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. 2013 Nov 1;288(50):36061–36072. doi: 10.1074/jbc.M113.509927

TABLE 6.

In vitro esterase activities

Esterase activity was measured from purified enzymes using pNPB and pNPA as test substrates. Km and Vmax values were calculated using Michaelis-Menten approximations. Data are mean values from three independent experiments with the respective S.D. values.

Enzyme Substrate Vmax Km
μmol/min/mg mm
Lpx1p pNPB 3.76 ± 0.54 0.89 ± 0.13
pNPA 10.94 ± 0.98 2.50 ± 0.22
Ldh1p pNPB 0.90 ± 0.15 0.89 ± 0.15
pNPA 1.26 ± 0.18 1.78 ± 0.25
Ayr1p pNPB 14.06 ± 2.23 1.52 ± 0.24
pNPA 18.50 ± 2.76 3.50 ± 0.52
Eht1p pNPB 1.01 ± 0.14 0.88 ± 0.12
pNPA 3.44 ± 0.48 2.06 ± 0.29
Ybr056wp pNPB 1.439 ± 0.22 0.81 ± 0.12
pNPA 7.02 ± 1.26 3.51 ± 0.63
Control: GST tag pNPB 0.35 ± 0.05 0.37 ± 0.05
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