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Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Escherichia coli and UniProt Accession P37669

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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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This record set is specific for:
Escherichia coli
UNIPROT: P37669
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected 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
A-esterase
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-
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aminopeptidase P
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aryltriphosphatase
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esterase B1
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esterase E4
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-
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esterase, organophosphate
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esterase, paraoxon
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esterase, pirimiphos-methyloxon
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HuPON1
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OPA anhydrase
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-
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organophosphate hydrolase
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organophosphorus acid anhydrase
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organophosphorus hydrolase
paraoxon hydrolase
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paraoxonase
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phosphotriesterase
pirimiphos-methyloxon esterase
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PTE
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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
catalytic reaction with orpanophosphonates starts with cleavageof the P-O bond. Reaction proceeds through a displacement mechanism and generates a chiral product in situ with an inversion of stereochemical configuration at the phosphorous atom
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
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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
1-methylethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen (1-methylpropyl)phosphonate
show the reaction diagram
6.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
-
-
?
1-methylethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen methylphosphonate
show the reaction diagram
33.1% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
1-methylpropyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylpropyl hydrogen methylphosphonate
show the reaction diagram
29.5% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
4-nitrophenyl phenyl methylphosphonate + H2O
4-nitrophenol + phenyl hydrogen methylphosphonate
show the reaction diagram
45.2% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
4-nitrophenyl phenyl methylphosphonate + H2O
phenyl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
-
wild-type, 78% of the activity with propyl 4-nitrophenyl methylphosphonate
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-
?
4-nitrophenyl propan-2-yl methylphosphonate + H2O
propan-2-yl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
-
wild-type, 57% of the activity with propyl 4-nitrophenyl methylphosphonate
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-
?
4-nitrophenyl propyl methylphosphonate + H2O
4-nitrophenol + propyl hydrogen methylphosphonate
show the reaction diagram
58.5% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
butan-2-yl 4-nitrophenyl methylphosphonate + H2O
butan-2-yl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
-
wild-type, 50% of the activity with propyl 4-nitrophenyl methylphosphonate
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-
?
coumaphos + H2O
?
show the reaction diagram
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-
-
-
?
diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
show the reaction diagram
15.1% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
dimethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + dimethyl hydrogen phosphate
show the reaction diagram
13.3% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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?
ethyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl 1-methylethyl hydrogen phosphate
show the reaction diagram
18.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
ethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + ethyl hydrogen (1-methylpropyl)phosphonate
show the reaction diagram
14.7% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
ethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + ethyl hydrogen methylphosphonate
show the reaction diagram
29.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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-
?
ethyl 4-nitrophenyl methylphosphonate + H2O
ethyl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
-
wild-type, 50% of the activity with propyl 4-nitrophenyl methylphosphonate
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?
methyl 1-methylethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + methyl 1-methylethyl hydrogen phosphate
show the reaction diagram
100% activity
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-
?
methyl 4-nitrophenyl methylphosphonate + H2O
methyl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
-
wild-type, 733% of the activity with propyl 4-nitrophenyl methylphosphonate
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?
methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
show the reaction diagram
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?
O,O-diisopropyl-4-nitrophenyl phosphate + H2O
dipropan-2-yl hydrogen phosphate + 4-nitrophenol
show the reaction diagram
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?
O-methyl O-(4-nitrophenyl) methylphosphonothioate + H2O
O-methyl-methylphosphonothionic acid + 4-nitrophenol
show the reaction diagram
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?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
show the reaction diagram
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-
?
parathion + H2O
diethylthiophosphate + 4-nitrophenol
show the reaction diagram
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?
propyl 4-nitrophenyl methylphosphonate + H2O
propyl hydrogen methylphosphonate + 4-nitrophenol
show the reaction diagram
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?
additional information
?
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the enzyme does not hydrolyse 4-nitrophenyl phenyl ethylphosphonate and 1-methylpropyl 4-nitrophenyl ethylphosphonate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
Mn2+
activates
additional information
-
contains a binuclear metal center with two metals interactively involved in catalysis and/or structural functions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.22
methylparathion
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pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
0.12
paraoxon
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pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
additional information
additional information
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kinetics for diverse random mutant variants, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2300
methylparathion
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pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
11700
paraoxon
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pH 8.0, 37°C, recombinant His6-tagged wild-type OPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A14T/A80V/K185R/H257Y/I274N
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random saturation mutagenesis, variant 2H2, increased activity and altered kinetics compared to the wild-type enzyme
A80V/I274N/K185R
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site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
A80V/S365P
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random saturation mutagenesis, variant 2H2, increased activity and altered kinetics compared to the wild-type enzyme
H257Y
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random saturation mutagenesis, variant 6D4, increased activity and altered kinetics compared to the wild-type enzyme
I274N
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random saturation mutagenesis, variant 5A6, increased activity and altered kinetics compared to the wild-type enzyme
I274N/K185R
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site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
K185E
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site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
K185R
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site-directed mutagenesis, increased activity and altered kinetics compared to the wild-type enzyme
L182S/V310A
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random saturation mutagenesis, variant 2F6, increased activity and altered kinetics compared to the wild-type enzyme
R153A
R153L
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R153L/R370L
R153W
the mutant shows an increase of activity towards methyl 1-methylethyl 4-nitrophenyl phosphate and methyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme, the mutant shows a decrease of activity towards ethyl 4-nitrophenyl ethylphosphonate, 4-nitrophenyl propyl ethylphosphonate, and 1-methylethyl 4-nitrophenyl ethylphosphonate compared to the wild type enzyme
R153W/R370L
R370L
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene opd, expression of His-tagged wild-type and mutant enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lai, K.; Dave, K.I.; Wild, J.R.
Bimetallic binding motifs in organophosphorus hydrolase are important for catalysis and structural organization
J. Biol. Chem.
269
16579-16584
1994
Escherichia coli
Manually annotated by BRENDA team
Cho, C.M.H.; Mulchandani, A.; Chen, W.
Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents
Appl. Environ. Microbiol.
68
2026-2030
2002
Escherichia coli
Manually annotated by BRENDA team
Cho, C.M.H.; Mulchandani, A.; Chen, W.
Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides
Protein Eng. Des. Sel.
19
99-105
2006
Escherichia coli, Escherichia coli K-12, Escherichia coli K-12 XL1-Blue
Manually annotated by BRENDA team
Huang, L.F.; Su, B.; Jao, S.C.; Liu, K.T.; Li, W.S.
Aminopeptidase P mediated detoxification of organophosphonate analogues of sarin: mechanistic and stereochemical study at the phosphorus atom of the substrate
Chembiochem
7
506-514
2006
Escherichia coli
Manually annotated by BRENDA team
Hsu, Y.T.; Su, C.Y.; Du, H.C.; Jao, S.C.; Li, W.S.
Evaluation of organophosphorus chemicals-degrading enzymes: a comparison of Escherichia coli and human cytosolic aminopeptidase P
Chem. Biodivers.
5
1401-1411
2008
Escherichia coli (P15034), Homo sapiens (Q9NQW7)
Manually annotated by BRENDA team