WGU BIOCHEMISTRY FINAL REVIEW ACTUAL EXAM
NEWEST VERSION QUESTION AND CORRECT
DETAILED VERIFIED ANSWERS
2026/2027 Frequently Most Tested Questions and
100% Accurate From Past papers | Graded A+ ,
Reviewed and Updated | 100% Guarantee Pass | Latest
Exam and Newest Version!!!
A client with chronic myelogenous leukemia (CML) has a genetic mutation that results in
the production of the BCR-ABL enzyme, which accelerates cell division by utilizing ATP
as a substrate. The drug Gleevec (imatinib) is prescribed to impair the activity of this
enzyme. Based on the illustrations of the enzyme provided, which of the following best
describes the mechanism by which this drug exerts its therapeutic effect?
a. Gleevec is a competitive inhibitor that prevents ATP from binding to the active site of
the enzyme.
b. Gleevec is a competitive inhibitor that binds to an allosteric site on the enzyme to
prevent ATP from binding to the active site.
c. Gleevec is a non-competitive inhibitor that prevents ATP from binding to the active
site of an enzyme.
,d. Gleevec is a non-competitive inhibitor that binds to an allosteric site on the enzyme
to prevent ATP from binding to the active site.
✔️ Correct Answer: A
Rationale: Gleevec functions as a competitive inhibitor. It binds to the same active site
on the BCR-ABL enzyme where ATP, the substrate, would typically bind. By occupying
this site, Gleevec directly blocks ATP from accessing the enzyme's catalytic pocket,
thereby preventing the phosphorylation activity that drives cell division. This is a classic
example of competitive inhibition, which can often be overcome by increasing substrate
concentration.
A nurse is reviewing the schematic of the synthesis and degradation of acetylcholine, an
important neurotransmitter. If a drug is designed to keep the concentration of
acetylcholine high in the synaptic cleft, where should the inhibitor target?
a. Acetylcholine
b. Choline acetyltransferase
c. Choline
d. Acetylcholinesterase
✔️ Correct Answer: D
Rationale: Acetylcholinesterase is the enzyme responsible for the breakdown of
acetylcholine into acetate and choline. By inhibiting this specific enzyme, the
degradation of acetylcholine is prevented, which leads to a higher and more prolonged
concentration of the neurotransmitter at the synapse. This is a common mechanism of
action for drugs used to treat myasthenia gravis and Alzheimer's disease.
A patient presents with a deficiency in the enzyme phenylalanine hydroxylase, a
condition known as Phenylketonuria (PKU). Which of the following is the most likely
consequence of this enzyme deficiency?
a. Phenylalanine levels will decrease.
b. Tyrosine levels will increase.
, c. Phenylalanine levels will increase.
d. There will be no change in phenylalanine or tyrosine levels.
✔️ Correct Answer: C
Rationale: In PKU, the enzyme phenylalanine hydroxylase is deficient or non-functional.
This enzyme is responsible for converting the substrate phenylalanine into the product
tyrosine. When an enzyme is deficient, its substrate will accumulate. Therefore,
phenylalanine levels will increase, which is toxic to the developing brain, while tyrosine
levels will decrease as they are not being synthesized.
A patient with Phenylketonuria (PKU) presents with elevated phenylalanine levels, which
is toxic to the developing brain. Using the provided schematic of the metabolic pathway,
which of the following suggestions would best alleviate the problems associated with
this condition?
a. Supplement phenylalanine in the diet.
b. Increase the activity of phenylalanine hydroxylase.
c. Decrease the activity of phenylalanine hydroxylase.
d. Supplement tyrosine in the diet.
✔️ Correct Answer: B
Rationale: The goal is to reduce phenylalanine levels. Since phenylalanine is the
substrate for phenylalanine hydroxylase, increasing the activity of this enzyme would
facilitate the conversion of more phenylalanine into tyrosine, thereby decreasing its toxic
accumulation. While supplementing tyrosine may help with product deficiency, it does
not address the root problem of phenylalanine buildup.
In the reaction where glucose is converted to glucose-6-phosphate, the product
glucose-6-phosphate accumulates in the cell and binds to hexokinase at a site distinct
from the active site. This binding inhibits hexokinase from binding to its substrate. What
happens to the amount of glucose in the cell once hexokinase is inhibited?
