Reference no: EM1340132
1. What are the intermediate( s) in an enzyme catalyzed reaction? The superscript'" sign indicates a transition state.
a. ES, EX'" and EP
b. ES and EP
c. EX'"
d. EP
2. A hypothetical enzyme in which the active site is complementary to the substrate will:
a. Increase the rate of the reaction.
b. Decrease the rate of the reaction.
c. Have no effect on the rate of the reaction.
d. Change the equilibrium constant for the reaction.
3. Enzymes have active sites which are complementary to:
a. The substrate
b. The product
c. The transition state
d. Both the substrate and the product
4. For an efficient enzyme, the complementary fit of the enzyme is optimum with the:
a. Transition state
b. Substrate
c. Product
d. Substrate & product
5. Stabilization of which species, relative to all others, is essential for enzyme catalysis?
a. Transition state
b. ES intermediate
c. EP intermediate
d. Both ES and EP
The good transition state analog is one which would serve also as an effective;
a. Competitive inhibitor
b. Noncompetitive inhibitor
c. Allosteric effector
d. Uncompetitive inhibitor
8. Covalent catalysis is carried out by enzymes using a:
a. Ping-pong mechanism
b. Sequential bisubstrate mechanism
c. Random bisubstrate mechanism
d. Simple unimolecular mechanism
9. The reactive group in the enzyme, elastase, is: a.Serine
b. Cysteine
c. Histidine
d. Aspartic acid
10. In the list below, the most effective group in effecting general acidlbasecatalysis in enzymes IS:
a. Asparagine
b. Serine
c. Histidine
d. lysine
11. The catalytic triad which is found in elastase involves the shuttling of protons from:
a. Ser-his-asp
b. Ser-his-his
c. Cys-his-glu
d. Ser-asp-his