BIL 150 Metabolism Exam Questions with Correct Answers
Question 1:
Consider a situation in which the enzyme is operating at optimum temperature and pHpH, and
has been saturated with substrate. What is your best option for increasing the rate of the
reaction?
Answer:
Increase the enzyme concentration.
Question 2:
Explanation: If an enzyme is saturated with substrate, and it is operating at optimum pH and
optimum temperature, there is very little that can be done except to increase the enzyme
concentration. Some enzymes can be activated further by allosteric activators, in which case
one might add some activator to the reaction. But otherwise, increasing the enzyme
concentration is the only option. A (n) inhibitor has a structure that is so similar to the substrate
that it can bond to the enzyme just like the substrate.
Answer:
competitive
Question 3:
A (n) inhibitor binds to a site on the enzyme that is not the active site. Question
Answer:
noncompetitive
Question 4:
Usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active
site, which prevents the substrate from entering the active site or prevents catalytic activity.
Answer:
irreversible
Question 5:
The competitive inhibitor competes with the substrate for the on the enzyme.
Answer:
active site
, Question 6:
When the noncompetitive inhibitor is bonded to the enzyme, the shape of the is distorted.
Answer:
enzymeEnzyme inhibitors disrupt normal interactions between an enzyme and
itsenzymeEnzyme inhibitors disrupt normal interactions between an enzyme and its
enzyme
Enzyme inhibitors disrupt normal interactions between an enzyme and its
enzyme
Enzyme inhibitors disrupt normal interactions between an enzyme and its
Question 7:
Question
Answer:
substrate
Question 8:
You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the
reaction has stopped completely. What can you do to regain the activity of the enzyme?
Answer:
The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.
Question 9:
You have an enzymatic reaction proceeding at the optimum pH and optimum temperature. You
add a competitive inhibitor to the reaction and notice that the reaction slows down.
Answer:
Add more substrate; it will outcompete the inhibitor and increase the reaction rate.
Explanation: Competitive inhibition can be overcome by adding more substrate to outcompete
the inhibitor. Many drugs used to treat different medical conditions, including hypertension,
are competitive inhibitors. It is fairly easy to make a molecule that is similar in structure to a
particular substrate because the known enzyme's shape can be used as a model of what the
molecule needs to look like. It is more difficult to make a noncompetitive inhibitor because it is
less obvious what the noncompetitive inhibitor's shape and structure should be.
Question 10:
Which of the following statements is true regarding potential energy and kinetic energy?
Answer:
Question 1:
Consider a situation in which the enzyme is operating at optimum temperature and pHpH, and
has been saturated with substrate. What is your best option for increasing the rate of the
reaction?
Answer:
Increase the enzyme concentration.
Question 2:
Explanation: If an enzyme is saturated with substrate, and it is operating at optimum pH and
optimum temperature, there is very little that can be done except to increase the enzyme
concentration. Some enzymes can be activated further by allosteric activators, in which case
one might add some activator to the reaction. But otherwise, increasing the enzyme
concentration is the only option. A (n) inhibitor has a structure that is so similar to the substrate
that it can bond to the enzyme just like the substrate.
Answer:
competitive
Question 3:
A (n) inhibitor binds to a site on the enzyme that is not the active site. Question
Answer:
noncompetitive
Question 4:
Usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active
site, which prevents the substrate from entering the active site or prevents catalytic activity.
Answer:
irreversible
Question 5:
The competitive inhibitor competes with the substrate for the on the enzyme.
Answer:
active site
, Question 6:
When the noncompetitive inhibitor is bonded to the enzyme, the shape of the is distorted.
Answer:
enzymeEnzyme inhibitors disrupt normal interactions between an enzyme and
itsenzymeEnzyme inhibitors disrupt normal interactions between an enzyme and its
enzyme
Enzyme inhibitors disrupt normal interactions between an enzyme and its
enzyme
Enzyme inhibitors disrupt normal interactions between an enzyme and its
Question 7:
Question
Answer:
substrate
Question 8:
You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the
reaction has stopped completely. What can you do to regain the activity of the enzyme?
Answer:
The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.
Question 9:
You have an enzymatic reaction proceeding at the optimum pH and optimum temperature. You
add a competitive inhibitor to the reaction and notice that the reaction slows down.
Answer:
Add more substrate; it will outcompete the inhibitor and increase the reaction rate.
Explanation: Competitive inhibition can be overcome by adding more substrate to outcompete
the inhibitor. Many drugs used to treat different medical conditions, including hypertension,
are competitive inhibitors. It is fairly easy to make a molecule that is similar in structure to a
particular substrate because the known enzyme's shape can be used as a model of what the
molecule needs to look like. It is more difficult to make a noncompetitive inhibitor because it is
less obvious what the noncompetitive inhibitor's shape and structure should be.
Question 10:
Which of the following statements is true regarding potential energy and kinetic energy?
Answer:
