Fig. 4.
Progress curves of reactions catalyzed by AARCAp at different NADH concentrations. The acetoacetyl-CoA concentration was fixed at 400 mM. Time scale is in seconds. The thick lines represent the global fitting, while thinner lines represent the experimental data. Best fit curves were obtained with a competitive product inhibition model. The initial concentrations of NADH and enzyme were: (1) NADH = 12 mM, Enzyme = 0.05 mM. (2) NADH = 30 mM, Enzyme = 0.05 mM. (3) NADH = 46 mM, Enzyme = 0.05 mM. (4) NADH = 77 mM, Enzyme = 0.05 mM. (5) NADH = 78 mM, Enzyme = 0.05 mM. (6) NADH = 94 mM, Enzyme = 0.05 mM. (7) NADH = 111 mM, Enzyme = 0.05 mM. (8) NADH = 136 mM, Enzyme = 0.05 mM. (9) NADH = 150 mM, Enzyme = 0.05 mM. (10) NADH = 168 mM, Enzyme = 0.05 mM. (11) NADH = 9 mM, Enzyme = 0.1 mM. (12) NADH = 20 mM, Enzyme = 0.1mM. (13) NADH = 35 mM, Enzyme = 0.1 mM. (14) NADH = 47 mM, Enzyme = 0.1 mM. (15) NADH = 78 mM, Enzyme = 0.1 mM.