AP Biology
AP Bio Unit 3 MCQ Set A Concepts
Shared by Ashton · Nov 12, 2026 · 0 plays
18 questions across 5 sections. After every answer you’ll see why each choice is right or wrong, not just the one you picked.
Sample questions
Open a question to see the answer choices and the correct answer.
Which statement best describes how an enzyme increases the rate of a reaction?
- A. It lowers the activation energy of the reaction ✓
- B. It makes the products lower in free energy than before
- C. It shifts the reaction's equilibrium toward the products
- D. It supplies the extra energy the reactants need to react
Correct answer: A. Enzymes are catalysts that lower Eₐ (3.1.A.1); more molecules can react per second.
An enzyme hydrolyzes maltose but not sucrose, even though both are disaccharides. What is the best explanation?
- A. Sucrose's activation energy is too high for any enzyme to lower
- B. Sucrose is too large to enter the cell where the enzyme is
- C. The enzyme is used up after it hydrolyzes the maltose
- D. Only maltose has the shape and charge that fit the active site ✓
Correct answer: D. The substrate's shape and charge must be compatible with the active site (3.1.A.2).
The rate of a human enzyme's reaction increases as temperature rises from 10 °C to 30 °C. Which explanation is best?
- A. The active site partly unfolds, making it easier to enter
- B. Faster molecules collide with active sites more often ✓
- C. Hydrogen bonds in the enzyme break and expose the active site
- D. The reaction's ΔG becomes more negative as temperature rises
Correct answer: B. Below the optimum, more kinetic energy means more enzyme–substrate collisions (3.2.B.2).
Isoleucine is the final product of a five-step pathway. It binds the first enzyme of the pathway at a site other than the active site and slows the enzyme. This is an example of
- A. denaturation of the first enzyme caused by product buildup
- B. positive feedback that increases isoleucine production
- C. competitive inhibition, because isoleucine resembles the substrate
- D. allosteric inhibition by the pathway's end product (feedback) ✓
Correct answer: D. It binds an allosteric site, so it's noncompetitive (3.2.B.3), and it's the end product, so it's negative feedback.
A purified enzyme is unfolded with a chemical denaturant. When the chemical is removed, the enzyme refolds and regains most of its activity. This result best supports which claim?
- A. The chemical acted as a competitive inhibitor of the enzyme
- B. Some denaturation is reversible ✓
- C. Enzymes are denatured only by heat, never by chemicals
- D. Chemical denaturants break the enzyme's peptide bonds
Correct answer: B. 3.2.A.2. The primary structure holds the information for the active fold.