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Literature summary for 3.1.1.2 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

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. Mutant shows about 45% of phenyl acetate hydrolyzing activity of wild-type 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
2.1
-
phenyl acetate 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.
phenyl acetate + H2O
-
Homo sapiens phenol + acetate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
843.6
-
phenyl acetate pH 8.0, temperature not specified in the publication Homo sapiens