Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.1.2 - arylesterase and Organism(s) Oryctolagus cuniculus and UniProt Accession Q9BGN0

for references in articles please use BRENDA:EC3.1.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Oryctolagus cuniculus
UNIPROT: Q9BGN0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A-esterase
-
-
-
-
aromatic esterase
-
-
-
-
Aryl-ester hydrolase
-
-
-
-
K-45
-
-
-
-
paraoxonase
-
-
-
-
additional information
cf. EC 3.1.8.1
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a phenyl acetate + H2O = a phenol + acetate
show the reaction diagram
H115 acts as general base, H134 acts in a proton shuttle mechanismto increase H115’s basicity
-
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
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
show the reaction diagram
-
0.1% of the activity with phenyl acetate
-
-
?
2-naphthyl acetate + H2O
2-naphthol + acetate
show the reaction diagram
-
13.5% of the activity with phenyl acetate
-
-
?
2-nitrophenyl acetate + H2O
2-nitrophenol + acetate
show the reaction diagram
-
29% of the activity with phenyl acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
thiophenyl acetate + H2O
?
show the reaction diagram
-
30.5% of the activity with phenyl acetate
-
-
?
additional information
?
-
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
-
-
?
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
phenyl acetate + H2O
phenol + acetate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
Zn2+
-
Ca2+ is required for catalytic activity and structural stability. Cd2+ or Zn2+ substitute for Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxyquinoline
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
stimulates
dimyristoyl phosphatidylcholine
-
stimulates
dioleoyl phosphatidylcholine
-
stimulates
lecithin
-
stimulates
lysolecithin
-
stimulates
phosphatidylethanolamine
-
stimulates
phosphatidylglycerol
-
stimulates
phosphatidylsenine
-
stimulates
-
sphingomyelin
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.211
2-naphthyl acetate
pH 8.0
0.336
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.66
2-naphthyl acetate
pH 8.0
2500
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7500
4-nitrophenyl acetate
-
in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
-
enzyme purified from serum, in 20 mM Tris-HCl buffer (pH 7.4), at 37°C
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PON3_RABIT
354
0
39507
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39800
-
rabbit serum contains two major species of PON monomers (42300 Da and 39800 Da), SDS-PAGE
42300
-
rabbit serum contains two major species of PON monomers (42300 Da and 39800 Da), SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
at least 2 N-linked sugar chains, contains sialic acid residues
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of mutant rePON1-G2E6
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
mutant rePON1-G2E6, 91% identity with wild-type and several variations deriving from human, mouse or rat wild-type enzyme, crystal structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cibacron Blue 3GA-agarose column chromatography, DEAE-Sepharose column chromatography, gel filtration, and Sepharose CL-6B column chromatography
-
DEAE-Sepharose column chromatography, Concanavalin A-Sepharose column chromatography, and Sepharose CL-6B gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PON1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
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 (Q15166), Mus musculus (Q62087), Oryctolagus cuniculus (Q9BGN0)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team