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.