BRAINSCAPE1
CHEM 210 Biochemistry Module 1 to 8
Exams' & Final Exam () Portage
Learning Questions and Verified Answers,
100% Guaranteed Pass ||Complete A+ Guide
1. Enzymes increase reaction rates by:
a) Increasing ΔG
b) Lowering activation energy
c) Shifting equilibrium
d) Increasing substrate concentration
2. Which molecule binds at a site other than the active site?
a) Substrate
b) Competitive inhibitor
c) Allosteric regulator
d) Cofactor
3. Vmax represents:
a) Maximum substrate concentration
b) Enzyme affinity
c) Maximum reaction velocity
d) Rate at equilibrium
4. Km is best described as:
a) Maximum velocity
b) Substrate concentration at ½ Vmax
c) Enzyme concentration
d) Turnover number
5. A low Km indicates:
a) Low enzyme efficiency
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b) High substrate affinity
c) Poor binding
d) Enzyme saturation
6. Enzyme specificity is primarily due to:
a) pH
b) Temperature
c) Active site structure
d) Cofactors
7. Which factor does NOT affect enzyme activity?
a) Temperature
b) pH
c) Light intensity
d) Inhibitors
8. Enzymes are usually:
a) Lipids
b) Carbohydrates
c) Proteins
d) Nucleic acids
9. The induced-fit model suggests:
a) Active site is rigid
b) Enzyme changes shape on binding
c) Substrate changes shape only
d) Enzymes are consumed
10. Enzyme saturation occurs when:
a) All enzymes are inactive
b) Substrate is limiting
c) All active sites are occupied
d) Km equals Vmax
Questions 11–25: Inhibition
11. Competitive inhibitors bind:
a) Only allosteric site
b) Active site
c) Cofactor site
d) Enzyme-substrate complex
12. Competitive inhibition can be overcome by:
a) Lowering substrate concentration
b) Increasing substrate concentration
c) Removing enzyme
d) Increasing pH
13. Competitive inhibitors affect:
a) Vmax only
b) Km only
BRAINSCAPE1
CHEM 210 Biochemistry Module 1 to 8
Exams' & Final Exam () Portage
Learning Questions and Verified Answers,
100% Guaranteed Pass ||Complete A+ Guide
1. Enzymes increase reaction rates by:
a) Increasing ΔG
b) Lowering activation energy
c) Shifting equilibrium
d) Increasing substrate concentration
2. Which molecule binds at a site other than the active site?
a) Substrate
b) Competitive inhibitor
c) Allosteric regulator
d) Cofactor
3. Vmax represents:
a) Maximum substrate concentration
b) Enzyme affinity
c) Maximum reaction velocity
d) Rate at equilibrium
4. Km is best described as:
a) Maximum velocity
b) Substrate concentration at ½ Vmax
c) Enzyme concentration
d) Turnover number
5. A low Km indicates:
a) Low enzyme efficiency
BRAINSCAPE1
, BRAINSCAPE1
b) High substrate affinity
c) Poor binding
d) Enzyme saturation
6. Enzyme specificity is primarily due to:
a) pH
b) Temperature
c) Active site structure
d) Cofactors
7. Which factor does NOT affect enzyme activity?
a) Temperature
b) pH
c) Light intensity
d) Inhibitors
8. Enzymes are usually:
a) Lipids
b) Carbohydrates
c) Proteins
d) Nucleic acids
9. The induced-fit model suggests:
a) Active site is rigid
b) Enzyme changes shape on binding
c) Substrate changes shape only
d) Enzymes are consumed
10. Enzyme saturation occurs when:
a) All enzymes are inactive
b) Substrate is limiting
c) All active sites are occupied
d) Km equals Vmax
Questions 11–25: Inhibition
11. Competitive inhibitors bind:
a) Only allosteric site
b) Active site
c) Cofactor site
d) Enzyme-substrate complex
12. Competitive inhibition can be overcome by:
a) Lowering substrate concentration
b) Increasing substrate concentration
c) Removing enzyme
d) Increasing pH
13. Competitive inhibitors affect:
a) Vmax only
b) Km only
BRAINSCAPE1
