyme exhibits stereoselectivity toward the chiral phosphorus center of the p-nitrophenyl analogs of sarin and soman
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
catalytic mechanism, H287 is required for catalytic activity
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
the enzyme exhibits stereoselectivity toward the hydrolysis of chiral substrates with a preference for the S-P enantiomers
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
squide-type enzyme: diisopropyl fluorophosphate hydrolysed more rapidly than soman, Mazur-type enzyme: soman hydrolysed more rapidly than diisopropyl fluorophosphate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
calcium coordinating residue D229, in concert with direct substrate activation by the metal ion, renders the phosphorus atom of the substrate susceptible for attack of water, through generation of a phosphoenzyme intermediate
-
diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
diisopropyl-fluorophosphate fluorohydrolase
Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase.
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CAS REGISTRY NUMBER
COMMENTARY
9032-18-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme exhibiting additionally prolidase activity, E.C. 3.4.13.9
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
diisopropyl fluorophosphatase is a calcium-dependent phosphotriesterase that acts on a variety of highly toxic organophosphorus compounds, that act as inhibitors of acetylcholinesterase
additional information
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
-
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
-
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; 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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2,2-trimethylpropyl methylphosphonofluoridoate + H2O
1,2,2-trimethylpropyl methylphosphonate + fluoride + H+
-
-
-
-
?
1-methylethyl methylphosphonofluoridoate + H2O
1-methylethyl methylphosphonate + fluoride + H+
-
-
-
-
?
4-nitrophenylisopropyl phenylphosphinate + H2O
?
-
at 22% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
4-nitrophenylpropyl phenylphosphinate + H2O
?
-
at 24% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
cyclohexyl methylphosphonofluoridoate + H2O
cyclohexyl methylphosphonate + fluoride + H+
-
-
-
-
-
ethyl dimethylamidocyanophosphate + H2O
ethyl hydrogen dimethylphosphoramidate + HCN
-
-
-
-
?
ethyl N,N-dimethylphosphoramidocyanidate + H2O
ethyl N,N-dimethylphosphoramide + cyanide
-
i.e. tabun
-
-
?
mipafox + H2O
?
-
i.e. N,N'-diisopropyl phosphorodiamidofluoridate, poor substrate
-
-
?
O-ethyl S-(2-diisopropylamino)ethyl methylphosphonothioate + H2O
?
-
an organophosphorous nerve agent
-
-
?
(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-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
-
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
-
-
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. O,O-diisopropyl phosphorofluoridate
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
i.e. DFP
-
-
?
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
?
-
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
?
-
i.e. diethyl-4-nitrophenyl phosphate, poor substrate
-
-
?
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
pH 8.0, 25°C, 1 mM MgCl2
-
-
?
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
?
-
at 38% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
sarin + H2O
?
-
at 10% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
soman + H2O
?
-
at 240% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
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
?
-
-
-
-
?
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
?
-
i.e. N,N-dimethylethylphosphoramidocyanidate, at 124% the rate of diisopropyl fluorophosphate hydrolysis
-
-
?
additional information
?
-
-
not: 4-nitrophenylphosphonate, 4-nitrophenylphosphinorylcholine
-
-
-
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: 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
?
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diisopropyl fluorophosphate + H2O
diisopropyl phosphate + fluoride
-
-
-
-
?
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
Q03336
SMP30 is important in diisopropyl phosphofluoridate detoxification
-
-
?
additional information
?
-
-
the natural substrates for enzyme are unknown, enzyme may, in nature, be used in peptide metabolism
-
-
-
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
?
-
-
the natural substrates for enzyme are unknown
-
-
-
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
?
-
-
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
?
-
Q03336
enzyme expression in liver decreases androgen-independently of aging
-
-
-
additional information
?
