EC 18.104.22.168 - Arylesterase
IntEnz Enzyme Nomenclature
17309 [IUBMB]a phenyl acetatea phenyl acetateGENERIC:11449Is ROOT: no
ROOT compound: GENERIC:11403Number of residues: 1H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)<?>a phenola phenolGENERIC:11405Is ROOT: no
ROOT compound: GENERIC:11403Number of residues: 1acetateacetateName origin: UniProt - CHECKED (C)Formula: C2H3O2
Charge: -1ChEBI compound status: CHECKED (C)
Acts on many phenolic esters. The reactions of EC 22.214.171.124 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 .
Links to other databases
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).
Esterases in the milk and blood of swine. I. Substrate specificity and electrophoresis studies.Biochem. J. 71: 477-484 (1959).
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]
Nonserine esterases from rat liver cytosol.Protein Expr. Purif. 1: 19-27 (1990).
Distinction between 'A'-esterases and arylesterases. Implications for esterase classification.Biochem. J. 245: 293-296 (1987). [PMID: 2822017]
In: Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.) Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood, Chichester, UK, 1989
Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase.Biochemistry 44: 6371-6382 (2005). [PMID: 15835926]
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.J. Lipid Res. 46: 1239-1247 (2005). [PMID: 15772423]
[EC 126.96.36.199 created 1961, modified 1989]