Arylesterase

arylesterase
Identifiers
EC no.	3.1.1.2
CAS no.	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

In enzymology, an arylesterase (EC 3.1.1.2) is an enzyme that catalyzes the chemical reaction

a phenyl acetate + H₂O $\rightleftharpoons$ 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 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. PMC 1198110. PMID 13032041.
• AUGUSTINSSON KB, OLSSON B (1959). "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies". Biochem. J. 71 (3): 477–84. PMC 1196820. 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.
• Kim DH, Yang YS, Jakoby WB (1990). "Nonserine esterases from rat liver cytosol". Protein. Expr. Purif. 1 (1): 19–27. doi:10.1016/1046-5928(90)90040-6. PMID 2152179.
• Mackness MI, Thompson HM, Hardy AR, Walker CH (1987). "Distinction between 'A'-esterases and arylesterases. Implications for esterase classification". Biochem. J. 245 (1): 293–6. PMC 1148115. PMID 2822017.
• Khersonsky O, Tawfik DS (Apr 2005). "Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase". Biochemistry. 44: 6371–82. doi:10.1021/bi047440d. PMID 15835926.
• Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN (June 2005). "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". J. Lipid Res. 46: 1239–47. doi:10.1194/jlr.M400511-JLR200. PMID 15772423.{{cite journal}}: CS1 maint: unflagged free DOI (link)
• "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities". The Journal of Lipid Research. 46: 1239–1247. doi:10.1194/jlr.m400511-jlr200.{{cite journal}}: CS1 maint: unflagged free DOI (link)