Amino Acid Metabolism Flashcards

1
Q

What must occur to proteins before they are absorbed in the intestines, and what enzyme faciliates this reaction?

A

proteolytic enzyms.

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2
Q

Tripeptides and Dipeptides are broken down by what enzyme before they are released in the blood?

A

peptidases

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3
Q

What are required for intracellular protein turnover?

A

proteasomes

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4
Q

In the production of ammonia, an amino group is transferred to what other amino acid?

A

glutamate

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5
Q

What enzyme transfers an amino acid to glutamate?

A

aminotransferase

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6
Q

What enzyme involves glutamate and the production of NADH, as well as urea?

A

dehydrogenase

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7
Q

Where does the urea cycle occur?

A

The liver

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8
Q

What components of the urea cycle are found in the liver?

A

carbamoyl phosphate and citrulline

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9
Q

What enzyme helps funnel nitrogens into the urea cycle?

A

aminotransferase

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10
Q

In the brain, the conversion of alpha ketoglutarate to glutamate is facilitated by what enzyme?

A

glutamate dehydrogenase

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11
Q

In the brain, the conversion of glutamate to glutamine synthetase is facilitated by what enzyme?

A

glutamine synthetase

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12
Q

In the brain, alpha ketoglutarate must be converted into what amino acid before it can travel to the bloodstream?

A

Glutamine

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13
Q

What does the liver convert glutamine into so that it can go into the urea cycle?

A

ammonium (NH4+)

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14
Q

What enzyme in the liver converts glutamine into glutamate?

A

glutaminase

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15
Q

What is the purpose of the glucose-alanine cycle?

A

To remove excess ammonia from the muscles.

It involves converting alanine and glutamate into ammonium.

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16
Q

What are the two major types of reactions that remove nitrogen?

A

deamination

trans-amination

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17
Q

True or false: only amino acids (di and tripeptides) get into the bloodstream.

A

true

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18
Q

Does pepsinogen or pepsin break down things in the stomach?

A

pepsin

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19
Q

What is the role of trypsinogen?

A

To break down proteins into amino acids.

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20
Q

Proteins can be degraded via two methods. What are they?

A

lysosomal breakdown

proteosomes

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21
Q

The carbon skeleton from proteins can bue used for what?

A

cellular respiration.

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22
Q

The first step of the urea cycle is what type of reaction?

A

trans-amination (transfer of an amino group).

Glutamate is made.

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23
Q

Once amino acids have formed glutamate, what happens to them?

A

They undergo dehydrogenation to become urea.

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24
Q

What is the rate-limiting step of the urea cycle?

A

The production of carbamoyl phosphate from ammonium and carbon dioxide.

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25
Q

How is ammonium toxic to the brain?

A

Because the brain is de-energized when there is an excess amount of ammonia.

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26
Q

Protein breakdown in the muscles helps to regulate the balance of what?

A

nitrogen

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27
Q

What enzyme converts carbon dioxide into carbamoyl phosphate?

A

carbamoyl phosphate synthetase I.

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28
Q

What enzyme converts carbamoyl phosphate to citruline?

A

transcarbamoylase

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29
Q

What enzyme converts citrulline to argininosuccinate?

A

argininosuccinate synthetase

30
Q

What enzym converts arginosuccinate into arginate?

A

arginosuccinate lyase

31
Q

What enzyme converts arginine to ornithine?

A

argininase I

32
Q

What is needed between ornithin and citruline?

A

An ornithine/citrulline transporter.

33
Q

What does glucogenic mean?

A

an amino acid that is capable of making glucose.

34
Q

What does ketogenic mean?

A

The ability to make ketones

35
Q

Where does citro-anemia occur?

A

Between citrulline and arginosuccinate.

36
Q

A deficiency in enzymes does what to BUN levels?

A

Causes BUN levels to decrease.

37
Q

What is a positive NB?

A

Amount of nitrogen intake is higher than nitrogen excretion.

38
Q

What is negative NB?

A

nitrogen excretion is higher than intake

Is the case in starvation/malnutrition

39
Q

Where do the amino groups in urea come from?

A

glutamate and aspartate

40
Q

What urea cycle intermediate is shuttled into the mitochondria?

A

ornithine

41
Q

What enzyme catalyzes the rate-limiting step of the urea cycle?

A

carbamoyl phosphate synthetase

42
Q

Heme is a ___ containing compound

A

Nitrogen

43
Q

What is the rate determining step of heme synthesis?

A

the reaction of succinyl CoA and glycine.

44
Q

What vitamin is required in the first reaction of heme synthesis?

A

vitamin B6

45
Q

What is the enzyme used in the rate-determing step?

A

allosynthase

46
Q

What organ is affected by acute intermittent porphyria?

A

The liver

47
Q

Congenital erythropoietic porphyria has an effect on what?

A

red blood cells

48
Q

What protein carries bilirubin in the blood?

A

albumin

49
Q

Conjugated bilirubin is associated with what sugar?

A

diglucuronide

50
Q

What distinguishes the conjugated and nonconjungated (indirect) bilirubins?

A
The conjugate rubin is solubule and can be tested in a blood sample. 
Th nonconjugated (indirect) has to be separated from albumin.

Conjugated bilirubin has the diglucuronide

51
Q

Histamine is derived from what amino acid?

A

Histidine

52
Q

Sphingosine is derived from what amino acid?

A

serine

53
Q

Thyroxine is derived from what amino acid?

A

tyrosine

54
Q

Epinephrine is derived from what amino acid?

A

tyrosine

55
Q

Serotonin is derived from what amino acid?

A

tryptophan

56
Q

NAD is derived from what amino acid?

A

tryptophan

57
Q

Nitric oxide is derived from what amino acid?

A

arginine

58
Q

What cofactor dos nitric oxide need?

A

BH4

59
Q

What is nNOS?

A

neuronal nitric oxide synthase. IT is expressed in neurons and produces nitric oxide as a neurotransmitter.

60
Q

What is iNOS?

A

inducable nitric oxide synthase. It is found in the immune system and is a killer compound to bacteria and microorganisms.

61
Q

What is eNOS?

A

endothelial-derived nitric oxide synthse. It acts as a vasodilator and is produced in endothelium. It moves through the surrounding muscle and relaxes.

62
Q

What are porphyrins synthesized from?

A

glycine and succinyl CoA

63
Q

What enzyme converts delta-amino levullinate into porphobillnogen?

A

ALA dehydratase.

It is associated with lead poisoning.

64
Q

What enzyme converts porphobillnogen into a linear tetrapyrrole?

A

prophobilinogen deaminase

It is associated with acute intermittent porphyria

65
Q

What enzme converts a linear tetrapyrrole into uroporphyrinogen III?

A

uroporphyrinogen III synthase

It is associated with congenital erythropoetic porphyria

66
Q

What enzyme converts urophyrinogen III into corproporphyrinogen III?

A

uroporphyrinogen decarboxylase

67
Q

The heme degradation products (billverdin and Billrubin) are responsible for what?

A

the color of bruises

68
Q

What are the degradation products of heme?

A

billiverdin and billirubin

69
Q

Glutathione reacts with hydrogen peroxide and organic peroxides. What does this indicate that glutathione is?

A

an antioxidant

70
Q

Selenium is important in what system?

A

The glutathoine system

71
Q

Protein digestion leads to absorption of what?

A

amino acids and di (tri) peptides.