Enzyme Practice Questions

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Last updated 2:45 PM on 8/31/26
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45 Terms

1
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Which of the following is a common method for regulating enzyme activity in

cells?

o A) Changing the enzyme’s color

o B) Altering the enzyme’s genetic code

o C) Phosphorylation and dephosphorylation

o D) Increasing the cell’s temperature

C) Phosphorylation and dephosphorylation

2
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What happens to an enzyme when it is denatured?

o A) It becomes more active

o B) It loses its shape and function

o C) It binds more tightly to substrates

o D) It speeds up the reaction

B) It loses its shape and function

3
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Which of the following is true about enzyme specificity?

o A) One enzyme can catalyze multiple types of reactions

o B) Each enzyme can only catalyze one specific reaction

o C) Enzymes are not specific and can catalyze any reaction

o D) Enzyme specificity is determined by the enzyme’s color

B) Each enzyme can only catalyze one specific reaction

4
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What is the term for the molecule upon which an enzyme acts?

o A) Product

o B) Substrate

o C) Inhibitor

o D) Coenzyme

B) Substrate

5
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What is the effect of a competitive inhibitor on enzyme activity?

o A) It binds to the active site and decreases enzyme activity

o B) It binds to a different site and increases enzyme activity

o C) It binds to the active site and increases enzyme activity

o D) It binds to a different site and decreases enzyme activity

A) It binds to the active site and decreases enzyme activity

6
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Which of the following statements about enzymes is true?

o A) Enzymes are consumed in the reactions they catalyze

o B) Enzymes are specific to their substrates

o C) Enzymes can function at any temperature

o D) Enzymes are made up of nucleic acids

B) Enzymes are specific to their substrates

7
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Which of the following is an example of an enzyme?

o A) Hemoglobin

o B) Insulin

o C) Amylase

o D) Collagen

C) Amylase

8
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What is a coenzyme?

o A) A protein that speeds up chemical reactions

o B) A non-protein molecule that assists enzyme function

o C) A molecule that inhibits enzyme activity

o D) A molecule that stores genetic information

B) A non-protein molecule that assists enzyme function

9
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Which of the following factors does NOT affect enzyme activity?

o A) Temperature

o B) pH

o C) Substrate concentration

o D) Color of the enzyme

D) Color of the enzyme

10
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What is the primary function of enzymes in biological systems?

o A) To provide structural support

o B) To store genetic information

o C) To catalyze biochemical reactions

o D) To transport molecules across cell membranes

C) To catalyze biochemical reactions

11
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What does a low KM value indicate about an enzyme’s affinity for its substrate?

o A) Low binding affinity

o B) High binding affinity

o C) No binding affinity

o D) Variable binding affinity

B) High binding affinity

12
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What happens to most human enzymes at temperatures higher than 37?

o A) They become more active

o B) They denature and lose their secondary and tertiary structure

o C) They bind more tightly to substrates

o D) They speed up the reaction

B) They denature and lose their secondary and tertiary structure

13
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Which type of inhibition is characterized by a rapid dissociation of the enzyme-

inhibitor complex?

o A) Irreversible inhibition

o B) Reversible inhibition

B) Reversible inhibition

14
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What is the effect of a non-competitive inhibitor on enzyme activity?

o A) It binds to the active site and decreases enzyme activity

o B) It binds to a different site and decreases enzyme activity

o C) It binds to the active site and increases enzyme activity

o D) It binds to a different site and increases enzyme activity

B) It binds to a different site and decreases enzyme activity

15
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Which of the following is an example of a competitive inhibitor?

o A) Penicillin

o B) Aspirin

o C) Methotrexate

o D) Lactase

C) Methotrexate

16
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What is the role of positive allosteric modulation in enzyme activity?

