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Comprehensive Study Guide- Solved Exam Q&A
BIOCHEM - Ch7 |2025-2026 LATEST UPDATED| 75 REAL EXAM AND
COMPLETE QUESTIONS AND ANSWERS | 100% RATED CORRECT |
100% VERFIED | ALREADY GRADED A+
Which of the following best describes negative cooperativity?
A. Binding of one substrate molecule prevents the enzyme from working at all.
B. Binding of one substrate molecule inhibits the binding of a second substrate.
C. Binding of one substrate molecule enhances the binding of a second substrate.
D. Binding of one substrate molecule inhibits the binding of other effectors. - (answer)B.
Binding of one substrate molecule inhibits the binding of a second substrate.
The saturation curve for aspartyl transcarbamylase has a similar shape to the curve for:
A. Myoglobin
B. Hemoglobin
C. Chymotrypsin
D. Both hemoglobin and chymotrypsin.
E. All of these. - (answer)B. Hemoglobin
CTP is a known inhibitor of ATCase, the enzyme that catalyzes the first reaction in the pathway
for the synthesis of this compound. This is an example of
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Comprehensive Study Guide- Solved Exam Q&A
A. irreversible inhibition
B. feedback inhibition
C. zymogenic inhibition
D. negative cooperativity - (answer)B. feedback inhibition
Homotrophic effects for allosteric enzymes involve
A. the same molecule binding to different sites in the enzyme.
B. different molecules binding to the same site in an enzyme.
C. different molecules binding to different sites in the same enzyme.
D. All of these are homotrophic effects. - (answer)A. the same molecule binding to different sites
in the enzyme.
Enzyme kinetics falls into two general categories, simple saturation and cooperative kinetics.
A. True
B. False - (answer)A. True
Which of the following is a mechanism of regulating enzyme activity?
A. Feedback inhibition by product.
B. Addition or removal of phosphate groups from of the enzyme.
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Comprehensive Study Guide- Solved Exam Q&A
C. Presence of activators.
D. Activation of zymogens.
E. All of these regulate enzyme activity. - (answer)E. All of these regulate enzyme activity.
Which of the following is true
A. Allosteric enzymes are rarely important in the regulation of metabolic pathways.
B. Michaelis-Menten kinetics describe the reactions of allosteric enzymes
C. Allosteric enzymes have a hyperbolic plot of reaction rate vs. substrate concentration
D. none of these is true - (answer)D. none of these is true
Which of the following is not required in order for an enzyme to display cooperative kinetics?
A. Multiple subunits.
B. A value for the Michaelis constant, KM.
C. Allosteric sites which affect the binding of substrate to the active site.
D. Ability to display a Vmax.
E. All of these are characteristic of cooperative enzymes. - (answer)B. A value for the Michaelis
constant, KM.
In a comparison of allosteric and non-allosteric enzymes
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Comprehensive Study Guide- Solved Exam Q&A
BIOCHEM - Ch7 |2025-2026 LATEST UPDATED| 75 REAL EXAM AND
COMPLETE QUESTIONS AND ANSWERS | 100% RATED CORRECT |
100% VERFIED | ALREADY GRADED A+
Which of the following best describes negative cooperativity?
A. Binding of one substrate molecule prevents the enzyme from working at all.
B. Binding of one substrate molecule inhibits the binding of a second substrate.
C. Binding of one substrate molecule enhances the binding of a second substrate.
D. Binding of one substrate molecule inhibits the binding of other effectors. - (answer)B.
Binding of one substrate molecule inhibits the binding of a second substrate.
The saturation curve for aspartyl transcarbamylase has a similar shape to the curve for:
A. Myoglobin
B. Hemoglobin
C. Chymotrypsin
D. Both hemoglobin and chymotrypsin.
E. All of these. - (answer)B. Hemoglobin
CTP is a known inhibitor of ATCase, the enzyme that catalyzes the first reaction in the pathway
for the synthesis of this compound. This is an example of
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Comprehensive Study Guide- Solved Exam Q&A
A. irreversible inhibition
B. feedback inhibition
C. zymogenic inhibition
D. negative cooperativity - (answer)B. feedback inhibition
Homotrophic effects for allosteric enzymes involve
A. the same molecule binding to different sites in the enzyme.
B. different molecules binding to the same site in an enzyme.
C. different molecules binding to different sites in the same enzyme.
D. All of these are homotrophic effects. - (answer)A. the same molecule binding to different sites
in the enzyme.
Enzyme kinetics falls into two general categories, simple saturation and cooperative kinetics.
A. True
B. False - (answer)A. True
Which of the following is a mechanism of regulating enzyme activity?
A. Feedback inhibition by product.
B. Addition or removal of phosphate groups from of the enzyme.
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Comprehensive Study Guide- Solved Exam Q&A
C. Presence of activators.
D. Activation of zymogens.
E. All of these regulate enzyme activity. - (answer)E. All of these regulate enzyme activity.
Which of the following is true
A. Allosteric enzymes are rarely important in the regulation of metabolic pathways.
B. Michaelis-Menten kinetics describe the reactions of allosteric enzymes
C. Allosteric enzymes have a hyperbolic plot of reaction rate vs. substrate concentration
D. none of these is true - (answer)D. none of these is true
Which of the following is not required in order for an enzyme to display cooperative kinetics?
A. Multiple subunits.
B. A value for the Michaelis constant, KM.
C. Allosteric sites which affect the binding of substrate to the active site.
D. Ability to display a Vmax.
E. All of these are characteristic of cooperative enzymes. - (answer)B. A value for the Michaelis
constant, KM.
In a comparison of allosteric and non-allosteric enzymes
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