AP Biology · Topic 3.1
Enzyme Structure Practice
Part of Cellular Energetics.(ENE-1.L)
Practice questions
4
Sample questions
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Sample 1difficulty 2/5
A non-protein helper required by some enzymes for activity is called a
- A
Allosteric regulator (binds elsewhere)
- Bcheck_circle
Cofactor (or coenzyme if organic)
- C
Substrate (binds active site)
- D
Inhibitor (blocks active site)
Why
Inorganic ions (e.g., Mg²⁺) = cofactors; organic helpers (e.g., NAD⁺, vitamins) = coenzymes.
- A
Sample 2difficulty 2/5
The active site of an enzyme is
- A
A region whose chemistry is independent of the identity of the substrate
- Bcheck_circle
A pocket whose shape and chemistry are complementary to the substrate
- C
A pocket built from nucleic acid bases rather than from amino acid residues
- D
The entire outer surface of the enzyme where any substrate can dock
Why
Substrate binds in the active site (induced fit), where chemistry converts it to products.
- A
Sample 3difficulty 2/5
What does this diagram illustrate about enzyme function?
- A
Enzymes are consumed during the reaction
- B
Enzymes denature when substrates fit
- C
All substrates can be acted on by any enzyme
- Dcheck_circle
Substrate specificity - only molecules with complementary shape bind the active site
Why
Active sites have specific 3D shapes. Only substrates whose shape and chemistry match (induced fit) can bind effectively.
- A
Sample 4difficulty 2/5
Magnesium ion shown bound to the apoenzyme is best classified as:
- A
An allosteric activator made of protein
- B
A substrate
- C
A competitive inhibitor
- Dcheck_circle
An inorganic cofactor required for enzyme activity
Why
Inorganic ions (e.g., Mg2+, Zn2+, Fe2+) that are required for enzyme catalysis are cofactors. Organic cofactors are called coenzymes (e.g., NAD+).
- A