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KIPS S.R Biology Unit 2: Biological Molecules & Enzymes

10 multiple-choice questions (rising difficulty) based on Prep Titans KIPS S.R Unit#2 Biological Molecules & Enzymes material.

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Abdul Rafay
Abdul Rafay
Published June 24, 2026

Quiz Questions & Answers

Review every prompt, the correct responses, and helpful context to prep for your own run-through.

Question 1: Which group of biological molecules commonly serves as long-term energy storage and is hydrophobic?

Proteins

Lipids

Nucleic acids

Carbohydrates

Question 2: What is the basic monomer unit of proteins?

Fatty acid

Nucleotide

Amino acid

Monosaccharide

Question 3: Which bond joins monosaccharides in a carbohydrate polymer?

Peptide bond

Phosphodiester bond

Glycosidic bond

Ester bond

Question 4: Which macromolecule stores genetic information in cells?

Lipids

Nucleic acids

Polysaccharides

Carbohydrates

Question 5: Which property of enzymes most directly explains why only specific substrates bind to an enzyme?

Solubility in water

Denaturation point

Primary sequence length

Active site specificity

Question 6: Which factor commonly increases the rate of an enzyme-catalyzed reaction up to a point, before causing denaturation if excessive?

Substrate inhibition

Cofactor absence

Temperature

pH neutrality

Question 7: Which type of enzyme inhibitor binds irreversibly to the active site and permanently inactivates the enzyme?

Irreversible inhibitor

Allosteric activator

Competitive inhibitor

Noncompetitive inhibitor

Question 8: Which carbohydrate is a structural polysaccharide found in plant cell walls?

Cellulose

Glycogen

Fructose

Starch

Question 9: Which statement best describes the role of cofactors in enzyme activity?

Cofactors assist enzyme function by enabling proper active site conformation or participating in catalysis.

Cofactors are polysaccharides that store energy for enzymes.

Cofactors are only required at extremely high temperatures.

Cofactors permanently inhibit enzymes by blocking substrates.

Question 10: Which change to an enzyme would most likely lower its Vmax but not alter substrate binding affinity (Km) in classic Michaelis–Menten terms?

Competitive inhibition

Noncompetitive inhibition

Increasing substrate concentration

Allosteric activation