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Literature summary for 3.1.8.1 extracted from

  • Bajaj, P.; Tripathy, R.K.; Aggarwal, G.; Pande, A.H.
    Characterization of human paraoxonase 1 variants suggest that His residues at 115 and 134 positions are not always needed for the lactonase/arylesterase activities of the enzyme (2013), Protein Sci., 22, 1799-1807.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.8.1

Protein Variants

Protein Variants Comment Organism
L69G/S111T/H115W/H134R/R192K/F222S/T332S mutant designed for expression in Escherichia coli in soluble and active form. Mutants is more than 20fold better in hydrolyzing paraoxon substrate compared to wild-type and more than 100fold better in hydrolsis of diisopropyl fluorophosphate Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inhibition of phenyl acetate hydrolyzing activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
 paraoxon pH 8.0, temperature not specified in the publication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diisopropyl fluorophosphate + H2O
-
 Homo sapiens isopropanol + ?
-
 ?
paraoxon + H2O
-
 Homo sapiens 4-nitrophenol + diethyl phosphate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.89
-
 paraoxon pH 8.0, temperature not specified in the publication Homo sapiens