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Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Oryctolagus cuniculus and UniProt Accession Q9BGN0
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3.1.8.1 aryldialkylphosphataseIUBMB 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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Word Map
- 3.1.8.1
- arylesterase
- paraoxonase-1
- cholesterol
- nerve
- atherosclerosis
- cardiovascular
-
low-density
-
insecticide
- triglyceride
- coronary
-
apolipoproteins
- acetylcholinesterase
- malondialdehyde
- diminuta
-
poison
- soman
- p-nitrophenol
-
warfare
- sarin
-
bioremediation
- chlorpyrifos
- vx
-
antiatherogenic
-
decontamination
-
bioscavenger
- atherogenesis
- cholinesterase
- phenylacetate
- medicine
-
binuclear
-
phosphotriesters
-
atherogenic
- flavobacterium
- carboxylesterase
-
hdl-cholesterol
- apoa-i
- butyrylcholinesterase
- fluorophosphate
-
surface-expressed
- diazoxon
- tabun
-
thiolactone
-
g-type
-
salt-stimulated
-
triesters
- malathion
- ochrobactrum
- sphingobium
- radiobacter
- cyclosarin
-
loligo
- synthesis
- environmental protection
- drug development
- degradation
- biotechnology
- diagnostics
- agriculture
- analysis
- nutrition
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-esterase
-
-
-
-
aryltriphosphatase
-
-
-
-
esterase B1
-
-
-
-
esterase E4
-
-
-
-
esterase, organophosphate
-
-
-
-
esterase, paraoxon
-
-
-
-
esterase, pirimiphos-methyloxon
-
-
-
-
HuPON1
-
-
-
-
OPA anhydrase
-
-
-
-
OPH
-
-
-
-
organophosphate hydrolase
-
-
-
-
organophosphorus acid anhydrase
-
-
-
-
organophosphorus hydrolase
-
-
-
-
paraoxon hydrolase
-
-
-
-
paraoxonase
-
-
-
-
phosphotriesterase
-
-
-
-
pirimiphos-methyloxon esterase
-
-
-
-
PTE
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
catalytic reaction mechanism involving residue Asp269, and role of Asp270 for the catalytic function, molecular dynamics and modelling, overview. The reaction is supposed to proceed by a two-step addition-elimination (An + Dn) mechanism, which goes through a common pentavalent intermediate observed in phosphoryl transfer reactions. The first step is the activation of H2O by Asp269 and Glu53 to form a nucleophile hydroxide and a metastable pentavalent complex. Both the residues Asn168 and Asn224 help the leaving group leave through hydrogen bonds
an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol
reaction mechanism of lactonase activity and paraoxonase activity of the enzyme PON1, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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
117698-12-1
-
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
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
tabun + H2O
?
-
efficient hydrolysis of tabun (100 nM) is observed with about 0.025-0.04 units of paraoxonase 1. Tabun hydrolysis with paraoxonase 1 is about 30-60times and about 200-260times more efficient than that with sarin and soman, respectively
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
both docking and molecular dynamics simulations suggest that the only way paraoxon can be accommodated in the PON1 active site is by pushing Y71 out of the active site, causing the active site loop to take on a partially open conformation
-
-
?
diisopropyl fluorophosphate + H2O
?
-
high concentration of purified rabbit serum paraoxonase 1 (about 0.025 mg) is required to hydrolyze 0.002 mM diisopropyl fluorophosphates
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
0.2% of the activity with phenyl acetate
-
-
?
sarin + H2O
?
-
efficient hydrolysis of sarin (11 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
soman + H2O
?
-
efficient hydrolysis of soman (3 nM) is observed with about 0.08-0.25 units of paraoxonase 1
-
-
?
additional information
?
-
molecular docking of substrates to wild-type and mutant enzymes using the crystal structure of PON1 (PDB ID 3SRG with resolution 2.19 A), overview. The enzyme also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate
-
-
?
additional information
?
