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Information on EC 3.1.1.2 - arylesterase and Organism(s) Mus musculus and UniProt Accession Q62087
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3.1.1.2 arylesteraseIUBMB 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 .
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Word Map
- 3.1.1.2
- lipoprotein
- cholesterol
-
high-density
- atherosclerosis
- cardiovascular
-
low-density
- coronary
-
apolipoproteins
- artery
- triglyceride
-
organophosphate
- malondialdehyde
-
hdl-associated
- lactonase
-
anti-oxidant
-
atherogenic
- mellitus
-
c-reactive
-
organophosphorus
-
pesticide
- acetylcholinesterase
- phenylacetate
-
lipoprotein-associated
-
hdl-cholesterol
- homocysteine
- atherogenesis
- esterases
- cholinesterase
- apoa-i
-
antiatherogenic
-
ox-ldl
- chlorpyrifos
-
atheroprotective
-
oxons
- butyrylcholinesterase
- carboxylesterase
-
lipoprotein-cholesterol
- paf-ah
- lp-pla2
- phosphotriesterase
- parathion
- soman
- analysis
- clopidogrel
-
acetylhydrolase
- drug development
-
allozyme
-
oxidant-antioxidant
- sarin
-
lecithin:cholesterol
- medicine
-
thiolactone
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A-esterase
-
-
-
-
aromatic esterase
-
-
-
-
Aryl-ester hydrolase
-
-
-
-
K-45
-
-
-
-
paraoxonase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
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].
CAS REGISTRY NUMBER
COMMENTARY
9032-73-9
-
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
additional information
?
-
PON1 is a lipo-lactonase which is associated with high density lipoprotein and possesses antioxidative properties
-
-
?
additional information
?
-
-
PON1 is a lipo-lactonase which is associated with high density lipoprotein and possesses antioxidative properties
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
0.9 mM, the further increase of the calcium concentration does not significantly increase arylesterase activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aspirin
induces enzyme 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 enzyme expression in the liver and stimulates enzymatic activity in blood plasma
additional information
serum arylesterase activity is positively correlated with serum total cholesterol and low density lipoprotein and very low density lipoprotein-cholesterol concentrations
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
phenyl acetate
wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C
0.201
phenyl acetate
wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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_MOUSE
354
0
39351
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
diminishing the pH below 8.0 in the Tris/HCl medium does not cause the activation of arylesterase
692124
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
increasing the temperature over 25°C in the Tris/HCl medium does not cause the activation of arylesterase
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of di-oleoyl phosphatidylcholine to serum stabilizes PON1 activity and protects PON1 from nitrilotriacetic acid-induced inactivation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
PON1 overexpression is associated with decreased diabetes-induced macrophage oxidative stress, decreased diabetes development, and decreased mortality
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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), Mus musculus
Lopez-Oliva, E.; Nus, M.; Agis-Torres, A.; Villaro, W.; Sanchez-Montero, J.M.; Munoz-Martinez, E.; Sanchez-Muniz, F.J.
Growth hormone improves lipoprotein concentration and arylesterase activity in mice with an atherogenic lipid profile induced by lactalbumin
Br. J. Nutr.
101
518-526
2009
Mus musculus (P52430)
Nus, M.; Sanchez-Muniz, F.J.; Gago, J.V.; Lopez-Oliva, E.; Sanchez-Montero, J.M.
Determination of rat and mice arylesterase activity using serum mimetics
Enzyme Microb. Technol.
43
252-256
2008
Mus musculus (P52430), Rattus norvegicus (P55159)
-
Rozenberg, O.; Shiner, M.; Aviram, M.; Hayek, T.
Paraoxonase 1 (PON1) attenuates diabetes development in mice through its antioxidative properties
Free Radic. Biol. Med.
44
1951-1959
2008
Mus musculus (P52430), Mus musculus
Chang, P.; Long, D.; Sun, Q.; Wang, Q.; Bu, Y.; Wu, Y.
Identification and characterization of a splice variant of the catalytic domain of mouse NTE-related esterase
Gene
417
43-50
2008
Mus musculus
EXTERNAL LINKS (specific for EC-Number 3.1.1.2)
Transporter Classification Database (TCDB): 1.A.6.2.6
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