For a Michaelis-Menten deacetylase with a Ks for substrate binding of 2.6 x μM, half maximal velocity is achieved with a substrate concentration of 2.8 μM. a. What is Km for the deacetylase and what kind of kinetics does this enzyme follow: rapid equilibrium or just the general steady state? Justify your answer. b. How many times larger is the reverse rate constant for substrate binding, k-1, than the catalytic rate constant for this deacetylase? c. How many times larger is the rate constant for substrate binding k1 than the catalytic rate constant? d. In a reaction with a substrate concentration of 4.5 μM and enough deacetylase to achieve a Vmax of 10 nM/min, what is the initial velocity of the deacetylation? e. If the amount of enzyme in part d was 10 pM, and there are 2 active sites per enzyme, what is the efficiency of the enzyme? Is it a perfect enzyme? Justify your answer.