View source for ADP-dependent short-chain-acyl-CoA hydrolase

{{enzyme
| Name = arylesterase
| EC_number = 3.1.1.2
| CAS_number = 9032-73-9
| IUBMB_EC_number = 3/1/1/2
| GO_code = 0004064
| image = 
| width = 
| caption = 
}}
In [[enzymology]], an '''arylesterase''' ({{EC number|3.1.1.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:a phenyl acetate + H<sub>2</sub>O <math>\rightleftharpoons</math> a phenol + acetate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[phenyl acetate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[phenol]] and [[acetate]].

This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on carboxylic [[ester]] bonds.  The systematic name of this enzyme class is '''aryl-ester hydrolase'''. Other names in common use include '''A-esterase''', '''paraoxonase''', and '''aromatic esterase'''.  This enzyme participates in [[bisphenol a degradation]].  

==Structural studies==

As of late 2007, two [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1V04}} and {{PDB link|1VA4}}.

==References==
{{reflist|1}}
* {{cite journal | author = ALDRIDGE WN | date = 1953 | 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.  | volume = 53 | pages = 110&ndash;7  | pmid = 13032041 | issue = 1 | pmc = 1198110 }}
* {{cite journal | author = AUGUSTINSSON KB, OLSSON B | date = 1959 | title = Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies | journal = Biochem. J.  | volume = 71 | pages = 477&ndash;84  | pmid = 13638253 | issue = 3 | pmc = 1196820 }}
* {{cite journal | author = Bosmann HB | date = 1972 | title = Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate | journal = Biochim. Biophys. Acta.  | volume = 276 | pages = 180&ndash;91  | pmid = 5047702 | issue = 1 }}
* {{cite journal | author = Kim DH, Yang YS, Jakoby WB | date = 1990 | title = Nonserine esterases from rat liver cytosol | journal = Protein. Expr. Purif.  | volume = 1 | pages = 19&ndash;27  | pmid = 2152179 | doi = 10.1016/1046-5928(90)90040-6 | issue = 1 }}
* {{cite journal | author = Mackness MI, Thompson HM, Hardy AR, Walker CH | date = 1987 | title = Distinction between 'A'-esterases and arylesterases. Implications for esterase classification | journal = Biochem. J.  | volume = 245 | pages = 293&ndash;6  | pmid = 2822017 | issue = 1 | pmc = 1148115 }}
* {{cite journal | author = UK, 1989 | date =  | title = 7  [PMID:15835926] | journal = Khersonsky O, Tawfik  | volume = DS. | pages = DS }}
* {{cite journal | author = Biochemistry 44 (2005) 6371-82 | date =  | title = 8  [PMID:15772423] | journal = Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du  | volume = BN. | pages = BN }}
* J Lipid Res 46 (2005) 1239-47.

{{hydrolase-stub}}

[[Category:EC 3.1.1]]
[[Category:Enzymes of known structure]]