Amino acids and protein metabolism Flashcards

1
Q

Function of transamination?

A

Turn AA into intermediate in TCA cycle

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

What catalyses process of transamination?

A

Amino transferase

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

Outline process of transamination?

A

1) Transfer amine group from amino acid to alpha-ketoacid
2) Makes alpha-ketoacid and amino acid

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

What is the universal acceptor of amine groups?

A

Alpha-ketoglutarate

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

What enzyme does alanine use?
What does it form?

A

Alanine aminotransferase (ALT)
Form pyruvate and glutamate

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

Explain process of deamination?

A

Glutamate converted back to alpha ketoglutarate

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

What enzyme converts glutamate ack to alpha-ketoglutamate?

A

Glutamate dehydrogenase

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

What does process deamination produce?

A

Ammonium- removed urea cycle

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

What cycle do aa enter?

A

TCA cycle

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

How much albumin is produced/day?

A

9-12g

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

How is albumin returned to liver?

A

Collected by lymphatics
Returned via thoracic duct

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

Functions of albumin? (4)

A

1) Binding and transport
2) Maintenance colloid osmotic pressure
3) Free radicals neutralisation
4) Anticoagulant effects

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

What is extrinsic pathway activated by?

A

Factor VII coming into contact with tissue factor

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

Where are fibrinogen, prothrombin, IV,V,VI,VII PRODUCED?

A

Liver

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

Can proteins be stored?

A

No

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

How are proteins degraded? (2)

A

1) Proteasome- ubiquitin dependent
2) Lysosomal

17
Q

Explain process of proteasome degradation?

A

1) Ubiquitin activated by E1 enzyme in ATP-dependent reaction
2) Activated ubiquitin conjugated to specific ubiquitin-conjugating enzyme (E2)
3) This complex binds to ubiquitin ligase (E3)
4) Ubiquitin-ligase complex binds to a specific target protein resulting in polyubiquitination
5) Polyubiquitinated protein identified and directed to proteasome for degradation
6) Recycle Ub and amino acids for future use

18
Q

What 3 enzymes involved in proteosome degradation?

A

E1 – ubiquitin-activating enzyme
E2 – ubiquitin-conjugating enzyme
E3 – ubiquitin-protein ligase

19
Q

How does lysosomal degradation work?

A

Non selective
Digest protein, carbs, fats
Proteolytic enzymes

19
Q

How does lysosomal degradation work?

A

Non selective
Digest protein, carbs, fats
Proteolytic enzymes

20
Q

What occurs when dietary protein enters stomach, SI and enterocytes?

A