EC 3.1.1.2 - Arylesterase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.1.1.2

Names

Accepted name:
arylesterase
Other names:
A-esterase
aromatic esterase
paraoxonase
Systematic name:
aryl-ester hydrolase

Reaction

Comments:

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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004064
CAS Registry Number: 9032-73-9
UniProtKB/Swiss-Prot: (20) [show] [UniProt]

References

  1. Aldridge, W.N.
    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: 110-117 (1953).
  2. Augustinsson, K.-B. and Olsson, B.
    Esterases in the milk and blood of swine. I. Substrate specificity and electrophoresis studies.
    Biochem. J. 71: 477-484 (1959).
  3. Bosmann, H.B.
    Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate.
    Biochim. Biophys. Acta 276: 180-191 (1972). [PMID: 5047702]
  4. Kim, D.-H., Yang, Y.-S. and Jakoby, W.B.
    Nonserine esterases from rat liver cytosol.
    Protein Expr. Purif. 1: 19-27 (1990).
  5. Mackness, M.I., Thompson, H.M., Hardy, A.R. and Walker, C.H.
    Distinction between 'A'-esterases and arylesterases. Implications for esterase classification.
    Biochem. J. 245: 293-296 (1987). [PMID: 2822017]
  6. In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.) Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989
  7. Khersonsky, O. and Tawfik, D.S.
    Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.
    Biochemistry 44: 6371-6382 (2005). [PMID: 15835926]
  8. Draganov, D.I., Teiber, J.F., Speelman, A., Osawa, Y., Sunahara, R. and La Du, B.N.
    Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.
    J. Lipid Res. 46: 1239-1247 (2005). [PMID: 15772423]

[EC 3.1.1.2 created 1961, modified 1989]