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Synonyms
pon-1, serum paraoxonase, phosphotriesterase, organophosphorus hydrolase, dfpase, serum paraoxonase 1, pon 1, methyl parathion hydrolase, organophosphate hydrolase, hupon1,
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1-methylethyl 4-nitrophenyl (1-methylpropyl)phosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen (1-methylpropyl)phosphonate
6.8% relative specific activity compared to methyl 1-methylethyl 4-nitrophenyl phosphate
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1-methylethyl 4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + 1-methylethyl hydrogen methylphosphonate
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
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
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
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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
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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
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
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wild-type, 50% of the activity with propyl 4-nitrophenyl methylphosphonate
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coumaphos + H2O
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diethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + diethyl hydrogen phosphate
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
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
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
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
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
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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
100% activity
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methyl 4-nitrophenyl methylphosphonate + H2O
methyl hydrogen methylphosphonate + 4-nitrophenol
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wild-type, 733% of the activity with propyl 4-nitrophenyl methylphosphonate
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methyl parathion + H2O
dimethyl thiophosphate + 4-nitrophenol
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O,O-diisopropyl-4-nitrophenyl phosphate + H2O
dipropan-2-yl hydrogen phosphate + 4-nitrophenol
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O-methyl O-(4-nitrophenyl) methylphosphonothioate + H2O
O-methyl-methylphosphonothionic acid + 4-nitrophenol
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paraoxon + H2O
diethylphosphate + 4-nitrophenol
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parathion + H2O
diethylthiophosphate + 4-nitrophenol
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propyl 4-nitrophenyl methylphosphonate + H2O
propyl hydrogen methylphosphonate + 4-nitrophenol
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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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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
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
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
R153A
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prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153A
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
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prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153L/R370L
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
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hydrolyses the (S)-enantiomer of O-methoxy-p-nitrophenyl methylphosphonate significantly faster than the (R)-isomer. Prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R153W/R370L
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
R370L
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prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
R370L
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
W88L
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prefers the formation of (S)-O-methyl-methylphosphonothionic acid over the (R)-enantiomer
W88L
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
additional information
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enzyme variants with improved degradation of methyl parathion by DNA shuffling
additional information
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construction of diverse mutant variants by saturation mutagenesis, e.g. mutant 22A11, sequencing of randomly chosen mutants, the mutants show increased activity and altered kinetics compared to the wild-type enzyme, overview
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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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda