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Information on EC 3.1.8.1 - aryldialkylphosphatase

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.8 Phosphoric-triester hydrolases
                3.1.8.1 aryldialkylphosphatase
IUBMB Comments
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
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UNIPROT: Q93LD7
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
pon-1, serum paraoxonase, phosphotriesterase, organophosphorus hydrolase, dfpase, serum paraoxonase 1, pon 1, methyl parathion hydrolase, organophosphate hydrolase, hupon1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bacterial phosphotriesterase
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A-esterase
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-
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aryltriphosphatase
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esterase B1
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esterase E4
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esterase, organophosphate
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esterase, paraoxon
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-
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esterase, pirimiphos-methyloxon
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-
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HuPON1
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-
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OPA anhydrase
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-
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OPH
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-
-
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organophosphate hydrolase
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-
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organophosphorus acid anhydrase
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-
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organophosphorus hydrolase
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paraoxon hydrolase
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-
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paraoxonase
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phosphotriesterase
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pirimiphos-methyloxon esterase
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-
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PTE
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
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-
-
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SYSTEMATIC NAME
IUBMB Comments
aryltriphosphate dialkylphosphohydrolase
Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.
CAS REGISTRY NUMBER
COMMENTARY hide
117698-12-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dichlorvos + H2O
2,2-dichloroethenol + dimethyl hydrogen phosphate
show the reaction diagram
-
-
-
?
dimethoate + H2O
?
show the reaction diagram
-
-
-
?
methyl chlorpyrifos oxon + H2O
?
show the reaction diagram
-
-
-
?
methyl chlorpyrifos thion + H2O
?
show the reaction diagram
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
show the reaction diagram
-
-
-
?
methyl parathion + H2O
4-nitrophenol + dimethyl thiophosphate
show the reaction diagram
-
-
-
?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
show the reaction diagram
methyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
trimethyl phosphate + H2O
?
show the reaction diagram
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-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dichlorvos + H2O
2,2-dichloroethenol + dimethyl hydrogen phosphate
show the reaction diagram
-
-
-
?
methyl-parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
paraoxon + H2O
diethyl phosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
parathion + H2O
diethyl thiophosphate + 4-nitrophenol
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
activates the enzyme, the enzyme is a natively heterobinuclear iron-zinc metalloprotein, overview, Fe2+ is essential, but can be replaced by Co2+ in supplemented medium for growth of Escherichia coli cells recombinantly expressing the enzyme, Co2+ addition leads to higher activity compared to Fe2+
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 0.41
methyl parathion
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
dichlorvos
pH 8.0, 37°C, enzyme administered in monkeys in vivo
1.1
parathion
pH 8.0, 25°C, enzyme administered in rats in vivo
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
168
recombinant enzyme in presence of Co2+
34
recombinant enzyme in absence of Co2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evaluation of protective effect of the enzyme in plasma of rats against in vitro challenge of intoxication with parathion or paraoxon in rats, effectiveness of the enzyme as bioscavenger in vivo, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q93LD7_RHIRD
384
0
41363
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with Co2+, hanging drop vapour diffusion method, 0.005 ml of protein solution containing 6.4 mg/ml protein in 50 mM Hepes, pH 7.0, 150 mM NaCl, and 1 mM CoCl2, are mixed with 0.005 ml of reservoir solution that consists of 20% w/v PEG 3350 and 0.2 M sodium nitrate, X-ray diffraction structure determination and analysis at 1.9 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant OpdA from Escherichia coli strain DH5alpha by anion exchange chromatography, dialysis, sulphopropyl affinity chromatography, and again dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene opdA, expression in Escherichia coli strain DH5alpha, growth in media supplemented with different divalent metal ions, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
the enzyme is used for the detoxification of organophosphate pesticides and realted chemical warfare agents such as VX and sarin
environmental protection
the enzyme is used for the detoxification of organophosphate pesticides and related chemical warfare agents such as VX and sarin
medicine
use of organophosphorus hydrolase OpdA prevents lethality in an African green monkey model of acute organophosphrus poisoning. Treated monkeys received 1.2 mg/kg OpdA iv immediately after poisoning with dichlorvos. In Opda-treated animals, heart andrespiratory rates are unchanged from baseline over a 240-minute observation period. AChE activityslowly declines, but remains above 25% of baseline for the entire duration. Dichlorvos concentrationsreach a mean peak of 0.19 microg/ml at 40 min after poisoning and decrease to a mean of 0.05 microg/ml at 240 min
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackson, C.J.; Liu, J.W.; Coote, M.L.; Ollis, D.L.
The effects of substrate orientation on the mechanism of a phosphotriesterase
Org. Biomol. Chem.
3
4343-4350
2005
Agrobacterium tumefaciens (Q93LD7)
Manually annotated by BRENDA team
Jackson, C.J.; Carr, P.D.; Kim, H.K.; Liu, J.W.; Herrald, P.; Mitic, N.; Schenk, G.; Smith, C.A.; Ollis, D.L.
Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site
Biochem. J.
397
501-508
2006
Agrobacterium tumefaciens (Q93LD7), Agrobacterium tumefaciens
Manually annotated by BRENDA team
Jackson, C.J.; Foo, J.L.; Kim, H.K.; Carr, P.D.; Liu, J.W.; Salem, G.; Ollis, D.L.
In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase
J. Mol. Biol.
375
1189-1196
2008
Agrobacterium tumefaciens (Q93LD7), Agrobacterium tumefaciens
Manually annotated by BRENDA team
Jackson, C.J.; Carville, A.; Ward, J.; Mansfield, K.; Ollis, D.L.; Khurana, T.; Bird, S.B.
Use of OpdA, an organophosphorus (OP) hydrolase, prevents lethality in an African green monkey model of acute OP poisoning
Toxicology
317
1-5
2014
Agrobacterium tumefaciens (Q93LD7), Agrobacterium tumefaciens
Manually annotated by BRENDA team
Ashani, Y.; Leader, H.; Aggarwal, N.; Silman, I.; Worek, F.; Sussman, J.L.; Goldsmith, M.
Invitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for invivo protection against organophosphate intoxications
Chem. Biol. Interact.
259
252-256
2016
Pseudomonas sp., Brevundimonas diminuta (P0A434), Homo sapiens (P27169), Agrobacterium tumefaciens (Q93LD7)
Manually annotated by BRENDA team