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. 2015 Jan 21;10(1):e0116898. doi: 10.1371/journal.pone.0116898

Table 1. Kinetic parameters for catalysis by wild-type PTEN, K13A PTEN, and PTEN-La.

Enzyme [NaCl] (mM) kcat/KM (μM–1min–1)b kcat (min–1) KM (μM) hc
Wild-type PTEN 0 174 ± 40 4000 ± 300 23 ± 5 1.00 ± 0.14
100 108 ± 14c 2720 ± 130c 25 ± 3c 1.54 ± 0.16
200 20 ± 4c 1430 ± 200c 70 ± 11c 2.93 ± 0.92
K13A PTEN 0 1.4 ± 0.4 91 ± 9 64 ± 16 1.25 ± 0.33
100 1.0 ± 0.3 101 ± 12 100 ± 25 1.36 ± 0.35
200 0.39 ± 0.13 139 ± 24 359 ± 96 1.35 ± 0.21
PTEN-L 0 100 ± 25 477 ± 28 4.8 ± 1.1 0.84 ± 0.30
100 42 ± 8 515 ± 30 12 ± 2 1.23 ± 0.31
200 10 ± 2 477 ± 40 47 ± 8 1.19 ± 0.17

a Reactions were performed in 50 mM Tris–HCl buffer, pH 7.6, containing NaCl (0, 100, or 200 mM), EDTA (2.0 mM), MESG (0.20 mM), and DTBA (40 mM), and were initiated with the addition of PTEN to 20 nM.

b Values (± SE) were derived by fitting initial velocity data to eq 1, unless noted otherwise.

c Values (± SE) were derived by fitting initial velocity data to eq 2, and include k cat/K 0.5 and K 0.5 rather than k cat/K M and K M.