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. 2014 Sep 15;33(21):2547–2563. doi: 10.15252/embj.201488517

Table 3.

Intrinsic GTPase activities of wt and mutant ctelF5B(517–858) and ecEF-Tu

Protein Construct KCl (mM) k (min−1) Fold reduction compared to wild-type at 200 mM KCl
ctelF5B wt 200 0.023 ± 0.0015
wt 0 0.0021 ± 0.001 11
D533A 200 0.0018 ± 0.0005 13
D533A 0 0.0016 ± 0.0008 14
D533N 200 0.017 ± 0.002 1.4
D533R 200 0.0028 ± 0.0007 8
ecEF-Tu wt 200 0.026 ± 0.0005
wt 0 0.003 ± 0.0002 9
D21A 200 0.0035 ± 0.0008 7
D21A 0 0.0041 ± 0.0001 6

Measurements were performed two to three times.

k, rate of GTP hydrolysis under the used experimental conditions.

Measured under multiple turnover conditions at 35°C.

Measured under single turnover conditions at 30°C.