o A) It decreases the enzyme’s affinity for the substrate

o B) It enhances the attraction between substrate molecules and other

binding sites

o C) It inhibits the enzyme’s activity

o D) It changes the enzyme’s genetic code

B) It enhances the attraction between substrate molecules and other

binding sites

17
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What is the function of phosphorylation in protein regulation?

o A) It turns off the enzyme’s activity

o B) It turns on the enzyme’s activity

o C) It degrades the enzyme

o D) It stores the enzyme for future use

B) It turns on the enzyme’s activity

18
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What is the role of the ubiquitin-proteasome system (UPS) in protein

degradation?

o A) It degrades long-lived proteins and insoluble protein aggregates

o B) It eliminates short-lived proteins and soluble misfolded proteins

o C) It stores proteins for future use

o D) It transports proteins across cell membranes

B) It eliminates short-lived proteins and soluble misfolded proteins

19
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What is the function of chaperone-mediated autophagy?

o A) It degrades long-lived proteins

o B) It facilitates the degradation of unfolded proteins

o C) It degrades damaged organelles

o D) It degrades intracellular pathogens

B) It facilitates the degradation of unfolded proteins

20
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What is the Michaelis constant (KM)?

o A) The maximum velocity of an enzyme-catalyzed reaction

o B) The substrate concentration at which the reaction velocity is 50% of the

Vmax

o C) The rate of enzyme reaction at high substrate concentrations

o D) The energy required to start a reaction

B) The substrate concentration at which the reaction velocity is 50% of the

Vmax

21
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Which of the following statements about enzyme inhibition is true?

o A) Irreversible inhibitors dissociate quickly from the enzyme

o B) Competitive inhibitors bind to a site other than the active site

o C) Non-competitive inhibitors compete with the substrate for the active

site

o D) Competitive inhibitors can be reversed by adding more substrate

D) Competitive inhibitors can be reversed by adding more substrate

22
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What is the effect of a competitive inhibitor on enzyme activity?

o A) It binds to the active site and decreases enzyme activity

o B) It binds to a different site and increases enzyme activity

o C) It binds to the active site and increases enzyme activity

o D) It binds to a different site and decreases enzyme activity

A) It binds to the active site and decreases enzyme activity

23
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Which of the following is an example of an irreversible inhibitor?

o A) Methotrexate

o B) Penicillin

o C) Lactase

o D) Amylase

B) Penicillin

24
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What is the role of cofactors in enzyme activity?

o A) They provide structural support to the enzyme

o B) They assist in catalysis by being non-protein components

o C) They inhibit enzyme activity

o D) They store genetic information

B) They assist in catalysis by being non-protein components

25
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What happens to an enzyme when it is denatured?

o A) It becomes more active

o B) It loses its shape and function

o C) It binds more tightly to substrates

o D) It speeds up the reaction

B) It loses its shape and function

26
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Which of the following statements about allosteric regulation is true?

o A) Allosteric activators bind to the catalytic site

o B) Allosteric inhibitors increase the enzyme’s activity

o C) Allosteric activators change the conformation of the catalytic site to

increase substrate affinity

o D) Allosteric regulation involves the enzyme’s genetic code

C) Allosteric activators change the conformation of the catalytic site to

increase substrate affinity

27
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Which of the following statements about GTP and GDP is true?

• A) GTP is the inactive form, and GDP is the active form

• B) GDP is the inactive form, and GTP is the active form

• C) Both GTP and GDP are active forms

• D) Both GTP and GDP are inactive form

B) GDP is the inactive form, and GTP is the active form

28
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What happens to a target protein when it is bound to GTP?

o A) It becomes inactive

o B) It becomes active

o C) It is degraded

o D) It is transported out of the cell

B) It becomes active

29
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What is the significance of the polyubiquitin tail in the UPS?

o A) It provides energy for protein degradation

o B) It marks proteins for degradation by the proteasome

o C) It transports proteins to the lysosome

o D) It synthesizes new proteins

B) It marks proteins for degradation by the proteasome

30
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Which of the following processes is NOT associated with the ubiquitin-

proteasome system?

