Problem Set: Enzymes and Enzyme Kinetics

1. In an enzyme catalyzed reaction, if the transition state has lower free energy than that of the products,
what will be the outcome of the reaction?
a) Enzyme catalyzed reaction will be faster than uncatalyzed reaction
b) Enzyme will not bind to substrate
c) Reaction will not proceed beyond enzyme-substrate complex formation
d) Enzyme will catalyze product formation but they will remain bound to the enzyme

3. A Methanol poisoning is treated with ethanol which actually slows down the formation of
formaldehyde. This is an example of
a) Competitive inhibition b) Uncompetitive inhibition
c) Allosteric regulation d) Non-competitive inhibition

4.Effect of a reversible competitive inhibitor can be nullified by

a) increasing enzyme concentration b) increasing substrate concentration
c) increasing product concentration d) increasing temperature

5. If the reaction A + B C is first order with respect to A and first order with respect to B, then the rate
equation for the forward reaction would be
a) Rate=k[A] b) Rate=k[B]
c) Rate=k[A][B] d) Rate=ka[A]+kb[B]

6. An allosteric inhibitor of an enzyme usually

a) denatures the enzyme b) causes the enzyme to work faster
c) binds to the active site d) changes the conformation of the active site

7. Which of the following statements about Michaelis constant (KM) of an enzyme is correct?
a) It is defined as the concentration of substrate required for the reaction to reach maximum velocity
b) It is defined as the dissociation constant of the enzyme-substrate complex
c) It is expressed in terms of the reaction velocity
d) It is a measure of the affinity the enzyme has for its substrate

8. For an efficient enzyme, what relative values of KM and kcat are correct?
(a) Low KM and high kcat (b) High KM and high kcat
(c) High KM and low kcat (d) Low KM and low kcat