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. 2018 Oct 26;14(10):e1007404. doi: 10.1371/journal.ppat.1007404

Table 1. Steady-state kinetics analysis of recombinant TbAdoMetSyn.

kcat (s-1) Km (mM)
ATP Methionine ATP Methionine
TbAdoMetSyn
(150 nM)		 0.21
(0.20–0.23)		 0.19
(0.18–0.19)		 0.31
(0.24–0.40)		 0.031
(0.025–0.039)
TbAdoMetSyn
(75 nM)		 0.24
(0.22–0.25)		 0.21
(0.20–0.22)		 0.35
(0.27–0.44)		 0.045
(0.034–0.061)

Data were collected in triplicate. Range in parenthesis represents 95% confidence interval. kcat values reported are from respective substrate dose-response curves. Data were collected at two different enzyme concentrations to demonstrate that the Vmax was linearly dependent on enzyme concentration (kcat = Vmax/[E]).