3.1.1.2: arylesterase
This is an abbreviated version!
For detailed information about arylesterase, go to the full flat file.
Word Map on EC 3.1.1.2
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3.1.1.2
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lipoprotein
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cholesterol
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high-density
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atherosclerosis
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cardiovascular
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low-density
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coronary
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apolipoproteins
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artery
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triglyceride
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organophosphate
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malondialdehyde
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hdl-associated
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lactonase
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anti-oxidant
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atherogenic
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mellitus
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c-reactive
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organophosphorus
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pesticide
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acetylcholinesterase
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phenylacetate
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lipoprotein-associated
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hdl-cholesterol
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homocysteine
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atherogenesis
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esterases
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cholinesterase
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apoa-i
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antiatherogenic
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qq
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ox-ldl
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chlorpyrifos
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atheroprotective
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oxons
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butyrylcholinesterase
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carboxylesterase
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lipoprotein-cholesterol
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paf-ah
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lp-pla2
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phosphotriesterase
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parathion
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soman
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analysis
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clopidogrel
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acetylhydrolase
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drug development
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allozyme
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oxidant-antioxidant
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sarin
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lecithin:cholesterol
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medicine
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thiolactone
- 3.1.1.2
- lipoprotein
- cholesterol
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high-density
- atherosclerosis
- cardiovascular
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low-density
- coronary
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apolipoproteins
- artery
- triglyceride
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organophosphate
- malondialdehyde
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hdl-associated
- lactonase
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anti-oxidant
-
atherogenic
- mellitus
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c-reactive
-
organophosphorus
-
pesticide
- acetylcholinesterase
- phenylacetate
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lipoprotein-associated
-
hdl-cholesterol
- homocysteine
- atherogenesis
- esterases
- cholinesterase
- apoa-i
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antiatherogenic
-
ox-ldl
- chlorpyrifos
-
atheroprotective
-
oxons
- butyrylcholinesterase
- carboxylesterase
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lipoprotein-cholesterol
- paf-ah
- lp-pla2
- phosphotriesterase
- parathion
- soman
- analysis
- clopidogrel
-
acetylhydrolase
- drug development
-
allozyme
-
oxidant-antioxidant
- sarin
-
lecithin:cholesterol
- medicine
-
thiolactone
Reaction
Synonyms
(R)-specific SGNH arylesterase, A-esterase, alpha-esterase, ARE, AREase, aromatic esterase, Aryl-ester hydrolase, aryldialkylphosphatase, arylesterase, DvvII, EST-1, EST-2, EST-3, ESt-A, Est0881, EstB, EstR5, G3C9 rePON1, gox0881, HDL-PON1, K-45, lp_1002, More, neuropathy target esterase-related esterase, NRE, NRECV, NTE-R1, NTE-related 1, NTE-related esterase, paraoxonase, paraoxonase 1, paraoxonase-1, paraoxonase/arylesterase, paraoxonase1, patatin-like phospholipase 7, phenyl acetate esterase, phenyl valerate esterase, PNPLA7, PON-aryl, PON1, PON1/Aryl, pyrethroid-resistance-associated esterase, Saci_2140, SacPox, serum paraoxonase/arylesterase 1, SGNH arylesterase, SGNH-arylesterase, SisLac, Sm23, Vmut2255, VmutPLL
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3.1.1.2 arylesteraseAdvanced search results
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Source Tissue on EC 3.1.1.2 - arylesterase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
of patients with disorders of galactose metabolism. Low total antioxidant status and high galactose 1-phosphate levels may reduce activity of paraoxonase 1/arylesterase
PON1 activity is lower in chronic hepatitis patients compared with the control subjects
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enzyme activity against the phenylacetate is higher, and phenotype-dependent, only in diabetic patients with type II diabetes mellitus. Less antiatherogenic paraoxonase B allele is more frequent in type II diabetes mellitus than in the healthy population. Their lipid status is more atherogenic, which could indicate a risk of premature atherosclerosis
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in serum, the esterase is tightly bound to the high density lipoproteins, particularly apo A-l
in the blood of Gulf War veterans who developed delayed neurotoxicity symptoms the levels of serum paraoxonase (PON1) isozyme type Q is significantly lower than in the control, unaffected veteran group
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of A and B phenotypes. Human serum contains a single enzyme with both paraoxonase and arylesterase activities
phenylketonuric patients. Paraoxonase/arylesterase activities are strongly related to the dietary control of phenylketonuric patients
PON1 activity determined towards the synthetic compounds paraoxon and phenyl acetate reflects no association with markers of oxidative stress
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two proteins capable of hydrolyzing paraoxon are present in rat liver microsomes, enzyme form M1 and M2
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692695, 707155, 709755, 714045, 714112, 714759, 714893, 714895, 715735, 715738, 716956, 729339, 729341, 730929, 730945
the enzyme activity is significantly lower in serum from patients with hyperemesis gravidarum than in serum from healthy individuals
the enzyme is exclusively located on high density lipoprotein in serum
