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Information on EC 3.1.1.2 - arylesterase and Organism(s) Rattus norvegicus and UniProt Accession P55159

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.2 arylesterase
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 .
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Rattus norvegicus
UNIPROT: P55159
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aryldialkylphosphatase
exhibits multiple enzyme activities including organophosphate esterase, carboxyl esterase, lactonase, and phospholipase A2 activity
phenyl acetate esterase
-
A-esterase
aromatic esterase
-
-
-
-
Aryl-ester hydrolase
-
-
-
-
K-45
-
-
-
-
paraoxonase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
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 hide
9032-73-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
0.9 mM, the further increase of the calcium concentration does not significantly increase arylesterase activity
Ca2+
-
optimal concentration is 2 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-hydroxymercuribenzoate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclophosphamide
22% increase in the activity of PON1 in the liver and 23% increase in PON1 activity in the serum is observed 24 h after treatment with a single dose of 150 mg/kg cyclophosphamide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46 - 0.64
phenyl acetate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PON1_RAT
355
0
39358
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
x * 43000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
diminishing the pH below 8.0 in the Tris/HCl medium does not cause the activation of arylesterase
692124
5 - 10
almost 100% activity is maintained during the incubation period of 180 min
649767
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
increasing the temperature over 25°C in the Tris/HCl medium does not cause the activation of arylesterase
40 - 55
180 min, quite stable
60
90 min, 50% loss of activity
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
two A-esterases, difficult to separate
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both Wakame and Nori algae diets significantly increase arylesterase activity. Arylesterase activity increases in cholesterol-enriched-diet and Wakame-diet rats but not in Nori-diet rats compared with their corresponding counterparts
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there is a significant decrease of arylesterase 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 arylesterase activity in respect to rats receiving hypercholesterolemic diet without any treatment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
Abraham, P.; Sugumar, E.
Increased glutathione levels and activity of PON1 (phenyl acetate esterase) in the liver of rats after a single dose of cyclophosphamide: a defense mechanism?
Exp. Toxicol. Pathol.
59
301-306
2008
Rattus norvegicus (P55159), Rattus norvegicus
Manually annotated by BRENDA team
Harisa, G.
L-arginine ameliorates arylesterase/paraoxonase activity of paraoxonase-1 in hypercholesterolemic rats
Asian J. Biochem.
6
263-272
2011
Rattus norvegicus
-
Manually annotated by BRENDA team
Olivero-David, R.; Schultz-Moreira, A.; Vazquez-Velasco, M.; Gonzalez-Torres, L.; Bastida, S.; Benedi, J.; Isabel Sanchez-Reus, M.; Jose Gonzalez-Munoz, M.; Sanchez-Muniz, F.J.
Effects of Nori- and Wakame-enriched meats with or without supplementary cholesterol on arylesterase activity, lipaemia and lipoproteinaemia in growing Wistar rats
Br. J. Nutr.
106
1476-1486
2011
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team