Unit 5: Enzymes, Vitamins and Minerals - Practice Quiz

BTY105 — Fundamentals Of Biochemistry 60 Questions
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1 What is the main function of an enzyme?

Mechanisms of enzymes action Easy
A. To increase activation energy
B. To become a permanent product
C. To stop all cellular reactions
D. To speed up a chemical reaction

2 The region of an enzyme where the substrate binds is called the:

Mechanisms of enzymes action Easy
A. Peptide bond
B. Carboxyl group
C. Phosphate group
D. Active site

3 According to the lock-and-key model, the active site and substrate are:

Mechanisms of enzymes action Easy
A. Both made of lipids
B. Completely unrelated
C. Complementary in shape
D. Temporarily destroyed

4 Many enzyme names end with which suffix?

Nomenclature and classification of enzymes Easy
A. -ide
B. -ase
C. -ose
D. -one

5 Which enzyme class catalyzes oxidation-reduction reactions?

Nomenclature and classification of enzymes Easy
A. Isomerases
B. Oxidoreductases
C. Hydrolases
D. Ligases

6 Enzymes that break chemical bonds by adding water belong to which class?

Nomenclature and classification of enzymes Easy
A. Hydrolases
B. Lyases
C. Ligases
D. Transferases

7 What usually happens to enzyme activity when temperature increases from a low value to the optimum temperature?

Factors affecting enzyme activity Easy
A. It remains exactly constant
B. It always disappears
C. It changes into a vitamin
D. It usually increases

8 What may happen to an enzyme at a very high temperature?

Factors affecting enzyme activity Easy
A. It changes into a mineral
B. It gains unlimited activity
C. It becomes a carbohydrate
D. It may be denatured

9 The pH at which an enzyme works most effectively is called its:

Factors affecting enzyme activity Easy
A. Melting point
B. Boiling point
C. Optimum pH
D. Neutral point

10 How does increasing substrate concentration usually affect enzyme activity when enzyme concentration is fixed?

Factors affecting enzyme activity Easy
A. It stops activity immediately
B. It changes the enzyme into water
C. It removes all active sites
D. It increases activity until saturation

11 What does the reaction rate describe in enzyme kinetics?

Enzyme kinetics Easy
A. The temperature of the solvent
B. The speed of product formation
C. The mass of the test tube
D. The amount of enzyme color

12 The maximum reaction rate of an enzyme is commonly represented by:

Enzyme kinetics Easy
A.
B.
C.
D.

13 In the Michaelis-Menten equation, represents:

Enzyme kinetics Easy
A. Product concentration
B. Salt concentration
C. Substrate concentration
D. Enzyme concentration

14 When all enzyme active sites are occupied by substrate, the enzyme is described as:

Enzyme kinetics Easy
A. Oxidized
B. Hydrolyzed
C. Saturated
D. Denatured

15 What is enzyme inhibition?

Overview of enzyme inhibition Easy
A. An increase in enzyme synthesis
B. A complete increase in product formation
C. A decrease in enzyme activity
D. A change from protein to lipid

16 A competitive inhibitor usually binds to the enzyme's:

Overview of enzyme inhibition Easy
A. Product molecule
B. Cell membrane
C. Nucleus
D. Active site

17 A noncompetitive inhibitor usually binds to:

Overview of enzyme inhibition Easy
A. Only the substrate
B. A site other than the active site
C. Water molecules only
D. The product after release

18 Vitamins are generally needed by the body in:

Introduction to vitamins and minerals Easy
A. Only gaseous form
B. Amounts equal to water
C. Small amounts
D. Very large amounts

19 Which statement best describes minerals?

Introduction to vitamins and minerals Easy
A. They are always carbohydrates
B. They are made only by enzymes
C. They are all proteins
D. They are inorganic elements

20 Which vitamin is commonly associated with vision and healthy skin?

Introduction to vitamins and minerals Easy
A. Vitamin C
B. Vitamin K
C. Vitamin B12
D. Vitamin A

21 An enzyme binds a substrate and slightly changes its shape so that the substrate fits more closely. Which model best describes this interaction?

