“Arylesterase”的意思、由来-开放百科全书

词条

Arylesterase

释义

Structural studies
References

{{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 catalyzes the chemical reaction

a phenyl acetate + H₂O a phenol + acetate

Thus, the two substrates of this enzyme are phenyl acetate and H₂O, whereas its two products are phenol and acetate.

This enzyme belongs to the family of hydrolases, 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 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1V04}} and {{PDB link|1VA4}}.

References

{{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 = 110–7 | pmid = 13032041 | issue = 1 | pmc = 1198110 | doi=10.1042/bj0530110}}
{{cite journal | vauthors = 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 = 477–84 | 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 = 180–91 | pmid = 5047702 | issue = 1 | doi=10.1016/0005-2744(72)90019-8}}
{{cite journal | vauthors = Kim DH, Yang YS, Jakoby WB | date = 1990 | title = Nonserine esterases from rat liver cytosol | journal = Protein. Expr. Purif. | volume = 1 | pages = 19–27 | pmid = 2152179 | doi = 10.1016/1046-5928(90)90040-6 | issue = 1 }}
{{cite journal | vauthors = 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 = 293–6 | pmid = 2822017 | issue = 1 | pmc = 1148115 | doi=10.1042/bj2450293}}
{{cite journal | vauthors = Khersonsky O, Tawfik DS | date = Apr 2005| title = Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.|PMID=15835926 | journal = Biochemistry | volume = 44| pages = 6371–82| doi=10.1021/bi047440d}}
{{cite journal | date = June 2005| title = Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities|PMID=15772423 | vauthors = Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN | volume = 46| pages = 1239–47| doi=10.1194/jlr.M400511-JLR200 | journal=J. Lipid Res.}}
{{cite journal | doi = 10.1194/jlr.m400511-jlr200 | volume=46 | title=Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities | journal=The Journal of Lipid Research | pages=1239–1247 | pmid=15772423 | date=June 2005 | vauthors=Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN}}

2 : EC 3.1.1|Enzymes of known structure

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