Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Fundamentals of the living cell > Proteolysis > Flashcards

Proteolysis Flashcards

1
Q

What is proteolysis?

A

Proteolysis is the biochemical process of breaking down proteins into smaller peptides or amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

True or False: Proteolysis is essential for protein turnover in cells.

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Fill in the blank: Proteolysis is primarily carried out by enzymes known as ______.

A

proteases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are the two main types of proteolysis?

A

Endopeptidase and Exopeptidase.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Multiple Choice: Which of the following is NOT a type of protease? A) Serine protease B) Cysteine protease C) Lipase D) Aspartic protease

A

C) Lipase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What role does proteolysis play in digestion?

A

It breaks down dietary proteins into amino acids for absorption.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

True or False: Proteolysis can occur both intracellularly and extracellularly.

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Fill in the blank: The process of proteolysis is crucial for ______ regulation.

A

cellular

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the function of proteasomes in proteolysis?

A

Proteasomes degrade ubiquitinated proteins within the cell.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Multiple Choice: Which enzyme class is primarily responsible for cleaving peptide bonds? A) Lipases B) Glycosidases C) Proteases D) Nucleases

A

C) Proteases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the significance of zymogens in proteolysis?

A

Zymogens are inactive precursors that require activation to become active proteases.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

True or False: Proteolysis can lead to the activation of signaling pathways.

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Fill in the blank: The amino acids released by proteolysis can be used for ______ synthesis.

A

protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Multiple Choice: Which of the following conditions can stimulate proteolysis? A) Starvation B) Overeating C) Sleep D) None of the above

A

A) Starvation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the role of lysosomes in proteolysis?

A

Lysosomes contain proteases that degrade proteins within the cell.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

True or False: Proteolysis is only important for protein breakdown.

A

False

17
Q

Fill in the blank: Proteolysis is involved in the regulation of ______ and metabolic pathways.

A

cell cycle

18
Q

What is the relationship between proteolysis and cancer?

A

Dysregulation of proteolysis can contribute to cancer progression and metastasis.

19
Q

Multiple Choice: Which of the following diseases is associated with abnormal proteolysis? A) Alzheimer’s B) Diabetes C) Hypertension D) All of the above

A

A) Alzheimer’s

20
Q

What is the role of caspases in proteolysis?

A

Caspases are proteases that play essential roles in programmed cell death (apoptosis).

21
Q

True or False: Proteolysis can only occur in the presence of water.

A

True

22
Q

Fill in the blank: The degradation of misfolded proteins is a critical function of ______.

A

proteolysis

23
Q

What is the effect of proteolysis on cellular signaling?

A

Proteolysis can activate or deactivate signaling molecules, influencing cellular responses.

24
Q

Multiple Choice: Which type of protease is involved in blood clotting? A) Serine protease B) Metalloprotease C) Cysteine protease D) Aspartic protease

A

A) Serine protease

25
Q

What are the different classifications of proteases?

A

1) proteases
2) proteinases
3) peptidase
4) cathepsins

26
Q

What are endopeptidases and exopeptidases?

A

Endopeptidases- enzymes that break peptide bonds within a protein chain—-> beginning of a chain

Exopeptidases- enzymes that break peptide bonds at the terminal end of a chain

27
Q

What are aminopeptidases and carboxypeptidases

A

Aminopeptidases- enzymes that cleave amino acids from N-Terminal of proteins

Carboxypeptidases- enzymes that break down proteins by splitting off amino acids

28
Q

What is protein activation and protein degradation?

A

Protein activation- structural/conformational chances to enhance proteins biological activity.

Protein degradation- proteins are broken down into amino acids.

29
Q

What is protein activation and protein degradation?

A

Protein activation- structural/conformational chances to enhance proteins biological activity.

Protein degradation- proteins are broken down into amino acids.

30
Q

Explain protein activation by proteolysis?

A

This involves the cleavage of specific peptide bonds within a protein—> this leads to structural changes within the protein.

1) Zymogen activation:
-zymogens are enzymes/signalling proteins that are synthesised or inactive precursors.

2) Confirmation changes:
-cleavage allows the protein to adopt an active site, exposing/creating the active site.

3) Regulatory role:
-proteolytic activation serves as a regulatory mechanism this controlling metabolic and physiological processes.

31
Q

What is ubiquitylation?

A

Ubiquitylation- involves the attachment of ubiquity (small protein) to a target protein.

32
Q

Explain the components of the ubiquitinating enzyme complex

A

Ubiquitin activation enzyme (E1):
-formation of thioester bond between the C-terminus of ubiquitin and a cystein on E1

Ubiquitin-conjugating enzyme (E2):
-transfer of ubiquitin to a cystein on E2

Ubiquitin-protein ligase (E3):
-transfer of ubiquitin (small protein) from E2 to a lysine on a target protein.

33
Q

Explain the components of the ubiquitinating enzyme complex

A

Ubiquitin activation enzyme (E1):
-formation of thioester bond between the C-terminus of ubiquitin and a cystein on E1

Ubiquitin-conjugating enzyme (E2):
-transfer of ubiquitin to a cystein on E2

Ubiquitin-protein ligase (E3):
-transfer of ubiquitin (small protein) from E2 to a lysine on a target protein.

34
Q

Explain the N-End rule

A

This explains the relationship between protein half life and amino terminal amino acid residue.

N-terminal residues are associated with rapid degradation.
N terminal residues are also tagged for degradation by the ubiquitin-proteasome system

35
Q

Explain the N-End rule

A

This explains the relationship between protein half life and amino terminal amino acid residue.

N-terminal residues are associated with rapid degradation.
N terminal residues are also tagged for degradation by the ubiquitin-proteasome system

36
Q

What class of proteases is involved in the coagulation cascade?

A

Carboxyproteases.

37
Q

What is the role of factor IX proprotein?

A

Zymogen of the clotting cascade

38
Q

How many proteolytic cleavages are required to convert preproinsulin to mature insulin?

A

2

Fundamentals of the living cell (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions