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Adv Nutrition Proteins > Protein 3 > Flashcards

Protein 3 Flashcards

1
Q

What are Transamination and deamination methods for?

A

Protein degradation

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2
Q

Products of Transamination

A

Forms a new AA and a new α-keto acid

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3
Q

2 Primary Enzymes:

transaminases

A

–Alanine aminotransferase (ALT)

–Aspartate aminotransferase (AST)

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4
Q

Alanine + alpha keto acid =

A

Pyruvate + alpha AA

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5
Q

Alpha keto acid + aspartate =

A

Alpha AA + oxaloacetate

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6
Q

Carbon skeleton of glutamate

A

Alpha keto acid

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7
Q

Carbon skeleton of alanine

A

Pyruvate

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8
Q

Carbon skeleton of aspartate

A

Oxaloacetate

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9
Q

Deamination

A

Removal of amino group from AA by lyases, dehydratases or dehydrogenases

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10
Q

Products of deamination

A

Alpha keto acid and ammonia

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11
Q

4 commonly delaminated AA

A

Glutamate

Histidine

Serine

Glycine

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12
Q

What’s important about the products of deamination

A

Ammonia occurs in equilibrium with ammonium ion

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13
Q

At normal physiological pH which is preferred?

Ammonium ion or ammonia

A

Ammonium ion

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14
Q

What organ removes ammonia produced by deamination reaction

A

Liver

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15
Q

Ammonia is toxic to what

A

Central nervous system

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16
Q

Why is ammonia toxic to CNS

A

Ammonia reacts with alpha ketoglutarate to form glutamate. Which depletes the brain of alpha ketoglutarate

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17
Q

What are some side effects of ammonia intoxication

A

tremor, slurred speech, blurred vision, coma, and death

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18
Q

What are the 3 enzymes involved in ammonia disposal

A

Glutamate dehydrogenase

Glutamine synthetase

Carbomoyl phosphate synthase I (CPSI)

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19
Q

What are the three substrates used by glutamate dehydrogenase

A

Uses NADPH, +NH4 and α-ketoglutarate

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20
Q

What is the product of glutamate dehydrogenase reaction

A

Glutamate

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21
Q

What are the three substrates used by glutamine synthetase

A

Uses ATP, glutamate, +NH4

22
Q

What is the product of glutamine synthetase reaction

A

Glutamine

23
Q

What is the product of CPSI

A

Carbomoyl phosphate

24
Q

What are the 4 substrates for CPSI reaction

A

ATP, ammonia, CO(2), N-Acetyl glutamate

25
Q

What is CPSI involved in

A

Urea cycle

26
Q

What is urea made of

A

Urea contains one nitrogen from ammonia and one from aspartate – the carbon comes from CO2 or HCO3-

27
Q

What is the effect of high protein diet and starvation on urea synthesis

A

Can increase synthesis of enzymes involved in urea cycle

28
Q

Glucagon and glucocorticoids effect on urea synthesis

A

Increase its activity

29
Q

What is the first intermediate in urea cycle?

What does it combine with and what is the product?

A

Carbomoyl phosphate

Ornithine

Citrulline

30
Q

What is the primary regulator of urea cycle

A

Carbamoyl phosphate synthase I

31
Q

Activity of the CPS1 is determined by

A

N-acetylglutamate

32
Q

Low levels of NAG have what effect on urea cycle

A

Decrease activity

33
Q

Tyrosine is an important precursor for what?

A

Hormones, neurotransmitters, melanin, and thyroid hormones

34
Q

Characteristic of tyrosine

A

Both glucogenic and ketogenic

35
Q

Characteristic of methionine

A

Glucogenic

36
Q

Methionine yields

A

Succinyl- CoA

37
Q

What are the steps of metabolism of methionine

A

–Conversion to S-adenosyl methionine (SAM) by methionine adenosyl transferase
–Demethylation of SAM by methyl transferase yields S-adenosyl homocysteine (SAH)
–SAH hydrolase converts SAH to homocysteine

38
Q

Is homocysteine supposed to be in high amounts in the body

A

No

39
Q

What are the two ways homocysteine can be converted back to methionine

A

–Betaine-dependent reaction which forms glycine

–Vitamin B12-folate-dependent reaction

40
Q

What is another fate of homocysteine

A

Homocysteine can be further catabolized by cystathionine synthase and cystathionine lyase to form cysteine

41
Q

Why is SAM important

A

Methyl donor

42
Q

SAM primarily acts on?

A

DNA to change its gene expression

43
Q

What 4 things is SAM required for synthesis of?

A

carnitine, creatine, epinephrine, melatonin

44
Q

What is SAM effect on methionine

A

Promotes methionine catabolism by stimulating cystathionine synthase, which converts homocysteine to cystathionine

45
Q

What is SAM important for preventing

A

Homocysteine build up

46
Q

What are some risks of high homocysteine levels

A

–Blood clots
•Coronary artery disease
•Stroke
–Dementia

47
Q

What are 4 cause of high homocysteine

A

–Defects in cystathionine synthase
–Vitamin B6 deficiency
–Vitamin B12 deficiency
–Folate deficiency

48
Q

Where does degradation of phenylalanine occur

A

Primarily liver and kidneys

49
Q

Phenylalanine is catabolized to?

A

Tyrosine

50
Q

What hormone activates and inhibits phenylalanine

A

Glucagon activates

Insulin inhibits

51
Q

Transamination

A

Transfer of an amino group from a AA to a α- keto acid (AA carbon skeleton)

Adv Nutrition Proteins (9 decks)

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