Below is the data from his kinetic analysis of the enzyme in the absence and presence of two different inhibitors. The enzyme is known to follow Michaelis-Menton kinetics. The assay mixture contains 1 mg of enzyme in a total volume of 1.0 ml. 1. Using this data construct a Lineweaver-Burke plot and determine Vmax and Km for the enzyme alone and in the presence of each inhibitor. 2. Indicate the kind of inhibition each inhibitor demonstrates. 3. Can the action of either of these inhibitors be overcome by adding more alpha-ketoglutarate? Vo (umol/min) no inhibitor + 1mM inhibitor [a-ketoglutarate] mM + 1 mM inhibtor B A 1.5 1.23 0.88 1.04 2.0 1.43 1.06 1.18 2.5 1.61 1.23 1.30 4.0 2.00 1.60 1.52 10.0 2.63 2.30 1.85