Mechanisms of enzymes action Medium
A. Induced-fit model
B. Fluid-mosaic model
C. Lock-and-key model
D. Negative-feedback model

22 How does an enzyme increase the rate of a biochemical reaction?

Mechanisms of enzymes action Medium
A. By shifting the final equilibrium toward products
B. By permanently changing the substrate structure
C. By increasing the reaction's free-energy change
D. By lowering the reaction's activation energy

23 A mutation replaces an active-site amino acid that normally donates a proton during catalysis. Which consequence is most likely?

Mechanisms of enzymes action Medium
A. The reaction equilibrium will shift permanently
B. The catalytic rate may decrease substantially
C. The enzyme will become a structural protein
D. The enzyme will always bind more substrate

24 An enzyme transfers a phosphate group from ATP to glucose. Which enzyme class most directly describes this reaction?

Nomenclature and classification of enzymes Medium
A. Hydrolase
B. Isomerase
C. Oxidoreductase
D. Transferase

25 Which enzyme class catalyzes the hydrolysis of peptide bonds using water?

Nomenclature and classification of enzymes Medium
A. Ligases
B. Lyases
C. Isomerases
D. Hydrolases

26 An enzyme catalyzes the joining of two molecules using energy from ATP hydrolysis. Which class does it belong to?

Nomenclature and classification of enzymes Medium
A. Ligase
B. Transferase
C. Lyase
D. Oxidoreductase

27 An enzyme shows maximum activity at pH 7.0 but loses activity at pH 3.0. What is the most likely explanation?

Factors affecting enzyme activity Medium
A. Ionization of active-site groups is altered
B. The substrate becomes permanently radioactive
C. The enzyme concentration becomes infinite
D. The reaction's equilibrium constant becomes zero

28 Why does enzyme activity often decline sharply above the enzyme's optimum temperature?

Factors affecting enzyme activity Medium
A. The enzyme may denature or lose its shape
B. Activation energy becomes permanently negative
C. Product molecules stop existing
D. Substrate concentration becomes negligible

29 If substrate concentration is increased while enzyme concentration remains constant, the reaction rate eventually reaches a plateau because:

Factors affecting enzyme activity Medium
A. The enzyme is converted into product
B. The substrate changes into an inhibitor
C. All enzyme active sites become occupied
D. The reaction temperature falls automatically

30 Two reaction mixtures contain the same enzyme concentration, but one has twice as much enzyme substrate available. Under substrate-limited conditions, what is expected?

Factors affecting enzyme activity Medium
A. The mixture with more substrate stops immediately
B. The mixture with more substrate reacts faster
C. The enzyme becomes unrelated to its substrate
D. Both mixtures must have identical rates

31 For a Michaelis-Menten enzyme, the substrate concentration equals . What fraction of is the reaction rate approximately equal to?

Enzyme kinetics Medium
A.
B.
C.
D.

32 An enzyme has a lower than another enzyme for the same substrate under identical conditions. What does this generally indicate?

Enzyme kinetics Medium
A. Higher apparent substrate affinity
B. Lower apparent substrate affinity
C. Lower maximum catalytic capacity
D. Complete resistance to inhibition

33 If an enzyme concentration is doubled while substrate is abundant, what change is expected in the initial reaction rate?

Enzyme kinetics Medium
A. The rate remains exactly zero
B. The rate approximately doubles
C. The rate decreases by half
D. The rate becomes independent of enzyme amount

34 A reaction has an initial rate of micromoles per minute at a given substrate concentration. If the substrate concentration is increased far above , what rate is most likely approached?

Enzyme kinetics Medium
A. A rate close to
B. A rate close to micromoles per minute
C. A rate close to micromoles per minute
D. A rate close to zero

35 A competitive inhibitor binds reversibly to the active site. Which kinetic change is expected when sufficient substrate is added?

Overview of enzyme inhibition Medium
A. increases while is unchanged
B. decreases while increases
C. decreases and cannot be restored
D. Both and become zero

36 An inhibitor binds only to the enzyme-substrate complex and reduces the maximum rate. Which type of inhibition best fits this description?

