Reference no: EM132293242

Question 1. In class, we measured the activity of "flipase" as a function of increasing substrate concentration (number of cards). In the experiment, the concentration of enzyme ([E]_T) was 2.0 x 10^-6 M. The table shows the data after averaging duplicate measures and expressing activity in cards (mM) per second.

Plot these data as a Lineweaver-Burke plot (1/v_o vs 1/[S]) and attached your graph. From this graph, determine the following:

a. V_max

b. K_M

c. k_cat (expressed in s^-1)

d. k_cat/K_M (expressed in M^-1 s^-1)

Question 2. Consider performing the same reaction of flipping cards and including playing cards that looked like the actual cards but could not be flipped, i.e., a competitive inhibitor. If the competitive inhibitor was included at 1.00 mM and it has an inhibition constant (K_I) of 0.25 mM, how would this affect the V_max, the K_M, and the rate of reaction (v_o) at the lowest concentration of cards (10 mM)?

Question 3a. Based upon the value of k_cat from question 1, determine the activation energy (ΔG^‡_cat) for the catalyzed reaction (assuming T = 25°C). Show your work.

Question 3b. If our enzyme enhanced rates of reaction by 10⁹-fold, what are the first order rate constant (k_uncat) and activation energy (ΔG^‡_uncat) of the uncatalyzed reaction (at T = 25°C)?