. Author manuscript; available in PMC: 2015 Nov 14.

Published in final edited form as: Biochem Biophys Res Commun. 2014 Oct 19;454(2):308–312. doi: 10.1016/j.bbrc.2014.10.070

Table 1.

Apparent Michaelis-Menten constants for the three forms of ATPase of EcSecA in the presence of RB. Experimental conditions were as Figure 1. The values of K_m and V_max were determined by nonlinear regression analysis by Prism 5 (GraphPad Software, La Jolla, CA).

			RB concentration

			0 μM	20 μM	40 μM

Intrinsic	High [ATP] Low [ATP]	V_max^† K_m(mM) V_max† K_m(mM)	7.37 1.68±0.21 3.07±0.16 0.14	6.08 1.68±0.21 3.07±0.16 0.25	3.99 1.68±0.21 3.07±0.16 0.46

			0 μM	2 μM	4 μM

Membrane		V_max^† K_m(mM)	26.95 0.31±0.03	13.61 0.31±0.03	8.18 0.31±0.03

			0 μM	0.75 μM	1 μM

Translocation		V_max^† K_m(mM)	57.27 0.18±0.01	23.42 0.18±0.01	15.06 0.18±0.01

^†

Unit: molePi·moleSecA⁻¹min⁻¹