-
-
the natural substrates for enzyme are unknown
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
Mg2+
fully activates the hydrolysis of diisopropyl phosphofluoridate
Mn2+
Ni2+
Zn2+
additional information
Cd2+
slightly activates the hydrolysis of diisopropyl phosphofluoridate
Co2+
fully activates the hydrolysis of diisopropyl phosphofluoridate
Mn2+
the active site harbors the binuclear Mn2+ ions, three glycolate oxygens of the enzyme coordinate the two Mn2+ atoms. All the oxygens of the carboxylate side chains coordinate the Mn2+ ions in the more favorable syn configuration, binding structure analysis, detailed overview
Mn2+
fully activates the hydrolysis of diisopropyl phosphofluoridate
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
additional information
-
activity is driven by a binuclear metal center in the C-terminal region
additional information
no effect by Ca2+ on SMP30, the enzyme does not bind to Ca2+ at all
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N,N'-diisopropyldiamidofluorophosphate
i.e. mipafox or DDFP. the inhibitor's hydrolysis product, N,N'-diisopropyldiamidophosphate, is present in the cocrystal structure and bound by coordinating the binuclear metals and forming hydrogen bonds and nonpolar interactions with active site residues. An unusual common feature of the binding of the two ligands is the involvement of only one oxygen atom of the glycolate carboxylate and the product DDP tetrahedral phosphate in bridging the two Mn2+ ions, binding structure analysis, detailed overview
O,O-dicyclopentylphosphoroamidate
-
crystallization data, phosphoryl oxygen of inhibitor is directly coordinated to the catalytic calcium ion
EGTA
-
only slightly by Fe3+ or Ni2+, not by Cs2+, Cu2+, Mg2+, Ca2+ or Zn2+; reversible by Mn2+ or Co2+
EGTA
-
Mn2+ reverses and stimulates over pre-EGTA-treatment activity level, Co2+ partially restores; reversible by Mn2+ or Co2+; strong
Mipafox
-
i.e. N,N'-diisopropyl phosphorodiamidofluoridate, DFPase-1, DFPase-2 and DFPase-3; reversible
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
an approach using recombinant enzyme encapsulated within sterically stabilized liposomes to enhance diisopropyl fluorophosphates degradation
-
CdCl2
1 mM, stimulates hydrolysis to a lesser extent, 38% activity, compared to MgCl2
CoCl2
1 mM, stimulates hydrolysis well, 102% activity, compared to MgCl2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.46
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
0.24
parathion
-
pH not specified in the publication, temperature not specified in the publication
0.048
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
2.72
diisopropyl fluorophosphate
-
wild-type, pH 7.5, 25°C, in nitrogen atmosphere
2.99
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
230
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
465
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
77
diisopropyl fluorophosphate
-
pH not specified in the publication, temperature not specified in the publication
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.125
O,O-dicyclopentylphosphoroamidate
-
wild-type, pH 7.5, 25°C, in nitrogen atmosphere
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.527
purified SMP30, substrate phenyl acetate; with phenyl acetate as substrate, pH 8.0, 25°C, 1 mM MgCl2
0.998
with diisopropyl phosphorofluoridate as substrate, pH 8.0, 25°C, 1 mM MgCl2
1.512
purified enzyme; purified SMP30, substrate diisopropyl phosphofluoridate
2.4
-
O-cyclohexyl methylphosphonofluoridate (-)isomer as substrate, pH 7.2, 1 mM MnCl2
2.7
-
O-cyclohexyl methylphosphonofluoridate (-)isomer as substrate, pH 7.2, 1 mM MnCl2
29.2
-
O-cyclohexyl methylphosphonofluoridate (+)isomer as substrate, pH 7.2, 1 mM MnCl2
65.3
-
O-cyclohexyl methylphosphonofluoridate (+)isomer as substrate, pH 7.2, 1 mM MnCl2
198
-
substrate cyclosarin, pH 8.0, temperature not specified in the publication
225
-
substrate diisopropyl fluorophosphate, pH 8.0, temperature not specified in the publication
additional information
-
pH dependence of the specific activity of the mutant H287N
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
the effect of pH 6.0-9.0 on kinetic constants kcat and KM is studied, KM shows no perceivable dependence on pH within this pH range, kcat increases with pH to a limiting value at pH 8.0
7.6 - 9
-
about half-maximal activity at pH 7.6 and about 60% of maximal activity at pH 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000 - 30000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
34000
35000
45000 - 50000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
58000
x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain
70000 - 100000
-
three enzyme types of different MW: 20000-30000, 45000-50000 and 70000-100000
35000
-
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 35000, OPH from displays the TIM barrel fold in the active site loaded with Zn2+, overview
monomer
tetramer
?
x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain
?
