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. 2016 Jul 21;63(2):337–346. doi: 10.1016/j.molcel.2016.06.012

Table 3.

Stability and Kinetic Parameters of PTE Variants

Variant Muta Normalized Activityb Inactivation Temperature (°C)
T1/2 Chelatorc (min) KM (mM)d kcat × 105 (min-1) d kcat/KM × 109 (min-1M-1) d
Lysate Purified
PTE-S5 3 1 50.9 ± 0.7 52.4 ± 0.2 7.5 ± 0.3 0.101 ± 0.023 0.970 ± 0.076 0.96 ± 0.33
dPTE1 9 2.0 54.7 ± 3.2 NDe NDe NDe NDe NDe
dPTE2 19 6.1 59.2 ± 0.7 62.0 ± 0.2 51.2 ± 5.1 0.060 ± 0.014 0.70 ± 0.05 1.17 ± 0.35
dPTE3 28 2.3 47.0 ± 1.3 NDe NDe NDe NDe NDe
a

Number of mutations relative to wild-type PTE.

b

Fold increase in activity in crude E. coli lysates relative to PTE-S5.

c

Chelator, 50 μM 1,10-phenanthroline.

d

Kinetic parameters for paraoxon.

e

ND, not determined.