Overview of enzyme inhibition Medium
A. Allosteric activation
B. Uncompetitive inhibition
C. Competitive inhibition
D. Substrate cooperation

37 A noncompetitive inhibitor binds at a site distinct from the active site and cannot be overcome by increasing substrate concentration. What happens to ?

Overview of enzyme inhibition Medium
A. It remains infinite
B. It increases substantially
C. It decreases
D. It becomes equal to

38 Which statement best distinguishes fat-soluble vitamins from water-soluble vitamins?

Introduction to vitamins and minerals Medium
A. Fat-soluble vitamins are stored more readily in body tissues
B. Fat-soluble vitamins cannot participate in metabolism
C. Water-soluble vitamins are absorbed only with dietary lipids
D. Water-soluble vitamins are always toxic at low doses

39 A person with inadequate vitamin C intake develops impaired wound healing. Which function of vitamin C is most directly related?

Introduction to vitamins and minerals Medium
A. DNA base pairing
B. Bile salt secretion
C. Insulin receptor destruction
D. Collagen formation

40 Which mineral is most directly required for hemoglobin synthesis and oxygen transport?

Introduction to vitamins and minerals Medium
A. Fluoride
B. Calcium
C. Iodine
D. Iron

41 A serine protease forms a tetrahedral intermediate during peptide-bond hydrolysis. Which event most directly stabilizes the highest-energy intermediate in the reaction coordinate?

Mechanisms of enzymes action Hard
A. Release of the peptide product before nucleophilic attack
B. Hydrophobic exclusion of water from the active site
C. Permanent oxidation of the catalytic serine residue
D. Electrostatic stabilization of the oxyanion by backbone NH groups

42 An enzyme accelerates a reaction by binding the transition state more tightly than either substrate or product. Which consequence is expected if a transition-state analog is introduced?

Mechanisms of enzymes action Hard
A. It should bind strongly and often inhibit catalysis
B. It should increase the reaction equilibrium constant
C. It should permanently activate the enzyme by lowering
D. It should bind weakly because it cannot form product

43 A mutant enzyme retains substrate binding but loses catalytic activity after replacement of a histidine residue that normally accepts a proton. Which mechanistic role was most likely disrupted?

Mechanisms of enzymes action Hard
A. Substrate-level phosphorylation
B. Product sequestration by covalent bonding
C. Reduction of the reaction equilibrium constant
D. General acid-base catalysis

44 An enzyme catalyzes the transfer of a phosphate group from ATP to a serine residue on a protein. Which EC class and reaction description are most appropriate?

Nomenclature and classification of enzymes Hard
A. Oxidoreductase; oxidation of protein serine
B. Transferase; transfer of a phosphoryl group
C. Lyase; elimination of phosphate from ATP
D. Hydrolase; hydrolysis of ATP only

45 Which enzyme-function pairing correctly distinguishes a lyase from a hydrolase?

Nomenclature and classification of enzymes Hard
A. A lyase transfers electrons, whereas a hydrolase transfers phosphate
B. A lyase requires ATP, whereas a hydrolase always requires a metal ion
C. A lyase binds allosteric ligands, whereas a hydrolase binds substrates
D. A lyase cleaves bonds by elimination, whereas a hydrolase uses water

46 An enzyme has maximal activity at pH 7.0, but activity decreases sharply at both pH 5 and pH 9. Which explanation best accounts for this pattern?

Factors affecting enzyme activity Hard
A. Only substrate concentration changes with pH
B. The enzyme becomes more concentrated at pH 7
C. The reaction equilibrium shifts completely toward substrate
D. Catalytic residues require particular protonation states

47 When temperature is increased over a narrow range, an enzyme's initial rate first rises and then falls abruptly. Which interpretation is most consistent with the data?

Factors affecting enzyme activity Hard
A. Catalysis accelerates initially, followed by thermal denaturation
B. Substrate binding becomes impossible before catalysis accelerates
C. The reaction becomes diffusion-independent at high temperature
D. The enzyme concentration increases and then decreases

48 An enzyme displays sigmoidal velocity versus substrate concentration, and a small amount of an end product shifts the curve to the right without changing the maximal velocity. What is the most likely explanation?

