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. Author manuscript; available in PMC: 2020 Nov 8.
Published in final edited form as: J Mol Biol. 2019 Aug 30;431(22):4455–4474. doi: 10.1016/j.jmb.2019.08.012

Figure 5. Catalytic Activity of TerLλ-D178N terminase.

Figure 5.

cos-cleavage nuclease, DNA packaging and steady-state ATPase activities were performed as described in Materials and Methods. Each bar represents the average of three separate experiments with error-bars indicating the standard errors in the mean. (B) Single turnover ATP hydrolysis was performed as described in Materials and Methods; the reaction was initiated by the addition of enzyme. The reaction time courses for WT (○) is well described by a single-turnover, monophasic exponential model (solid line). In contrast, TerLλ-D178N displays a significant lag phase (●), which is poorly described by the simple model (see text; dashed red line). The mutant data are better described by the three-state model that includes a slow step prior to catalysis (Equation 1, solid red line). The kinetic constants derived from non-linear regression analysis of each data set is presented in Table 3.