To determine the rate constant k and the initial rate vo of the enzymatic reaction, the student should first perform a series of experiments under varying substrate concentrations and inhibitor concentrations. The student should then analyze the data using the Michaelis-Menten equation and the Lineweaver-Burk plot.1. Michaelis-Menten equation: vo = Vmax * [A] / Km + [A] where vo is the initial rate, Vmax is the maximum rate, [A] is the substrate concentration, and Km is the Michaelis constant.2. Lineweaver-Burk plot:1/vo = Km/Vmax * 1/[A] + 1/VmaxThe Lineweaver-Burk plot is a double reciprocal plot of 1/vo against 1/[A]. The slope of the plot is Km/Vmax, and the y-intercept is 1/Vmax. By performing experiments at different substrate concentrations and plotting the data, the student can determine the values of Km and Vmax.Since the enzyme is inhibited by a competitive inhibitor, the student should also perform experiments with varying inhibitor concentrations. The competitive inhibition equation is:vo = Vmax * [A] / Km * 1 + [I]/Ki + [A] where [I] is the inhibitor concentration and Ki is the inhibition constant.3. To determine the inhibition constant Ki , the student should plot the Lineweaver-Burk plot for different inhibitor concentrations. In competitive inhibition, the lines will intersect at the y-axis 1/Vmax . The slopes of the lines will change with increasing inhibitor concentration, but the y-intercept will remain the same.4. To calculate Ki, the student should compare the slopes of the lines in the presence and absence of the inhibitor. The ratio of the slopes in the presence and absence of the inhibitor is 1 + [I]/Ki . By solving for Ki, the student can determine the inhibition constant.5. Since the student already knows that the enzyme is inhibited by a competitive inhibitor, there is no need to determine the type of inhibition. Competitive inhibition is characterized by an increase in the apparent Km value while the Vmax value remains unchanged.