Factors affecting enzyme activity Hard
A. Irreversible destruction of every active site
B. Competitive allosteric inhibition of a cooperative enzyme
C. Noncompetitive inhibition at saturating substrate
D. A decrease in the chemical equilibrium constant

49 For a Michaelis–Menten enzyme, and . What is the initial velocity at ?

Enzyme kinetics Hard
A.
B.
C.
D.

50 Two enzymes have the same , but enzyme A has a lower than enzyme B for the same substrate. At substrate concentrations well below both values, which conclusion is justified?

Enzyme kinetics Hard
A. Both enzymes must have identical substrate affinity and rate
B. B must have the greater catalytic efficiency regardless of
C. A has the greater catalytic efficiency if is equal
D. A must have a lower because its is lower

51 An enzyme-catalyzed reaction is measured under initial-rate conditions. Doubling enzyme concentration doubles the rate, whereas doubling substrate concentration has little effect when substrate is already saturating. Which parameter is most directly demonstrated to be proportional to enzyme concentration?

Enzyme kinetics Hard
A. The substrate's molecular mass
B.
C.
D. The equilibrium constant

52 A Lineweaver–Burk plot gives a -intercept of and an -intercept of . What are and ?

Enzyme kinetics Hard
A. and
B. and
C. and
D. and

53 A mutant enzyme shows a tenfold decrease in but no change in . Which conclusion is most defensible?

Enzyme kinetics Hard
A. Substrate recognition is unchanged, but the chemical step is slower
B. The enzyme cannot bind substrate at any concentration
C. The reaction equilibrium has shifted tenfold toward product
D. The total enzyme concentration has increased tenfold

54 An inhibitor increases the apparent but leaves unchanged, and its effect can be overcome by sufficiently high substrate concentration. What inhibition pattern is indicated?

Overview of enzyme inhibition Hard
A. Competitive inhibition
B. Pure noncompetitive inhibition
C. Irreversible inhibition
D. Uncompetitive inhibition

55 An inhibitor binds only to the enzyme–substrate complex. Which kinetic changes are expected for ideal uncompetitive inhibition?

Overview of enzyme inhibition Hard
A. Higher apparent and unchanged
B. Lower apparent and lower
C. Higher apparent and higher
D. Unchanged and higher

56 A reversible inhibitor produces intersecting Lineweaver–Burk lines on the -axis at different inhibitor concentrations. Which mechanism is most consistent with this result?

Overview of enzyme inhibition Hard
A. Uncompetitive inhibition
B. Competitive inhibition
C. Substrate inhibition
D. Pure noncompetitive inhibition

57 A drug contains a reactive group that becomes activated only after the target enzyme processes it, after which the enzyme is covalently modified. What type of inhibition is this?

Overview of enzyme inhibition Hard
A. Reversible competitive inhibition
B. Mechanism-based irreversible inhibition
C. Reversible uncompetitive inhibition
D. Allosteric activation

58 A patient has megaloblastic anemia and neurologic dysfunction. Folate supplementation corrects the anemia but worsens the diagnostic delay. Which deficiency should be specifically investigated?

Introduction to vitamins and minerals Hard
A. Vitamin C deficiency
B. Vitamin E deficiency
C. Vitamin B deficiency
D. Vitamin K deficiency

59 A person consuming a diet rich in plant-based iron develops iron deficiency despite adequate total iron intake. Which physiological factor most plausibly contributes?

Introduction to vitamins and minerals Hard
A. Heme iron is converted into a fat-soluble vitamin in the intestine
B. Vitamin D prevents all intestinal iron transport
C. Iron absorption is independent of chemical form and meal composition
D. Non-heme iron absorption is reduced by inhibitors such as phytate

60 Which combination best explains why vitamin C deficiency can impair connective tissue integrity and also contribute to anemia?

Introduction to vitamins and minerals Hard
A. Increased clotting-factor activation and enhanced copper absorption
B. Reduced DNA methylation and excessive calcium deposition
C. Impaired retinal pigment formation and increased hemoglobin synthesis
D. Defective collagen hydroxylation and reduced non-heme iron absorption