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EC Tree
IUBMB Comments Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate .
The taxonomic range for the selected organisms is: Oryctolagus cuniculus The enzyme appears in selected viruses and cellular organisms
Synonyms
paraoxonase, arylesterase, paraoxonase 1, paraoxonase-1, paraoxonase1, est-1, est-2, paraoxonase/arylesterase, a-esterase, alpha-esterase,
more
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aromatic esterase
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Aryl-ester hydrolase
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additional information
cf. EC 3.1.8.1
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a phenyl acetate + H2O = a phenol + acetate
H115 acts as general base, H134 acts in a proton shuttle mechanismto increase H115s basicity
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hydrolysis of carboxylic ester
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aryl-ester hydrolase
Acts on many phenolic esters. The reactions of EC 3.1.8.1 aryldialkylphosphatase, were previously attributed to this enzyme. It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases [7,8]. The natural substrates of the paraoxonases are lactones [7,8], with (+/-)-5-hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate [8].
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2-naphthyl acetate + H2O
2-naphthol + acetate
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-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
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0.1% of the activity with phenyl acetate
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-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
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13.5% of the activity with phenyl acetate
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-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
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29% of the activity with phenyl acetate
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-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
phenyl acetate + H2O
phenol + acetate
thiophenyl acetate + H2O
?
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30.5% of the activity with phenyl acetate
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-
?
additional information
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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 is a paraoxonase (EC 3.1.8.1) that also shows arylesterase activity (EC 3.1.1.2) with phenyl acetate as substrate
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?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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-
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-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
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31% of the activity with phenyl acetate
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-
?
phenyl acetate + H2O
phenol + acetate
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-
?
phenyl acetate + H2O
phenol + acetate
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-
?
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phenyl acetate + H2O
phenol + acetate
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?
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Cd2+
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Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
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Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Ca2+
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required
Ca2+
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included in active site
Ca2+
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Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+, two Ca2+ binding sites
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2-hydroxyquinoline
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dose-dependent inhibition of enzyme activity against 4-nitrophenyl acetate substrate
2-hydroxyquinoline
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specific paraoxonase 1 inhibitor, dose-dependent inhibition
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dimyristoyl phosphatidylcholine
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stimulates
dioleoyl phosphatidylcholine
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stimulates
lysolecithin
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stimulates
phosphatidylethanolamine
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stimulates
phosphatidylglycerol
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stimulates
phosphatidylsenine
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stimulates
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sphingomyelin
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stimulates
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0.211
2-naphthyl acetate
pH 8.0
0.336
4-nitrophenyl acetate
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in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
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0.66
2-naphthyl acetate
pH 8.0
2500
4-nitrophenyl acetate
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in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
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7500
4-nitrophenyl acetate
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in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
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3.5
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enzyme purified from serum, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
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UniProt
brenda
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brenda
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brenda
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PON3_RABIT
354
0
39507
Swiss-Prot
Secretory Pathway (Reliability: 1 )
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39800
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rabbit serum contains two major species of PON monomers (42300 Da and 39800 Da), SDS-PAGE
42300
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rabbit serum contains two major species of PON monomers (42300 Da and 39800 Da), SDS-PAGE
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?
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x * 40000-45000, paraoxonase 1 is separated as three bands with an approximate molecular weight of 40000-45000 Da, SDS-PAGE
?
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x * 40000-45000, rabbit serum purified paraoxonase 1 shows three bands in the about 40000-45000 kDa molecular weight regions, SDS-PAGE
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glycoprotein
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at least 2 N-linked sugar chains, contains sialic acid residues
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H115W/T332/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
H115W/T332S
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
H115W/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
I74F/H115W
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/H115W/T332
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/H115W/V346A
site-directed mutagenesis, the mutant shows no activity with phenylacetate compared to wild-type
I74F/T332S
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
I74F/V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
T332S
site-directed mutagenesis, the mutant shows 2fold increased activity with phenylacetate compared to wild-type
T332S/V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
V346A
site-directed mutagenesis, the mutant shows reduced activity with phenylacetate compared to wild-type
additional information
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mutant rePON1-G2E6, 91% identity with wild-type and several variations deriving from human, mouse or rat wild-type enzyme, crystal structure
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Cibacron Blue 3GA-agarose column chromatography, DEAE-Sepharose column chromatography, gel filtration, and Sepharose CL-6B column chromatography
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DEAE-Sepharose column chromatography, Concanavalin A-Sepharose column chromatography, and Sepharose CL-6B gel filtration
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gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3)
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medicine
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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
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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
brenda
Harel, M.; Aharoni, A.; Gaidukov, L.; Brumshtein, B.; Khersonsky, O.; Meged, R.; Dvir, H.; Ravelli, R.B.G.; McCarthy, A.; Toker, L.; Silman, I.; Sussman, J.L.; Tawfik, D.S.
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes
Nat. Struct. Mol. Biol.
11
412-419
2004
Oryctolagus cuniculus
brenda
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 (Q15166), Mus musculus (Q62087), Oryctolagus cuniculus (Q9BGN0)
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
Transporter Classification Database (TCDB):
1.A.6.2.6