Chapter 21: Amino Acid Metabolism Flashcards

1
Q

Why are amino acids unique?

A

Only macromolecule containing nitrogen.

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2
Q

Do amino acids get stored in the cell?

A

No

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3
Q

What are AA converted into?

A

Not excreted. There are converted into common metabolites such as precursors to glucose, fatty acids, and ketone bodies.

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4
Q

What are proteins denatured for? (3)

A

1) To store nutrients in the form of proteins and to break them down in times of metabolic need, processes that are especially important to muscles.

2) To eliminate abnormal proteins to prevent accumulation.

3) To permit the regulation of cellular metabolism by eliminating superfluous
enzymes and regulatory proteins.

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5
Q

What do lysosomes do?

A

Carry out autophagy (nonselective degradation)

Under starvation conditions, lysosomes may be selective

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6
Q

Where else can protein degradation occur outside lysosomes?

A

Ubiquitin, a protein

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7
Q

Covalently linking proteins to ubiquitin will do what?

A

Mark them for degradation.

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8
Q

For degradation to occur, ubiquitinated proteins ______

A

must be linked together.

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9
Q

1st transamination reaction:

A
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10
Q

2nd transamination reaction:

A
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11
Q

Can glutamate be deaminated?

A

Yes, by glutamate dehydrogenase to yield ammonia and a-ketoglutarate

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12
Q

Ammonia + Asparate = ?

A

Urea + Fumarate

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13
Q

1st committed step of urea cycle?

A

To make carbamoyl phosphate.

Catalyzed my carbamoyl phosphate synthetase I

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14
Q

Component needed to make carbamoyl phosphate?

A

N-acetylglutamate

Synthesized my glutamate and acetyl-coA. Catalyzed by N-acetylglutamate synthase.

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15
Q

Why does glutamate increase when amino acid breakdown increases?

A

Increases glutamate stimulates N-acetylglutamate synthesis, which results in activation of carbamoyl phosphate synthetase to increase urea production.

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16
Q

Strictly ketogenic amino acids:

A

Lysine and leucine

17
Q

General ketogenic amino acids:

A
  • leucine
  • lysine
  • isoleucine
  • threonine
  • phenylalanine
  • tryptophan
  • tyrosine
18
Q

Amphibolic amino acids:

A
  • phenylalanine
  • isoleucine
  • threonine
  • tryptophan
  • tyrosine
19
Q

Glucogenic amino acids:

A
  • alanine
  • arginine
  • asparagine
  • aspartic acid
  • cysteine
  • glutamic acid
  • glutamine
  • glycine
  • histidine
  • methionine
  • proline
  • serine
  • valine
20
Q

Amino acids that are degraded to pyruvate?

A

Alanine, cysteine, glycine, serine, and threonine.

21
Q

Amino acids that are degraded to oxaloacetate?

A

Asparagine and aspartate.

  • by means of transamination
22
Q

Amino acids that are degraded to a-ketoglutarate?

A

Arginine, glutamate, glutamine, histidine, and proline.

23
Q

Amino acids that are degraded to succinyl-CoA?

A

Methionine, threonine, isoleucine, and valine.

24
Q

Degradation of branched chain amino acids involved Acyl-CoA Oxidation?

A
  1. transamination to corresponding a-keto acid
  2. oxidative decarboxylation to the corresponding acyl-CoA
  3. dehydration by FAD to form a double bond
25
Q

Amino acids that are degraded to Acetyl-CoA/ Acetoacetate?

A

Leucine and lysine

26
Q

Amino acids that are degraded to alanine and Acetoacetate?

A

Tryptophan

27
Q

Amino acids that are degraded to fumarate and acetoacetate?

A

Phenylalanine and tyrosine.

28
Q

Essential amino acids?

A

Arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine

29
Q

_____ is made by the body, but it is still an essential amino acid.

A

Arginine

*can be made via the urea cycle, not enough quantities to support growth and development

30
Q

What are nonessential amino acids synthesized from?

A

Common metabolites, such as pyruvate/oxaloacetate/a-ketoglutarate

31
Q

What is the central control point in nitrogen metabolism?

A

Glutamine synthetase

32
Q

Taste and how humans evolved, we can taste amino acids and allows us to pick up nitrogen. More often than not we are tasting _____

A

Glutamate

33
Q

Why is tryptophan synthesis unique?

A

We take an indole rings and add a serine to it to get tryptophan. Indole provided bicyclic part and serine adds amino and carboxylic terminal ends.

34
Q
A