Biology:Arylesterase

arylesterase
Identifiers
EC number	3.1.1.2
CAS number	9032-73-9
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

The enzyme arylesterase (EC 3.1.1.2) catalyzes the reaction

a phenyl acetate + H₂O [math]\displaystyle{ \rightleftharpoons }[/math] a phenol + 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 1V04 and 1VA4.

References

• ALDRIDGE WN (1953). "Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate, and a method for their determination". Biochem. J. 53 (1): 110–7. doi:10.1042/bj0530110. PMID 13032041. 
• "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies". Biochem. J. 71 (3): 477–84. 1959. doi:10.1042/bj0710477. PMID 13638253. 
• Bosmann HB (1972). "Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate". Biochim. Biophys. Acta 276 (1): 180–91. doi:10.1016/0005-2744(72)90019-8. PMID 5047702. 
• "Nonserine esterases from rat liver cytosol". Protein Expr. Purif. 1 (1): 19–27. 1990. doi:10.1016/1046-5928(90)90040-6. PMID 2152179. 
• "Distinction between 'A'-esterases and arylesterases. Implications for esterase classification". Biochem. J. 245 (1): 293–6. 1987. doi:10.1042/bj2450293. PMID 2822017. 
• "Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.". Biochemistry 44 (16): 6371–82. Apr 2005. doi:10.1021/bi047440d. PMID 15835926. 
• "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". J. Lipid Res. 46 (6): 1239–47. June 2005. doi:10.1194/jlr.M400511-JLR200. PMID 15772423. 
• "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". The Journal of Lipid Research 46 (6): 1239–1247. June 2005. doi:10.1194/jlr.m400511-jlr200. PMID 15772423.