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Information on EC 3.1.8.1 - aryldialkylphosphatase and Organism(s) Rattus norvegicus and UniProt Accession Q68FP2
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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: Rattus norvegicus
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
paraoxonase-1
exhibits multiple enzyme activities including organophosphate esterase, carboxyl esterase, lactonase, and phospholipase A2 activity
phosphotriesterase
-
-
-
-
pirimiphos-methyloxon esterase
-
-
-
-
PTE
-
-
-
-
paraoxonase
-
-
-
-
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
chlorpyrifos + H2O
3,5,6-trichloro-pyridin-2-ol + diethyl thiophosphate
-
-
-
-
?
paraoxon + H2O
diethylphosphate + 4-nitrophenol
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
essential activator of rat plasma enzyme, nonessential activator of liver microsomal enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
ethanol consumption causes a significant decrease in liver paraoxonase activity. Gallic acid treatment partly restores this decreased paraoxonase activity. A gallic acid dose of 100 mg/kg shows highest restoring effect for paraoxonase activity. The activity of arylesterase is decreased in the ethanol group, but this decrease is not significant. Gallic acid treatment restores the loss of this activity due to ethanol exposure
additional information
infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
-
additional information
-
infection with the intestinal nematode Nippostrongylus brasiliensis leads to decreased PON1 serum activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
two proteins capable of hydrolyzing paraoxon are present in rat liver microsomes, enzyme form M1 and M2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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_RAT
354
0
39458
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
almost 100% activity is maintained during the incubation period of 180 min
649767
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
rat plasma enzyme is more stable to heat inactivation than rat liver microsomal enzyme, no loss of activity in human serum after 3 days and 33% after 5 days
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme is quite stable, showing no decrease in specific activity after storage for 1 month
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the presence of 2.5 mM Ca2+ and 0.1% (w/v) Triton X-100 (as detergent) in the buffers throughout the purification procedure is essential for maintaining the activity of the enzyme. In the absence of calcium and Triton X-100, the enzyme activity is quickly lost
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
there is a significant decrease of paraoxonase-1 activity of paraoxonase as a result of hypercholesterolemic diet feeding. Supplementation of rats with 3% (w/v) L-Arg in drinking water with standard diet or hypercholesterolemic diet markedly preserves enzymatic paraoxonase-1 activity in respect to rats receiving hypercholesterolemic diet without any treatment
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
-
no effect of caloric restriction upon triglyceride or total cholesterol concentration or on enzyme mRNA level. Enzyme activity tends to be higher in females and drops with caloric restriction in both genders. Variations in enzyme activity and apolipoprotein levels show gender-related differences that indicate a different adaptive strategy of male and female animals when faced with a period of food restriction
medicine
-
no effect of caloric restriction upon triglyceride or total cholesterol concentration or on enzyme mRNA level. Enzyme activity tends to be higher in females and drops with caloric restriction in both genders. Variations in enzyme activity and apolipoprotein levels show gender-related differences that indicate a different adaptive strategy of male and female animals when faced with a period of food restriction
medicine
-
ethanol consumption causes a significant decrease in liver paraoxonase activity. Gallic acid treatment partly restores this decreased paraoxonase activity. A gallic acid dose of 100 mg/kg shows highest restoring effect for paraoxonase activity. The activity of arylesterase is decreased in the ethanol group, but this decrease is not significant. Gallic acid treatment restores the loss of this activity due to ethanol exposure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gil, F.; Pla, A.; Gonzalvo, M.C.; Hernandez, A.F.; Villanueva, E.
Rat liver paraoxonase: subcellular distribution and characterization
Chem. Biol. Interact.
87
149-154
1993
Rattus norvegicus
Pond, A.L.; Chambers, H.W.; Coyne, C.P.; Chamers, J.E.
Purification of two rat hepatic proteins with A-esterase activity toward chlorpyrifos-oxon and paraoxon
J. Pharmacol. Exp. Ther.
286
1404-1411
1998
Rattus norvegicus
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
Gil, F.; Gonzalvo, M.C.; Hernandez, A.F.; Villanueva, E.; Antonio, P.
Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver
Biochem. Pharmacol.
48
1559-1568
1994
Rattus norvegicus
Gil, F.; Pla, A.; Gonzalco, M.C.; Hernandez, A.F.; Villanueva, E.
Partial purification of paraoxonase from rat liver
Chem. Biol. Interact.
87
69-75
1993
Rattus norvegicus
Pellin, M.C.; Moretto, A.; Lotti, M.; Vilanova, E.
Distribution and some biochemical properties of rat paraoxonase activity
Neurotoxicol. Teratol.
12
611-614
1990
Homo sapiens, Rattus norvegicus
Little, J.S.; Broomfield, C.A.; Fox-Talbot, M.K.; Boucher, L.J.; MacIver, B.; Lenz, D.E.
Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP)
Biochem. Pharmacol.
38
23-29
1989
Rattus norvegicus
Efremenko, E.N.; Sergeeva, V.S.
Organophosphate hydrolase - an enzyme catalyzing degradation of phosphorus-containing toxins and pesticides
Russ. Chem. Bull. (Translation of Izvestiya Akademii Nauk, Seriya Khimicheskaya)
50
1826-1832
2001
Brevundimonas diminuta, Flavobacterium sp., Rattus norvegicus
-
Rodrigo, L.; Gil, F.; Hernandez, A.F.; Marina, A.; Vazquez, J.; Pla, A.
Purification and characterization of paraoxon hydrolase from rat liver
Biochem. J.
321
595-601
1997
Rattus norvegicus
Rodrigo, L.; Gil, F.; Hernandez, A.F.; Pla, A.
Identification of two rat liver proteins with paraoxonase activity: biochemical evidence for the identity of paraoxonase and arylesterase
Chem. Biol. Interact.
119-120
263-275
1999
Rattus norvegicus
Rodrigo, L.; Gil, F.; Hernandez, A.F.; Lopez, O.; Pla, A.
Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties
Biochem. J.
376
261-268
2003
Rattus norvegicus (Q68FP2)
Thomas-Moya, E.; Gianotti, M.; Llado, I.; Proenza, A.M.
Effects of caloric restriction and gender on rat serum paraoxonase 1 activity
J. Nutr. Biochem.
17
197-203
2006
Rattus norvegicus
Farid, A.S.; Nakahara, K.; Murakami, N.; Hayashi, T.; Horii, Y.
Decreased serum paraoxonase-1 activity during intestinal nematode (Nippostrongylus brasiliensis) infection in rats
Am. J. Trop. Med. Hyg.
78
770-776
2008
Rattus norvegicus (P55159), Rattus norvegicus
Harisa, G.
L-arginine ameliorates arylesterase/paraoxonase activity of paraoxonase-1 in hypercholesterolemic rats
Asian J. Biochem.
6
263-272
2011
Rattus norvegicus
-
Kartkaya, K.; Oglakci, A.; sentuerk, H.; Bayramoglu, G.; Canbek, M.; Kanbak, G.
Investigation of the possible protective role of gallic acid on paraoxanase and arylesterase activities in livers of rats with acute alcohol intoxication
Cell Biochem. Funct.
31
208-213
2013
Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 3.1.8.1)
Transporter Classification Database (TCDB): 1.A.6.2.6
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