-
th enzyme is also active with the chromogenic lactone thiobutyl-gamma-butyric lactone (TBBL), cf. EC 3.1.1.81. It has both lactonase activity and paraoxonase activity. Empirical valence bond simulations of PON1-catalyzed hydrolyses of paraoxon and TBBL, overview
-
-
?
additional information
?
-
the mammalian serum paraoxonase 1 (PON1) is a calcium-dependent serum esterase which catalyzes the hydrolysis of a broad range of organic esters and organophosphorous (OP) compounds. PON1 is a lactonase with native substrates gamma- and delta-lactones which have long alkyl side chains, and PON1 possesses promiscuous OP hydrolase activity, particularly on paraoxon, which is attributed to its considerable plasticity of catalytic structure
-
-
?
additional information
?
-
the mammalian serum paraoxonase 1 (PON1) is a calcium-dependent serum esterase which catalyzes the hydrolysis of a broad range of organic esters and organophosphorous (OP) compounds. PON1 is a lactonase with native substrates gamma- and delta-lactones which have long alkyl side chains, and PON1 possesses promiscuous OP hydrolase activity, particularly on paraoxon, which is attributed to its considerable plasticity of catalytic structure
-
-
?
NATURAL SUBSTRATE
NATURAL 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
diethyl-paraoxon + H2O
diethyl phosphate + 4-nitrophenol
-
-
-
?
dimethyl-paraoxon + H2O
dimethyl phosphate + 4-nitrophenol
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
Ca2+
-
two calcium binding sites, the higher affinity site being essential for hydrolytic activity and its removal is irreversible, the lower affinity site being responsible for catalytic activity with reversible binding of Ca2+
Ca2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
Ca2+
dependent on, PON1 has a six-blade beta-propeller fold with two calcium ions in its central tunnel. The structural Ca2+ is completely embedded inside the protein, and the catalytic Ca2+ is located at the bottom of the active site cavity. PTE Ca2+ binding structure comparisons
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-hydroxyquinoline
-
specific paraoxonase 1 inhibitor, dose-dependent inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HDL
modulation of substrate selectivity and catalytic stimulation by HDL
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.889
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.2
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
diethyl paraoxon
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.192
diethyl-paraoxon
pH 10.5, 25°C, recombinant mutant I74F/H115W/T332S
0.214
diethyl-paraoxon
pH 10.5, 25°C, recombinant mutant H115W/T332S
0.404
diethyl-paraoxon
pH 10.5, 25°C, recombinant mutant I74F/H115W
1.54
diethyl-paraoxon
pH 10.5, 25°C, recombinant mutant I74F/T332S
4.49
diethyl-paraoxon
pH 10.5, 25°C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
the impact of Y71 mutational substitutions on PON1's lactonase activity is minimal, whereas the kcat for the paraoxonase activity is negatively perturbed by up to 100fold, suggesting greater mutational robustness of the native activity. Additionally, while these substitutions modulate PON1's active site shape, volume, and loop flexibility, their largest effect is in altering the solvent accessibility of the active site by expanding the active site volume, allowing additional water molecules to enter. This effect is markedly more pronounced in the organophosphatase activity than the lactonase activity
physiological function
additional information
evolution
serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. Comparison of PON1 to other organophosphatases demonstrates that either a similar gating loop or a highly buried solvent excluding active site is a common feature of these enzymes
evolution
the phosphotriesterase activity development between PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, is investigated by using the hybrid density functional theory method B3LYP. Structure comparisons of evolutionarily related enzymes show that the mutation of Asn270 leads to the catalytic Ca2+ ion indirectly connecting the buried structural Ca2+ ion via hydrogen bonds in DFPase. It can reduce the plasticity of enzymatic structure, and possibly change the substrate preference from paraoxon (preferred substrate of PON1) to DFP (preferred substrate of DFPase), which implies an evolutionary transition from mono- to dinuclear catalytic centers, enzyme catalysis mechanism from an evolutionary perspective, overview
physiological function
-
paraoxonase 1 functions as an efficient catalytic bioscavenger against nerve agents
physiological function
serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. PON1 is a calcium-dependent hydrolytic enzyme that is found in all mammalian species. In vivo, this enzyme forms complexes with the membrane-like surface of high-density lipoprotein (HDL) and contributes to HDL's antioxidant properties. Modulation of substrate selectivity and catalytic stimulation by HDL
physiological function
the enzyme catalyzes the hydrolysis of organophosphorus (OP) compounds and enhances hydrolysis of various nerve agents. PON1's native function is likely to be a lactonase which hydrolyzes the lactones from the oxidized lipids
additional information
enzyme PON1 is a six-bladed beta-propeller with a flexible loop (residues 70-81) covering the active site. This loop contains a functionally critical Tyr at position 71, mutational analysis of the role of Y71 in PON1's lactonase and organophosphatase activities. The side chain of Y71 is highly mobile and has been shown to adopt various conformational substrates that have been suggested to differentially affect PON1's native and promiscuous functions. Residue Y71 does not play an active role in PON1's lactonase activity in general, and specifically not on the HDL-induced simulation. Molecular dynamics simulations of PON1, e.g. using crystal structure of RePON1 in complex with the inhibitor 2-hydroxyquinoline (2HQ) and obtained at pH 6.5 (PDB ID 3SRG). In the wild-type enzyme Y71 forms a hydrogen-bonding interaction with the side chain of D183, which is itself part of a hydrogen-bonding network that leads from N168 on the catalytic Ca2+ ion to the outer periphery of the protein. D183 is central to this hydrogen-bonding network, as in addition to the hydrogen bond it forms with the side chain of Y71, it also forms hydrogen-bonding interactions with the side chains of S166, N168, and H184, the backbone carbonyl group of S166, and an active site water molecule. Therefore, D183 acts as an anchor, keeping this hydrogen-bonding network together. Active site hydrophobicity and the role of the active site loop in determining substrate selectivity, active site structure, structure-function relationship, overview
additional information
the serum paraoxonase 1 (PON1) is a calcium-dependent beta-propeller protein. PON1 has a six-blade beta-propeller fold with two calcium ions in its central tunnel. The structural Ca2+ is completely embedded inside the protein, and the catalytic Ca2+ is located at the bottom of the active site cavity. PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, seem to employ similar catalytic mechanisms as phosphotriesterase, due to their structural similarities of active sites. The attacking nucleophile for phosphotriester hydrolysis is identified to be an activated water molecule, with the nucleophile attacking the phosphorus center. The E53Q and D269N mutants in PON1 both possess measurable lactonase and paraoxonase activity, and mutation studies combined with related molecular dynamics simulations suggest that the water activated by Glu53 and Asp269 is the most likely attacking nucleophile. Analysis of the rate-determining reaction step of the organophosphorus compound hydrolysis catalyzed both by DFPase and PON1. Structure-function relationship, overview. Active site structure of PON1 (PDB ID 3SRE) and substrate docking
additional information
the serum paraoxonase 1 (PON1) is a calcium-dependent beta-propeller protein. PON1 has a six-blade beta-propeller fold with two calcium ions in its central tunnel. The structural Ca2+ is completely embedded inside the protein, and the catalytic Ca2+ is located at the bottom of the active site cavity. PON1, EC 3.1.8.1, and DFPase, EC 3.1.8.2, seem to employ similar catalytic mechanisms as phosphotriesterase, due to their structural similarities of active sites. The attacking nucleophile for phosphotriester hydrolysis is identified to be an activated water molecule, with the nucleophile attacking the phosphorus center. The E53Q and D269N mutants in PON1 both possess measurable lactonase and paraoxonase activity, and mutation studies combined with related molecular dynamics simulations suggest that the water activated by Glu53 and Asp269 is the most likely attacking nucleophile. Analysis of the rate-determining reaction step of the organophosphorus compound hydrolysis catalyzed both by DFPase and PON1. Structure-function relationship, overview. Active site structure of PON1 (PDB ID 3SRE) and substrate docking
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PON3_RABIT
354
0
39507
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
rabbit serum contains two major species of PON monomers (42300 Da and 39800 Da), SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
enzyme PON1 is a six-bladed beta-propeller with a flexible loop (residues 70-81) covering the active site
?
