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Table 3 Activities of AbOPH and AbOPHI211A toward various substrates

From: Marked enhancement of Acinetobacter sp. organophosphorus hydrolase activity by a single residue substitution Ile211Ala

Substrates AbOPH (μmol min−1 mg−1) AbOPHI211A (μmol min−1 mg−1)
Phosphoesters
 Methyl-parathion ND 1.68 ± 0.08
 Ethyl-paraoxon ND 0.072 ± 0.012
 Fenitrothion 0.048 ± 0.011 0.543 ± 0.045
 Malathion ND ND
 Dimethoate ND ND
 Diazinon ND ND
Lactones
 3,4-Dihydrocoumarin 996 ± 22 389 ± 10
 δ-Decanolactone 54.1 ± 6.1 3.74 ± 0.56
 γ-Nonanolactone 14.8 ± 2.0 1.64 ± 0.12
Esters
 para-Nitrophenyl butyrate 3.73 ± 0.11 3.04 ± 0.50
 2-Naphthyl acetate 3.52 ± 0.46 2.53 ± 0.16
  1. Data were obtained with purified proteins
  2. ND no enzymatic activity was detected except spontaneous hydrolysis regardless of the high enzyme loading (2 mg/mL)