Protein Metabolism Flashcards

(56 cards)

1
Q

What is denaturation?

A

The unfolding of protein’s structure, often due to acid, heat or enzymes

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2
Q

What is proteolysis?

A

Enzymatic breakdown of proteins into peptides or amino acids

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3
Q

Where does protein denaturation mainly occur?

A

In the stomach

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4
Q

Which enzyme starts protein digestion in the stomach?

A

Pepsin

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5
Q

What kind of enzyme is pepsin?

A

An endopeptidase

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6
Q

Which enzymes act in the small intestine to digest proteins?

A

Trypsin and chymotrypsin

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7
Q

What are endopeptidase?

A

Enzymes that cleaves amino acids from internal peptide bonds

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8
Q

What are exopeptidases?

A

Enzymes that cleave amino acids from the ends of peptide chains

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9
Q

How do amino acids enter cells?

A

Via carrier protein mediated active transport

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10
Q

What happens after amino acids enter the cell?

A

The amino group is removed by deamination

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11
Q

What is deamination?

A

Removal of the amino group from an amino acid

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12
Q

What does deamination produce?

A

Ammonia and a carbon skeleton

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13
Q

What is transamination?

A

Transfer of an amino group to α-ketoglutarate to form glutamate

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14
Q

Which enzyme catalyses transamination?

A

Aminotransferase

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15
Q

What is oxidative deamination?

A

Removal of an amino group from glutamate to form ammonia

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16
Q

What enzyme catalyses oxidative deamination?

A

Glutamate dehydrogenase

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17
Q

Where does oxidative deamination mainly occur?

A

In the liver

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18
Q

Which two amino acids can be directly deaminated?

A

Serine and threonine

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19
Q

Why can serine and threonine be directly deaminated?

A

They have a hydroxyl group on the β-carbon

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20
Q

What happens to the carbon skeleton after deamination?

A

It’s converted into metabolic intermediates

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21
Q

What are the 7 metabolic intermediated derived from AAs?

A
  • Acetyl-CoA
  • Acetoacetyl-CoA
  • Pyruvate
  • α-ketoglutarate
  • Succinyl-CoA
  • Fumarate
  • Oxaloacetate
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22
Q

What are ketogenic amino acids?

A

AAs that form ketone bodies like acetoacetate

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23
Q

What are glucogenic amino acids?

A

AAs that form glucose via gluconeogenesis

24
Q

Which amino acids are purely ketogenic?

A

Leucine and lysine

25
Which 4 amino acids are both ketogenic and glucogenic?
- Isoleucine - Phenylalanine - Tryptophan - Tryosine
26
Which 5 amino acids can form pyruvate?
- Alanine - Serine - Cystine - Threonine - Tryptophan
27
Which 4 amino acids can form α-ketoglutarate?
- Glutamine - Proline - Arginine - Histidine
28
What happens to ammonia from deamination?
Its enters the urea cycle for detoxification
29
What happens to the carbon skeleton after deamination?
It enters the citric acid cycle or oxidative phosphorylation
30
What are essential amino acids?
AAs that must be obtained from the diet
31
Do essential amino acids vary by organism?
Yes plants can synthesise all 20 humans cannot
32
How many essential amino acids do humans need from the diet?
Nine
33
What are the nine essential amino acids?
- Histidine - Isoleucine - Leucine - Lysine - Methionine - Phenylalanine - Threonine - Tryptophan - Valin
34
What are nonessential amino acids?
Amino acids the body can synthesise from metabolic intermediates
35
What three pathways provide carbon skeletons for amino acid biosynthesis?
- Glycolysis - Citric acid cycle - Pentose phosphate pathway
36
What supplies the amino group in amino acid biosynthesis?
Glutamate or glutamine
37
What is the opposite of amino acid deamination?
Amination
38
What is amination?
The adding of an amino group
39
What is transamination in biosynthesis?
Transfer of an amino group to a carbon skeleton to form an amino acid
40
Is biosynthesis of amino acids the same for all AAs?
No some require simple transamination other need complex multistep synthesis
41
How is arginine synthesised?
Requires synthesis in two different tissues
42
Which amino acid requires the most ATP to synthesise?
Tyrosine
43
How is amino acid biosynthesis regulated?
Via multiple feedback mechanisms
44
What are aminoacidopathies?
Inborn errors of amino acid metabolism often life threatening in newborns
45
What is the main treatment for aminoacidopathies?
Strict dietary restriction of the affected amino acids
46
What is albinism caused by?
Deficiency of tyrosinase enzyme
47
What is PKU caused by?
Deficiency in hydroxylase
48
What happens if PKU is untreated?
Sever mental retardation
49
What causes maple syrup urine disease?
Defect in Keto acid decarboxylase
50
What are four signs of amino acid deficiencies in animals?
- Impaired growth - Poor appetite - Paralysis - Poor reproduction
51
What amino acid deficiency causes paralysis in animals?
Arginine
52
What are three signs of essential amino acid toxicity?
- Organ damage - Reduced feed intake - Poor growth
53
What happens with excess phenylalanine in animal diets?
Reduce feed intake and reproduction
54
What happens with excess tryosine?
Liver and kidney degeneration
55
What happens with excess tryptophan?
Kidney damage and growth cessation
56
Are disorders of amino acid metabolism reversible?
No