-
x * 40000-45000, paraoxonase 1 is separated as three bands with an approximate molecular weight of 40000-45000 Da, SDS-PAGE
?
-
x * 40000-45000, rabbit serum purified paraoxonase 1 shows three bands in about 40000-45000 Da molecular weight regions, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
at least 2 N-linked sugar chains, contains sialic acid residues
additional information
-
the deduced rabbit amino acid sequence contains five potential N-glycosylation sites, whereas the human sequence predicts four possible N-glycosylation sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D269N
site-directed mutagenesis, the mutant possesses measurable lactonase and paraoxonase activity
D270X
site-directed mutagenesis, mutation of the residue stabilizes the PON1-paraoxon substrate binding reducing the leaving group elimination rate. Effects of Asn270 mutation on enzymatic structure, overview
E53Q
site-directed mutagenesis, the mutant possesses measurable lactonase and paraoxonase activity
H115W/T332S
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
H115W/T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
H115W/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74A
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
I74F
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W/T332S
site-directed mutagenesis, the mutant shows very highly increased activity with diethyl-paraoxon compared to wild-type
I74F/H115W/V346A
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
I74F/T332S
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74F/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
I74L
site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type
I74V
site-directed mutagenesis, the mutant shows slightly reduced activity with diethyl-paraoxon compared to wild-type
I74W
site-directed mutagenesis, the mutant shows unaltered activity with diethyl-paraoxon compared to wild-type
L69A
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
L69I
site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type
T332A
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
T332S
site-directed mutagenesis, the mutant shows highly increased activity with diethyl-paraoxon compared to wild-type
T332S/V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
V346A
site-directed mutagenesis, the mutant shows increased activity with diethyl-paraoxon compared to wild-type
V346L
Y71A
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71F
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71G
site-directed mutagenesis, the mutant shows reduced lactonase and paraoxonase activities compared to the wild-type enzyme, the mutant shows an increased active site volume compared to the wild-type
Y71M
site-directed mutagenesis, the mutant shows reduced lactonase and paraoxonase activities compared to the wild-type enzyme, the mutant shows an increased active site volume compared to the wild-type
Y71W
site-directed mutagenesis, the mutant shows an increased active site volume compared to the wild-type
Y71X
site-saturation library screening. The impact of Y71 mutational substitutions on PON1's lactonase activity is minimal, whereas the kcat for the paraoxonase activity is negatively perturbed by up to 100fold, suggesting greater mutational robustness of the native activity. Additionally, while these substitutions modulate PON1's active site shape, volume, and loop flexibility, their largest effect is in altering the solvent accessibility of the active site by expanding the active site volume, allowing additional water molecules to enter. This effect is markedly more pronounced in the organophosphatase activity than the lactonase activity. Differential effect of mutating Y71 on the native and promiscuous activities of PON1, detailed overview
additional information
modulating the active site hydrophobicity is a key element in facilitating the evolution of organophosphatase activity. Molecular dynamics simulations of wild-type and mutant PON1 enzymes, detailed overview
V346L
site-directed mutagenesis, the mutant shows highly reduced activity with diethyl-paraoxon compared to wild-type
V346L
site-directed mutagenesis, the mutant shows slightly increased activity with diethyl-paraoxon compared to wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cibacron Blue 3GA-agarose column chromatography, DEAE-Sepharose column chromatography, gel filtration, and Sepharose CL-6B column chromatography
-
DEAE-Sepharose column chromatography, Concanavalin A-Sepharose column chromatography, and Sepharose CL-6B gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3)
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
paraoxonase 1 significantly protects against sarin and soman exposure in guinea pigs and supports the development of paraoxonase 1 as a catalytic bioscavenger for protection against lethal exposure of chemical warfare nerve agents exposure
medicine
-
PON1 shows potential as a prophylactic treatment against tabun exposure
medicine
PON1 shows great promise as a biotherapeutic due to its role in atherosclerosis and because of its ability to hydrolyze a broad range of organophosphates, including pesticides and nerve agents such as sarin, soman, and VX
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Furlong, C.E.; Richter, R.J.; Chapline, C.; Crabb, J.W.
