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Literature summary for 3.1.1.2 extracted from

  • Yeung, D.T.; Lenz, D.E.; Cerasoli, D.M.
    Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates (2005), FEBS J., 272, 2225-2230.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F222Y hydrolysis of phenyl acetate, but not of paraoxon Homo sapiens
H115W no hydrolysis of phenyl acetate, but hydrolysis of paraoxon. Phenyl acetate can act as an inhibitor Homo sapiens
H115W/N133S no hydrolysis of phenyl acetate, but hydrolysis of paraoxon Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
diisopropylfluorophosphate
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.61
-
phenyl acetate pH 8.0, 25°C, wild-type enzyme Homo sapiens
0.81
-
phenyl acetate pH 8.0, 25°C, mutant enzyme F222Y Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27169
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl acetate + H2O
-
Homo sapiens phenol + acetate
-
?
phenylacetate + H2O
-
Homo sapiens phenol + acetate
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.52
-
diisopropylfluorophosphate pH 8.0, 25°C, wild-type enzyme, substrate phenyl acetate Homo sapiens