WGU BIOCHEMISTRY FINAL REVIEW QUESTIONS & ANSWERS
1. Gleevec is a competitive inhibitor and prevents ATP from binding with
the active site of the enzyme.
Competitive inhibitors bind to an enzyme in the active site. Gleevec is
binding in the same site as ATP. ATP is the substrate, to the site of ATP
binding must be the active site. Gleevec is therefore is binding the active
site and is a competitive inhibitor.
If you chose, "Gleevac is a non-competitive inhibitor..." this is incorrect
because non-competitive inhibitors bind at a site different than the
active site. In the figure it can be seen that Gleevac binds the same site
on the enzyme as the substrate (ATP). This means that Gleevac is binding
the active site.
If you chose "Gleevac is a competitive inhibitor that binds to an allosteric
site...", this is incorrect because competitive inhibitors bind the active
site, not an allosteric site. - CORRECT ANSWER - Patients with chronic
mylogenous leukemia (CML) have a mutation that results in the
production of BCR-ABL, an enzyme that speeds up cell division using ATP
as a substrate. The drug Gleevec impairs the activity of the enzyme.
Using the illustrations of the enzyme above, what best describes how
the drug exerts its effect?
,1. Gleevec is a competitive inhibitor and prevents ATP from binding with
the active site of the enzyme.
2. Gleevec is a competitive inhibitor that binds to an allosteric site on the
enzyme to prevent ATP from binding to the active site.
3. Gleevec is a non competitive inhibitor and prevents ATP from binding
with the active site of an enzyme.
4. Gleevec is a non competitive inhibitor that binds to an allosteric site
on the enzyme to prevent ATP from binding to the active site.
1. The polymerase chain reaction is a tool used to study protein
structure.
True
False - CORRECT ANSWER - False
Feedback
PCR is a tool used to amplify a specific segment of DNA.
13. Myoglobin and hemoglobin each have different numbers of subunits
and this affects their respective oxygen storage and delivery capabilities.
How many subunits does myoglobin have versus hemoglobin?
,One, Four
Two, Three
One, Two
Four, One - CORRECT ANSWER - One, Four
Feedback
Correct! Myoglobin has one subunit and hemoglobin has four subunits.
2 ATP are generated when glucose is broken down in the muscle cell and
6 ATP are consumed when glucose is regenerated in the liver.
Feedback
2 ATP are generated when glucose is broken down in the muscle cell
(through glycolysis) and 6 ATP are consumed when ATP is regenerated in
the liver (through gluconeogenesis. - CORRECT ANSWER - The figure
of the Cori Cycle below demonstrates how glucose is consumed in the
muscle cell and regenerated in the liver. How many ATP are produced in
the muscle cell when glucose is broken down and how many ATP are
consumed in the liver when glucose is regenerated?
2 ATP are generated when glucose is broken down in the muscle cell and
6 ATP are consumed when glucose is regenerated in the liver.
, 2 ATP are generated when glucose is broken down in the muscle cell and
4 ATP are consumed when glucose is regenerated in the liver.
6 ATP are generated when glucose is broken down in the muscle cell and
2 ATP are consumed when glucose is regenerated in the liver.
30 ATP are generated when glucose is broken down in the muscle cell
and 6 ATP are consumed when glucose is regenerated in the liver.
2. Increase activity of phenylalanine hydroxylase.
Feedback
Correct! Increase activity of phenylalanine hydroxylase.
Increased phenylalanine levels lead to phenylketonuria, so symptoms
can be relieved by decreasing the level of phenylalanine. By increasing
the activity of the enzyme that uses phenylalanine, phenylalanine
hydroxylase, we can decrease the phenylalanine levels. - CORRECT
ANSWER - Phenylalanine is toxic to the developing brain. Using the
following schematic, propose a suggestion to alleviate the problems
associated with Phenylketonuria.
1. Supplement phenylalanine in the diet.
2. Increase activity of phenylalanine hydroxylase.
3. Decrease activity of phenylalanine hydroxylase.
4. Supplement tyrosine in the diet.
1. Gleevec is a competitive inhibitor and prevents ATP from binding with
the active site of the enzyme.