-
x * 58000, the enzyme OPAA structure is composed of two domains, a small N-terminal domain or N-domain, residue 1 to 160, and a large C-terminal domain or C-domain
-
tetramer
-
active enzyme, OPAA/prolidase from Alteromonas sp. JD6.5 displays the pita bread fold in the C-terminal region which houses the active metal site loaded with Mn2+, overview
tetramer
-
active enzyme, OPAA/prolidase from Alteromonas sp. JD6.5 displays the pita bread fold in the C-terminal region which houses the active metal site loaded with Mn2+, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified OPAA, in acetate buffer equilibrated in a reservoir solution containing a much greater concentration of acetate, 270 mM ammonium acetate and 60 mM sodium acetate, pH 4.6, X-ray structure determination and analysis at 2.7 A resolution for the enzyme with bound inhibitor N,N'-diisopropyldiamidophosphate, and at 2.3 A resolution for the native enzyme
at 2.2 A resolution, after exchange of available H atoms by using D2O. Collection of time-of-flight wavelength-resolved Laue images
-
by vapour diffusion using a protein solution with 2 mM protein in 10 mM Tris, pH 7.5, 2 mM CaCl2, against a precipitation solution containing 11% PEG 4000 in 0.1 M MES, pH 6.5, at room temperature, X-ray diffraction structure determination and analysis at 2.2 A resolution. Comparison with structures of enzyme mutants, overview
-
homology modeling and docking of substrates. The two identical hydrophobic isopropyl groups in diisopropyl fluorophosphate bind to two different sub-pockets in the binding-site. Sub-pocket 1 is formed by residues P36, E37, I72, A74 and M90 while sub-pocket 2 is formed by F173, N175, T195, and W244
-
hydrodynamic model calculations based on the DFPase crystal structure from the native state enzyme structure in solution by use of different scattering methods, i.e. small-angle neutron scattering, overview
-
in complex with inhibitor O,O-dicyclopentylphosphoroamidate. Phosphoryl oxygen of inhibitor is directly coordinated to the catalytic calcium ion
-
mutant enzymes are crystallized at room temperature by hanging drop vapor diffusion method, using 0.1 M Tris buffer pH 8.5, 2% tacsimate, 16% (w/v) PEG 3350 for mutant E37A/Y144A/R146A/T195M or 0.2 M KCl, 0.05 M HEPES buffer pH 7.5, 35% (w/v) pentaerythriol propoxylate for mutant E37D/Y144A/R16A/T195M
-
mutant enzymes N120D/N175D/D229N, E21QN120D/N175D/D229N, and D121E are crystallized by hanging drop vapor diffusion method, using 0.1 M MES buffer pH 6.5, 14-20% (w/v) PEG 3350
-
quantum mechanical/molecular mechanical umbrella sampling simulations. 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. The calculated free energy barrier for hydrolysis of (S)-sarin by the same mechanism 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
-
structural characterization of a squid-type enzyme, the overall structure of this protein represents a six-fold beta propeller with two calcium ions bound in a central water-filled tunnel
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT enhances stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
37°C, liposomes encapsulating enzyme incubated in blood, stable over 2 days
-
5°C, anchored to a photoluminescent porous silicon platform, bis-trispropane buffer and glycerol (1:1), no loss of activity for at least 6 months
-
frozen, less than 35% loss of activity within 6 months with repeated freeze-thawing cycles
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; SMP30 49fold from liver by anion exchange and hydrophobic interaction chromatography, and gel filtration
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the coexpression of recombinant human SMP30 with GroES/GroEL/Tf at 15°C, combined with the addition of a membrane fluidizer, increases osmolytes, and a two-step expression results in the highest enhancement of solubility and DFPase activity
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
D229N/N120D
D229N/N175D
-
catalytically inactive, no change in the calcium coordinating environment
E21Q/N120D/N175D/D229N
-
the mutations lead to a loss of calcium binding and enzymatic activity
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
H181N
H274N
H287N
N120D/N175D/D229N
-
the mutations lead to a loss of calcium binding and enzymatic activity
additional information
D229N/N120D
-
catalytically inactive, no change in the calcium coordinating environment
H274N
-
slight loss of activity in comparison to wild-type enzyme using pH Stat measurements, no alteration is observed with fluoride assay
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
degradation
environmental protection
medicine
additional information
analysis
-
biosensors using immobilized recombinant Escherichia coli cells expressing OPH are being employed for identifying OP nerve agents
analysis
-
biosensors using immobilized recombinant Escherichia coli cells expressing OPH are being employed for identifying OP nerve agents
degradation
-
enzyme is capable of detoxifying chemical warfare agents by hydrolysis
degradation
-
enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents; enzyme is capable of detoxifying chemical warfare agents by hydrolysis
degradation
-
enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents
degradation
-
approach to the use of enzyme encapsulated within liposomes, to protect against and treat chemical poisoning; enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents
environmental protection
-
detoxification of nerve agent exposed environments
environmental protection
-
to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach
environmental protection
-
to detoxify nerve agent exposed environments, a decontamination solution known as DS2 is being used in conjunction with bleach
environmental protection
-
detoxification of nerve agent exposed environments
environmental protection
-
detoxification of nerve agent exposed environments
environmental protection
-
detoxification of nerve agent exposed environments
-
medicine
-
OPH is also being used in medical applications as an antidote or a therapeutic in preventing organophosphorous poisoning
medicine
-
OPH is also being used in medical applications as an antidote or a therapeutic in preventing organophosphorous poisoning
additional information
-
the enzyme protects the liver from toxic effects of the substrate diisopropyl phosphorofluoridate
additional information
the enzyme protects the liver from toxic effects of the substrate diisopropyl phosphorofluoridate
additional information
-
the OPH enzyme is incorporated successfully into fire-fighting foams for large-scale response cleanup studies of contaminated areas
additional information
-
the OPH enzyme is incorporated successfully into fire-fighting foams for large-scale response cleanup studies of contaminated areas
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LINKS TO OTHER DATABASES (specific for EC-Number 3.1.8.2)
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