Review 8: Amino Acid Metabolism Flashcards

1
Q

What are 3 sources of free amino acids

A

1) degradation of ingested protein
2) biosynthesis of amino acids
3) degradation of endogenous protein

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2
Q

True or false: concentration of free amino acids is high

A

FALSE; conc is balanced so that utilization balances formation (<1mM in plasma)

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3
Q

How is nitrogen excreted in the body?

A

urea

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4
Q

What are the 2 steps in degrading amino acids?

A

1) removal of nitrogen to form urea (transamination)

2) degradation of carbon skeletons

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5
Q

What are the 2 sources of nitrogen for the biosynthesis of urea?

A

1) aspartate

2) ammonia

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6
Q

Where does urea synthesis occur?

A

liver

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7
Q

What is the purpose of urea biosynthesis?

A

detoxification of ammonia

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8
Q

What are ketogenic substrates?

A

1) acetoacetate

2) acetyl CoA

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9
Q

What are glucogenic substrates?

A

1) pyruvate
2) alpha ketoglutarate
3) succinyl CoA
4) fumarate
5) oxaloacetate

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10
Q

Define “nutritionally non-essential amino acids”

A

can be synthesized from precursor molecules

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11
Q

Define “nutritionally essential” amino acids

A

need to be consumed in the diet

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12
Q

What is the range of half lives for proteins in the body?

A

a few minutes - many days

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13
Q

What percentage of total body protein is degraded and resynthesized every day in adults?

A

2-3%

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14
Q

True or false: there is net accumulation of protein on a high protein diet

A

FALSE (excess amino acids are degraded, not stored)

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15
Q

The body degrades ___g of protein every day

A

55

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16
Q

What happens to the carbon skeletons of amino acids?

A

broken down and used immediately or stored as glycogen or fat

17
Q

What is the equation for nitrogen balance?

A

Nitrogen ingested (protein) - nitrogen excreted (urea)

18
Q

What are some examples where a POSITIVE nitrogen balance would be normal?

A

child growth, pregnancy, bodybuilding (ingest more than you excrete)

19
Q

When would you find NEGATIVE nitrogen balance?

A

starvation, trauma, infection, cancer, burn, sepsis

rate of protein synthesis is less than degradation so muscle mass decreases

20
Q

Urea biosynthesis occurs in the _________ and is excreted by the ___________

A

liver and kidney

21
Q

amino groups from amino acids are converted into what amino acid?

A

glutamate

22
Q

What is the pathway of nitrogen from an amino acid to urea?

A

NH2 group —-> glutamate ——> ammonia and aspartate —-> urea

23
Q

Define transamination

A

transfer of an amino group to alpha ketoglutarate to form glutamate

24
Q

True or false: there is just one transaminase

A

FALSE; there are multiple that act on specific amino acids

25
Q

What are the 2 transaminases that are important in clinical diagnosis?

A

1) Alanine transaminase
2) Asparate transaminase

both levels increase in the serum in times of liver failure

26
Q

What are the steps in urea synthesis?

A

1) transamination (move NH2 groups to glutamate)
2) production of aspartate and ammonia (formed from glutamate)
3) synthesis of urea from ammonia and aspartate

27
Q

Does urea synthesis consume or produce ATP?

A

consume

28
Q

Where in the cell does urea synthesis take place?

A

1) carbamoyl phosphate and citrulline synthase takes place in MITOCHONDRIA
2) all others in cytosol

29
Q

___________ enters the mitochondria and ___________ leaves it in the formation of urea

A

ornithine (IN); citrulline (OUT)

30
Q

increased levels of glutamate lead to increased ___ ____________ which activates the enzyme that makes carbomoyl phosphate

A

N-Acetylglutamate

31
Q

What are the two transporters of nitrogen to the liver?

A

1) alanine

2) glutamine

32
Q

What are the 2 ways to get hyperammonemia?

A

1) acquired (cirrhosis)

2) genetic (deficiency of enzyme in urea biosynthesis)

33
Q

Define glucogenic

A

yields TCA cycle intermediates or pyruvate that can be used for gluconeogenesis

34
Q

Define ketogenic

A

yields acetyl CoA, acetoacetyl CoA, or acetoacetate

35
Q

What are the only exclusively ketogenic amino acids?

A

lysine, leucine (two L amino acids)

36
Q

What amino acids are both ketogenic and glucogenic?

A
isoleucine
phenylalanine
threonine
tryptophan
tyrosine

(All the T’s –> think of T as plus sign. glucogenic + ketogenic)

37
Q

During an overnight fast, there is net protein ___________

A

degradation