Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor B for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor B (plus the control, with zero mM of inhibitor B). The following Table lists the inhibitor B concentrations [I], substrate concentrations [S], and resulting enzyme velocities (Vo) for all six of these experiments:   [I] [S] Vo 1/[S] 1/ Vo 0 mM 0.1 mM 0.333333333333 mM per minute     0 mM 0.2 mM 0.50     0 mM 0.3 mM 0.60     0 mM 0.4 mM 0.666666666667     0 mM 0.5 mM 0.714285714286     0.1 mM 0.1 mM 0.25     0.1 mM 0.2 mM 0.333333333333     0.1 mM 0.3 mM 0.375     0.1 mM 0.4 mM 0.40     0.1 mM 0.5 mM 0.416666666667     0.20 mM 0.1 mM 0.20     0.20 mM 0.2 mM 0.25     0.20 mM 0.3 mM 0.272727272727     0.20 mM 0.4 mM 0.285714285714     0.20 mM 0.5 mM 0.294117647059     0.3 mM 0.1 mM 0.166666666667     0.3 mM 0.2 mM 0.20     0.3 mM 0.3 mM 0.214285714286     0.3 mM 0.4 mM 0.222222222222     0.3 mM 0.5 mM 0.227272727273     0.40 mM 0.1 mM 0.142857142857     0.40 mM 0.2 mM 0.166666666667     0.40 mM 0.3 mM 0.176470588235     0.40 mM 0.4 mM 0.181818181818     0.40 mM 0.5 mM 0.185185185185     0.5 mM 0.1 mM 0.125     0.5 mM 0.2 mM 0.142857142857     0.5 mM 0.3 mM 0.150     0.5 mM 0.4 mM 0.153846153846     0.5 mM 0.5 mM 0.15625     Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor B ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor B?

Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor B for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor B (plus the control, with zero mM of inhibitor B). The following Table lists the inhibitor B concentrations [I], substrate concentrations [S], and resulting enzyme velocities (Vo) for all six of these experiments:

Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor B ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor B?