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. Author manuscript; available in PMC: 2010 May 26.
Published in final edited form as: Biochemistry. 2009 May 26;48(20):4305–4313. doi: 10.1021/bi9003759

Figure 1.

Figure 1

Oxamate inhibition of the bicarbonate-dependent ATPase reaction catalyzed by wild-type (●), K1119Q (▲) and T882A (■) RePC. (a) Initial rates were determined and data for the wild-type enzyme were fitted to the equation for substrate inhibition (eqn 2), omitting the initial data point for zero oxamate concentration. The partial inhibition data observed for the T882A mutant were fitted to eqn 3. (b) Reciprocal plot of the initial rates vs. oxamate concentration for the wild-type enzyme where vo is the initial rate in the absence of oxamate and vi is the rate determined in the presence of oxamate.