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Table 3 Steady state kinetic analysis of FtsZ, FtsZ84 and FtsZ84*. GTPase assays were carried out in identical conditions as the standard GTPase assay (Table 2) except GTP concentration was varied and the reactions were performed room temperature (50 mM MES, pH 6.5, 50 mM KCl, 2.5 mM MgCl2, 1 mM EGTA, 0.25-4.0 mM GTP, 22 °C). Km and Vmax values were determined by fitting the data points to a Hill-modified Michaelis-Menten equation (see Fig.4 for the data and curve fitting of each protein)

From: Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function

FtsZ species Km (mM) Vmax (GTP/FtsZ/min) n
FtsZ (wild type) 1.3 ± 0.18 17 ± 1.9 2.2 ± 0.56
FtsZ84 (G105S) 3.6 ± 0.79 12 ± 3.6 3 ± 1.1
FtsZ84*F39L 0.5 ± 0.14 6 ± 1.1 1.2 ± 0.32
FtsZ84*M206I 0.5 ± 0.26 6 ± 1.9 1.5 ± 0.70
FtsZ84*V293I 0.57 ± 0.069 5.0 ± 0.83 4 ± 2.7