L17: Nitrogen Metabolism Flashcards

1
Q
A
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2
Q

What is the amino acid pool?

A

Collection of free amino acids at low concs inside cells/blood stream. It includes mixing & exchange with other free amino acids around the body.

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3
Q

Why is protein needed in a diet?

A

No ‘storage’ form of protein in the body to replace amino acids & other N containing compounds.

Replace lost amino acids & allow tissue repair

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4
Q

Positive & negative nitrogen balance in terms of N intake & N excretion

A

Positive: N intake > N excretion
Negative: N intake < N excretion

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5
Q

Causes of positive nitrogen balance

A

1) Pregnancy
2) After immobilisation after accident
3) Recovering from serious illness
4) During normal growth in children

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6
Q

Causes of negative nitrogen balance

A

1) During illness
2) Starvation
3) Late stages of some cancer
4) Injury/trauma

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7
Q

Most cellular proteins degradation pathways

A
  • Recognised as ‘old’ or damaged
  • Removed by ubiquitin breakdown system
  • Mixture of 20 amino acids
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8
Q

Foreign ‘exogenous’ proteins degradation pathways

A
  • ‘Old’ or damaged sub-cellular organelles
  • Taken into vesicles by endocytosis where vesicles fuse with lysosomes & proteolytic enzymes degrade proteins into amino acids
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9
Q

Define deamination

A

Removal of alpha-amino group

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10
Q

Where does deamination occur?

A

Liver mitochondrial matrix

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11
Q

What is deamination in this reaction
Glutamate -> a-Ketoglutarate + NH4+
catalysed by?

A

Glutamate dehydrogenase

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12
Q

Why does deamination remove the amino group from glutamate?

A

It can enter the Urea cycle for safe disposal

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13
Q

Define transamination

A

Conversion of 1 amino acid to another

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14
Q

Process of transamination

A

a-amino group is transferred from an amino acid to a-ketoglutarate to produce glutamate + a keto acid

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15
Q

Whhat is transamination catalysed by?

A

Aminotransferases/transaminases

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16
Q

What is
alanine + a-KG -> glutamate + pyruvate
catalysed by?

A

alanine aminotransferase

17
Q

What is
aspartate + a-KG -> glutamate + oxaloacetate
catalysed by?

A

aspartate aminotransferase

18
Q

Define transdeamination

A

Combined action of aminotransferases & glutamate to allow a-amino groups to enter Urea cycle

Transamination & deamination

19
Q

Role of glutamine

A

Transport of ammonia in the blood

20
Q

How many N in glutamate & glutamine?

A

Glutamate: 1N
Glutamine: 2N

21
Q

What does the glucose-alanie cycle allow the liver to do?

A

Regenerate glucose from this alanine

22
Q

Where and when is alanine generated?

A

Generated in skeletal muscle during exercise

23
Q

What happens to glutamine that transports ammonia to liver?

A

Glutamine converted to glutamate + ammonia

24
Q

What is alanie converted to from skeletal muscle?

A

Glutamate + Pyruvate

25
Q

What is glutamate deaminated to generate?

A

a-ketoglutarate & ammonia

26
Q

Which carbon skeletons can enter TCA cycle to generate ATP?

A

Pyruvate
Oxaloacetate
Fumarate
Succinul-CoA
a-Ketoglutarate

27
Q

Which carbon skeletons can produce ketone bodies?

A

Acetoacetyl-CoA & Acetyl-CoA

28
Q

Define essential amino acids

A

Cannot be synthesised in humans- must be obtained via diet

29
Q

Role of glutamate

A

Central to amino acid degration

30
Q

Role of glutamine

A

Transport ammonia to the liver

31
Q

Role of alanine

A

Transport ammonia from skeletal muscle to the liver