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. 2014 Mar 24;9(3):e92257. doi: 10.1371/journal.pone.0092257

Table 3. Kinetic parameters for pNPA and pNPB hydrolysis by LpEst1.

Substrate Vmax (μmol min−1 mg−1) Km (mM) kcat (s−1) kcat/Vmax (s−1 mM−1)
pNPA 75±4 0.38±0.05 40.4±2.0 106±12
pNPB 8±1 0.2±0.1 4.4±0.3 14.7±3.3

Enzyme activities were determined at 30 °C in 50 mM sodium phosphate buffer, pH 7.0. Results are the mean value ± SD from three independent experiments.