Entry |
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Name |
arylesterase;
A-esterase;
paraoxonase;
aromatic esterase
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Class |
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
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Sysname |
aryl-ester hydrolase
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Reaction(IUBMB) |
a phenyl acetate + H2O = a phenol + acetate [RN: R07342]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
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].
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History |
EC 3.1.1.2 created 1961, modified 1989
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Pathway |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K01045 | arylesterase / paraoxonase |
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Genes |
» show all
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Reference |
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Authors |
ALDRIDGE WN. |
Title |
Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination. |
Journal |
Biochem J 53:110-7 (1953) |
Reference |
|
Authors |
AUGUSTINSSON KB, OLSSON B. |
Title |
Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies. |
Journal |
Biochem J 71:477-84 (1959) |
Reference |
|
Authors |
Bosmann HB. |
Title |
Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate. |
Journal |
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Reference |
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Authors |
Kim DH, Yang YS, Jakoby WB. |
Title |
Nonserine esterases from rat liver cytosol. |
Journal |
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Reference |
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Authors |
Mackness MI, Thompson HM, Hardy AR, Walker CH. |
Title |
Distinction between 'A'-esterases and arylesterases. Implications for esterase classification. |
Journal |
Biochem J 245:293-6 (1987) |
Reference |
6 |
Authors |
In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.), Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989. |
Reference |
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Authors |
Khersonsky O, Tawfik DS. |
Title |
Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. |
Journal |
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Reference |
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Authors |
Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN. |
Title |
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. |
Journal |
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Sequence |
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Other DBs |
ExplorEnz - The Enzyme Database: | 3.1.1.2 |
ExPASy - ENZYME nomenclature database: | 3.1.1.2 |
UM-BBD (Biocatalysis/Biodegradation Database): | 3.1.1.2 |
BRENDA, the Enzyme Database: | 3.1.1.2 |
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