Competitive inhibitors bind to an enzyme in the active site. Gleevec is
binding in the same site as ATP. ATP is the substrate, to the site of ATP
binding must be the active site. Gleevec is therefore is binding the active
site and is a competitive inhibitor.
If you chose, "Gleevac is a non-competitive inhibitor..." this is incorrect
because non-competitive inhibitors bind at a site different than the
active site. In the figure it can be seen that Gleevac binds the same site
on the enzyme as the substrate (ATP). This means that Gleevac is binding
the active site.
If you chose "Gleevac is a competitive inhibitor that binds to an allosteric
site...", this is incorrect because competitive inhibitors bind the active
site, not an allosteric site. - CORRECT ANSWER - Patients with chronic
mylogenous leukemia (CML) have a mutation that results in the
production of BCR-ABL, an enzyme that speeds up cell division using ATP
as a substrate. The drug Gleevec impairs the activity of the enzyme.
Using the illustrations of the enzyme above, what best describes how
the drug exerts its effect?
,1. Gleevec is a competitive inhibitor and prevents ATP from binding with
the active site of the enzyme.
2. Gleevec is a competitive inhibitor that binds to an allosteric site on the
enzyme to prevent ATP from binding to the active site.
3. Gleevec is a non competitive inhibitor and prevents ATP from binding
with the active site of an enzyme.
4. Gleevec is a non competitive inhibitor that binds to an allosteric site
on the enzyme to prevent ATP from binding to the active site.
1. The polymerase chain reaction is a tool used to study protein
structure.
True
False - CORRECT ANSWER - False
Feedback
PCR is a tool used to amplify a specific segment of DNA.
13. Myoglobin and hemoglobin each have different numbers of subunits
and this affects their respective oxygen storage and delivery capabilities.
How many subunits does myoglobin have versus hemoglobin?
,One, Four
Two, Three
One, Two
Four, One - CORRECT ANSWER - One, Four
Feedback
Correct! Myoglobin has one subunit and hemoglobin has four subunits.
2 ATP are generated when glucose is broken down in the muscle cell and
6 ATP are consumed when glucose is regenerated in the liver.
Feedback
2 ATP are generated when glucose is broken down in the muscle cell
(through glycolysis) and 6 ATP are consumed when ATP is regenerated in
the liver (through gluconeogenesis. - CORRECT ANSWER - The figure
of the Cori Cycle below demonstrates how glucose is consumed in the
muscle cell and regenerated in the liver. How many ATP are produced in
the muscle cell when glucose is broken down and how many ATP are
consumed in the liver when glucose is regenerated?
2 ATP are generated when glucose is broken down in the muscle cell and
6 ATP are consumed when glucose is regenerated in the liver.
, 2 ATP are generated when glucose is broken down in the muscle cell and
4 ATP are consumed when glucose is regenerated in the liver.
6 ATP are generated when glucose is broken down in the muscle cell and
2 ATP are consumed when glucose is regenerated in the liver.
30 ATP are generated when glucose is broken down in the muscle cell
and 6 ATP are consumed when glucose is regenerated in the liver.
2. Increase activity of phenylalanine hydroxylase.
Feedback
Correct! Increase activity of phenylalanine hydroxylase.
Increased phenylalanine levels lead to phenylketonuria, so symptoms
can be relieved by decreasing the level of phenylalanine. By increasing
the activity of the enzyme that uses phenylalanine, phenylalanine
hydroxylase, we can decrease the phenylalanine levels. - CORRECT
ANSWER - Phenylalanine is toxic to the developing brain. Using the
following schematic, propose a suggestion to alleviate the problems
associated with Phenylketonuria.
1. Supplement phenylalanine in the diet.
2. Increase activity of phenylalanine hydroxylase.
3. Decrease activity of phenylalanine hydroxylase.
4. Supplement tyrosine in the diet.
