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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

Table 1. Single Turnover ATPase Kinetic Analysis.

The data presented in Figure 5B were fit to a monophasic reaction time course and a three-state kinetic model as described in Materials and Methods. The derived rate constants are presented with standard deviations as indicated.

Enzyme Monophasic Model Three-State Model
kobs (s−1) k1 (M−1s−1) k2 (s−1)
WT (0.139 ± 0.016) - -
D178N (1.0 ± 0.4) x 10−3 (1.7 ± 0.2) x 104 (2.4 ± 0.1) x 10−3
R79A - (1.3 ± 0.9) x 104 (5.3 ± 2.9) x 10−3