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Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Mus musculus and UniProt Accession Q62087

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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:
Mus musculus
UNIPROT: Q62087
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The taxonomic range for the selected organisms is: Mus musculus
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
-
-
-
-
aryltriphosphatase
-
-
-
-
esterase B1
-
-
-
-
esterase E4
-
-
-
-
esterase, organophosphate
-
-
-
-
esterase, paraoxon
-
-
-
-
esterase, pirimiphos-methyloxon
-
-
-
-
HDL-PON1
-
-
HuPON1
-
-
-
-
OPA anhydrase
-
-
-
-
OPH
-
-
-
-
organophosphate hydrolase
-
-
-
-
organophosphorus acid anhydrase
-
-
-
-
organophosphorus hydrolase
-
-
-
-
paraoxon hydrolase
-
-
-
-
paraoxonase
paraoxonase 1
-
paraoxonase-1
phosphotriesterase
-
-
-
-
pirimiphos-methyloxon esterase
-
-
-
-
PTE
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric triester
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
paraoxon + H2O
4-nitrophenol + diethyl phosphate
show the reaction diagram
-
-
-
?
chlorpyrifos oxon + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl phosphate
show the reaction diagram
-
-
-
-
?
diazoxon + H2O
2-isopropyl-6-methyl-pyrimidin-4-ol + diethyl phosphate
show the reaction diagram
-
-
-
-
?
methyl paraoxon + H2O
4-nitrophenol + dimethyl phosphate
show the reaction diagram
-
weak activity
-
-
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
show the reaction diagram
-
-
-
-
?
paraoxon + H2O
4-nitrophenol + diethylphosphate
show the reaction diagram
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
show the reaction diagram
pirimiphos-methyloxon + H2O
?
show the reaction diagram
-
-
-
-
?
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
additional information
?
-
-
the enzyme associated to high-density lipoproteins HDL exhibits antioxidant function of particular physiological relevance, mechanism, compositional fluctuations of HDL effects the influence of the enzyme on cardiovascular risks, overview
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aspirin
induces paraoxonase 1 expression in the liver and stimulates enzymatic activity in blood plasma
di-oleoyl phosphatidylcholine
2.6 mM di-oleoyl phosphatidylcholine stimulates arylesterase activity of PON1 3.5fold
salicylic acid
induces paraoxonase 1 expression in the liver and stimulates enzymatic activity in blood plasma
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
paraoxon
pH 8.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
paraoxon
pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
epithelial cells of the bronchiole, PON1
Manually annotated by BRENDA team
fibre tracts of the encephalon, PON1
Manually annotated by BRENDA team
surface epithelium of the intestine, PON1
Manually annotated by BRENDA team
kidney proximal tubulus, PON1
Manually annotated by BRENDA team
eye lens epithelium, PON1
Manually annotated by BRENDA team
PON2 expression is restricted to the endomysium in muscle cells
Manually annotated by BRENDA team
exocrine pancreas acini, PON1
Manually annotated by BRENDA team
acini of the sebaceous gland, PON1
Manually annotated by BRENDA team
fibre tracts of the spinal cord, PON1
Manually annotated by BRENDA team
surface epithelium of the stomach, PON1
Manually annotated by BRENDA team
acini of the submandibular gland, PON1
Manually annotated by BRENDA team
tongue epithelium, PON1
Manually annotated by BRENDA team
epithelial cells of the trachea, PON1
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted to serum mediated by the associated high-density lipoproteins HDL
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
paraoxonase 1 knockout mice are dramatically more sensitive than wild type mice to the toxicity of chlorpyrifos oxon and diazoxon and to a lesser extent the parent phosphorothioates, chlorpyrifos and diazinon
physiological function
-
paraoxonase 1 modulates the toxicity of organophosphorous mixtures (paraoxon, chlorpytifoy oxon, diazoxon) by altering the activity of another detoxication enzyme, carboxylesterase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PON3_MOUSE
354
0
39351
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
331000
-
gel filtration
40000
-
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, SDS-PAGE
additional information
-
high-density lipoproteins HDL form an amphipathic environment for the associated enzyme whose hydrophobic, N-terminal region is shielded by that way required for the substrate binding of PON1
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PON1
-
the mutant is less able to detoxify diazoxon
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of di-oleoyl phosphatidylcholine to serum stabilizes PON1 activity and protects PON1 from nitrilotriacetic acid-induced inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, Y.S.; Woods, L.; Sultatos, L.G.
Solubilization and purification of A-esterase from mouse hepatic microsomes
Biochem. Pharmacol.
48
1273-1280
1994
Mus musculus
Manually annotated by BRENDA team
Mackness, M.I.; Thompson, H.M.; Hardy, A.R.; Walker, C.H.
Distinction between A-esterases and arylesterases. Implications for esterase classification
Biochem. J.
245
293-296
1987
Bos taurus, Felis catus, Homo sapiens, Hydrochoerus hydrochaeris, Meles taxus, Mus musculus, no activity in aves, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
James, R.W.; Deakin, S.P.
The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity
Free Radic. Biol. Med.
37
1986-1994
2004
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Efrat, M.; Rosenblat, M.; Mahmood, S.; Vaya, J.; Aviram, M.
Di-oleoyl phosphatidylcholine (PC-18:1) stimulates paraoxonase 1 (PON1) enzymatic and biological activities: in vitro and in vivo studies
Atherosclerosis
202
461-469
2009
Mus musculus (P52430)
Manually annotated by BRENDA team
Marsillach, J.; Mackness, B.; Mackness, M.; Riu, F.; Beltran, R.; Joven, J.; Camps, J.
Immunohistochemical analysis of paraoxonases-1, 2, and 3 expression in normal mouse tissues
Free Radic. Biol. Med.
45
146-157
2008
Mus musculus (P52430), Mus musculus (Q62086)
Manually annotated by BRENDA team
Parker-Katiraee, L.; Bousiaki, E.; Monk, D.; Moore, G.E.; Nakabayashi, K.; Scherer, S.W.
Dynamic variation in allele-specific gene expression of Paraoxonase-1 in murine and human tissues
Hum. Mol. Genet.
17
3263-3270
2008
Mus musculus (P52430)
Manually annotated by BRENDA team
Jaichander, P.; Selvarajan, K.; Garelnabi, M.; Parthasarathy, S.
Induction of paraoxonase 1 and apolipoprotein A-I gene expression by aspirin
J. Lipid Res.
49
2142-2148
2008
Homo sapiens (P27169), Mus musculus (P52430)
Manually annotated by BRENDA team
Cole, T.B.; Jansen, K.; Park, S.; Li, W.F.; Furlong, C.E.; Costa, L.G.
The toxicity of mixtures of specific organophosphate compounds is modulated by paraoxonase 1 status
Adv. Exp. Med. Biol.
660
47-60
2010
Mus musculus
Manually annotated by BRENDA team