. 2014 Dec 24;43(2):1098–1111. doi: 10.1093/nar/gku1337

Table 2. Steady-state kinetic parameters of RAD51-catalyzed ATP hydrolysis in the presence of ssDNA.

	WT	D149N	R150Q	G151D
k_cat (min⁻¹)	0.28 ± 0.01	0.25 ± 0.01	0.16 ± 0.01	0.17 ± 0.01
K_m (μM ATP)	20 ± 3	20 ± 3	76 ± 12	67 ± 9
k_cat/K_m (s^{−1 ×} M⁻¹)	230	210	34	41

All data were derived from computer fits of steady-state ATPase curves as shown in Figure 3A and as described in ‘Materials and Methods’ section. Each value represents the average (± standard deviation) from three different experiments.