o A) Protein synthesis

o B) Protein degradation

o C) Regulation of protein levels

o D) Removal of misfolded proteins

A) Protein synthesis

31
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Which of the following statements about the proteasome is true?

o A) It synthesizes new proteins

o B) It degrades ubiquitin-tagged proteins

o C) It transports proteins across cell membranes

o D) It stores genetic information

B) It degrades ubiquitin-tagged proteins

32
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Which enzyme is responsible for attaching ubiquitin to target proteins?

o A) Protease

o B) Ubiquitin ligase (E3)

o C) Kinase

o D) Phosphatase

B) Ubiquitin ligase (E3)

33
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Which of the following components is NOT involved in the ubiquitin-proteasome

system?

o A) Ubiquitin

o B) Proteasome

o C) Ribosome

o D) Ubiquitin ligases

C) Ribosome

34
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All of the following statements about enzymes are false except

A. They are reusable

B. They increase the activation energy of a reaction

C. They decrease the rate of a reaction

D. They do not catalyze metabolic pathways.

A. They are reusable

35
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True or False? Michaelis-Menten constant (Km) is a measure of substrate binding. If the rates of binding and reaction velocity are fast, Km will be high

False

36
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Which term describes the model of enzyme activity where the enzyme changes

shape to fit the substrate?

o A) Lock and key model

o B) Induced fit model

o C) Fluid mosaic model

o D) Double helix model

B) Induced fit model

37
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Which of the following statements about enzymes is true?

o A) Enzymes are consumed in the reactions they catalyze

o B) Enzymes are specific to their substrates

o C) Enzymes can function at any temperature

o D) Enzymes are made up of nucleic acids

B) Enzymes are specific to their substrates

38
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How do enzymes affect the activation energy of a reaction?

o A) They increase the activation energy

o B) They decrease the activation energy

o C) They do not affect the activation energy

o D) They eliminate the need for activation energy

B) They decrease the activation energy

39
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What is the function of chaperone-mediated autophagy?

o A) It degrades long-lived proteins

o B) It facilitates the degradation of unfolded proteins

o C) It degrades damaged organelles

o D) It degrades intracellular pathogens

B) It facilitates the degradation of unfolded proteins

40
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What is the primary function of lysosomes in the cell?

o A) To store genetic information

o B) To degrade long-lived proteins, insoluble protein aggregates, and

damaged organelles

o C) To transport molecules across cell membranes

o D) To provide structural support to cells

B) To degrade long-lived proteins, insoluble protein aggregates, and

damaged organelles

41
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What is the role of autophagosomes in lysosome-mediated degradation?

o A) They synthesize new proteins

o B) They transport proteins to the nucleus

o C) They encircle damaged organelles and fuse with lysosomes

o D) They store proteins for future use

C) They encircle damaged organelles and fuse with lysosomes

42
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Which form of autophagy involves the direct engulfment of small cytoplasmic

solutes by lysosomes?

o A) Macroautophagy

o B) Microautophagy

o C) Chaperone-mediated autophagy

o D) Endocytosis

B) Microautophagy

43
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What effect does the binding of one oxygen molecule have on the affinity of

hemoglobin for additional oxygen molecules?

o A) It decreases the affinity for additional oxygen molecules

o B) It increases the affinity for additional oxygen molecules

o C) It has no effect on the affinity for additional oxygen molecules

o D) It denatures hemoglobin

B) It increases the affinity for additional oxygen molecules

44
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What is the primary difference between the T state and R state of hemoglobin?

o A) The T state has a higher affinity for oxygen than the R state

o B) The R state has a higher affinity for oxygen than the T state

o C) The T state is denatured, while the R state is not

o D) The R state is denatured, while the T state is not

B) The R state has a higher affinity for oxygen than the T state

45
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True or False? Competitive inhibitors pushes km of enzymes towards higher side

True