Purification of rabbit and human serum paraoxonase
Biochemistry
30
10133-10140
1991
Oryctolagus cuniculus, Homo sapiens
Hassett, C.; Richter, R.J.; Humbert, R.; Chapline, C.; Crabb, J.W.; Omiecinski, C.J.; Furlong, C.E.
Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence
Biochemistry
30
10141-10149
1991
Oryctolagus cuniculus, Homo sapiens
Kuo, C.L.; La Du, B.N.
Comparison of purified human and rabbit serum paraoxonases
Drug Metab. Dispos.
23
935-944
1995
Oryctolagus cuniculus, Homo sapiens
Kuo, C.L.; La Du, B.N.
Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymic activity
Drug Metab. Dispos.
26
653-660
1998
Oryctolagus cuniculus, Homo sapiens
Aharoni, A.; Gaidukov, L.; Yagur, S.; Toker, L.; Silman, I.; Tawfik, D.S.
Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
Proc. Natl. Acad. Sci. USA
101
482-487
2004
Homo sapiens (P27169), Homo sapiens (Q15166), Mus musculus (Q62087), Oryctolagus cuniculus (Q9BGN0)
Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Doctor, B.P.; Nambiar, M.P.
Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1
Biochem. Biophys. Res. Commun.
403
97-102
2010
Oryctolagus cuniculus, Homo sapiens
Valiyaveettil, M.; Alamneh, Y.; Rezk, P.; Biggemann, L.; Perkins, M.W.; Sciuto, A.M.; Doctor, B.P.; Nambiar, M.P.
Protective efficacy of catalytic bioscavenger, paraoxonase 1 against sarin and soman exposure in guinea pigs
Biochem. Pharmacol.
81
800-809
2011
Oryctolagus cuniculus, Homo sapiens
Valiyaveettil, M.; Alamneh, Y.; Biggemann, L.; Soojhawon, I.; Farag, H.A.; Agrawal, P.; Doctor, B.P.; Nambiar, M.P.
In vitro efficacy of paraoxonase 1 from multiple sources against various organophosphates
Toxicol. In Vitro
25
905-913
2011
Oryctolagus cuniculus, Homo sapiens
Le, Q.A.; Chang, R.; Kim, Y.H.
Rational design of paraoxonase 1 (PON1) for the efficient hydrolysis of organophosphates
Chem. Commun. (Camb.)
51
14536-14539
2015
Oryctolagus cuniculus (P27170)
Blaha-Nelson, D.; Krueger, D.M.; Szeler, K.; Ben-David, M.; Kamerlin, S.C.
Active site hydrophobicity and the convergent evolution of paraoxonase activity in structurally divergent enzymes the case of serum paraoxonase 1
J. Am. Chem. Soc.
139
1155-1167
2017
Oryctolagus cuniculus (P27170)
Zhang, H.; Yang, L.; Ma, Y.Y.; Zhu, C.; Lin, S.; Liao, R.Z.
Theoretical studies on catalysis mechanisms of serum paraoxonase 1 and phosphotriesterase diisopropyl fluorophosphatase suggest the alteration of substrate preference from paraoxonase to DFP
Molecules
23
1660
2018
Oryctolagus cuniculus (P27170)
Zhang, H.; Yang, L.; Ma, Y.Y.; Zhu, C.; Lin, S.; Liao, R.Z.
Theoretical studies on catalysis mechanisms of serum paraoxonase 1 and phosphotriesterase diisopropyl fluorophosphatase suggest the alteration of substrate preference from paraoxonase to DFP
Molecules
23
E1660
2018
Oryctolagus cuniculus (P27170)
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Transporter Classification Database (TCDB): 1.A.6.2.6
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