NEWEST VERSION QUESTION AND CORRECT
DETAILED VERIFIED ANSWERS
2026/2027 Frequently Most Tested Questions and
100% Accurate From Past papers | Graded A+ ,
Reviewed and Updated | 100% Guarantee Pass | Latest
Exam and Newest Version!!!
A client with chronic myelogenous leukemia (CML) has a genetic mutation that results in
the production of the BCR-ABL enzyme, which accelerates cell division by utilizing ATP
as a substrate. The drug Gleevec (imatinib) is prescribed to impair the activity of this
enzyme. Based on the illustrations of the enzyme provided, which of the following best
describes the mechanism by which this drug exerts its therapeutic effect?
a. Gleevec is a competitive inhibitor that prevents ATP from binding to the active site of
the enzyme.
b. Gleevec is a competitive inhibitor that binds to an allosteric site on the enzyme to
prevent ATP from binding to the active site.
c. Gleevec is a non-competitive inhibitor that prevents ATP from binding to the active
site of an enzyme.
,d. Gleevec is a non-competitive inhibitor that binds to an allosteric site on the enzyme
to prevent ATP from binding to the active site.
✔️ Correct Answer: A
Rationale: Gleevec functions as a competitive inhibitor. It binds to the same active site
on the BCR-ABL enzyme where ATP, the substrate, would typically bind. By occupying
this site, Gleevec directly blocks ATP from accessing the enzyme's catalytic pocket,
thereby preventing the phosphorylation activity that drives cell division. This is a classic
example of competitive inhibition, which can often be overcome by increasing substrate
concentration.
A nurse is reviewing the schematic of the synthesis and degradation of acetylcholine, an
important neurotransmitter. If a drug is designed to keep the concentration of
acetylcholine high in the synaptic cleft, where should the inhibitor target?
a. Acetylcholine
b. Choline acetyltransferase
c. Choline
d. Acetylcholinesterase
✔️ Correct Answer: D
Rationale: Acetylcholinesterase is the enzyme responsible for the breakdown of
acetylcholine into acetate and choline. By inhibiting this specific enzyme, the
degradation of acetylcholine is prevented, which leads to a higher and more prolonged
concentration of the neurotransmitter at the synapse. This is a common mechanism of
action for drugs used to treat myasthenia gravis and Alzheimer's disease.
A patient presents with a deficiency in the enzyme phenylalanine hydroxylase, a
condition known as Phenylketonuria (PKU). Which of the following is the most likely
consequence of this enzyme deficiency?
a. Phenylalanine levels will decrease.
b. Tyrosine levels will increase.
, c. Phenylalanine levels will increase.
d. There will be no change in phenylalanine or tyrosine levels.
✔️ Correct Answer: C
Rationale: In PKU, the enzyme phenylalanine hydroxylase is deficient or non-functional.
This enzyme is responsible for converting the substrate phenylalanine into the product
tyrosine. When an enzyme is deficient, its substrate will accumulate. Therefore,
phenylalanine levels will increase, which is toxic to the developing brain, while tyrosine
levels will decrease as they are not being synthesized.
A patient with Phenylketonuria (PKU) presents with elevated phenylalanine levels, which
is toxic to the developing brain. Using the provided schematic of the metabolic pathway,
which of the following suggestions would best alleviate the problems associated with
this condition?
a. Supplement phenylalanine in the diet.
b. Increase the activity of phenylalanine hydroxylase.
c. Decrease the activity of phenylalanine hydroxylase.
d. Supplement tyrosine in the diet.
✔️ Correct Answer: B
Rationale: The goal is to reduce phenylalanine levels. Since phenylalanine is the
substrate for phenylalanine hydroxylase, increasing the activity of this enzyme would
facilitate the conversion of more phenylalanine into tyrosine, thereby decreasing its toxic
accumulation. While supplementing tyrosine may help with product deficiency, it does
not address the root problem of phenylalanine buildup.
In the reaction where glucose is converted to glucose-6-phosphate, the product
glucose-6-phosphate accumulates in the cell and binds to hexokinase at a site distinct
from the active site. This binding inhibits hexokinase from binding to its substrate. What
happens to the amount of glucose in the cell once hexokinase is inhibited?
