Amino Acids Flashcards

1
Q

What type of acid contains & produces the most energy?

A

fatty acids

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2
Q

What are the sources of carbon?

A
  • TCA cycle
  • glycolysis
  • PPP
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3
Q

What is both an essential & nonessential amino acid?

A

arginine

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4
Q

What is the difference between endopeptidase & exopeptidase?

A
  • endo: cleaves internal peptide bonds
  • exo: cleaves amino acids one at atime from the carboxyl or amino end
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5
Q

What 2 amino acids are only ketogenic?

A

leucine & lysine

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6
Q

What amino acid is considered a major ketogenic?

A

leucine

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7
Q

How are proteins broken down into glucogenic amino acids?

A

Converted into intermediates used to make glucose

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8
Q

How are proteins broken down into ketogenic amino acids?

A

Converted into intermediates used to make ketone bodies

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9
Q

What are the 3 ways oxygen degradation can happen?

A
  1. normal amino acid metabolism
  2. excess dietary protein
  3. starvation or diabetes
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10
Q

What is th elocation of oxygen degradation of amino acids?

A

liver

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11
Q

What is the function of oxidative degradation of amino acids?

A

amino groups are removed from amino acids

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12
Q

What are the 2 metabolic fates of amino groups?

A
  1. Ammonia can be used in the synthesis of other amino acids
  2. Ammonia can be used in the urea cycle and excreted via urination
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13
Q

Aminotransferases exist for all amino acids except for what?

A

Thr & Lys

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14
Q

What is the key enzyme & cofactor for transamination?

A
  • enzyme: aminotransferase
  • co-factor: PLP
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15
Q

What are the characteristics of glutamate dehydrogenase reaction?

A
  • function: glutamate <-> alpha-ketoglutarate + NH4
  • location: liver mitochondria
  • enzyme: glutamate dehydrogenase
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16
Q

How is the glutamate dehydrogenase reaction regulated?

A
  • activated by ADP
  • inhibited GTP
  • flipped when alpha-keto -> glutamate
17
Q
A
18
Q

What are the required co-factors for glutamate dehydrogenase reaction?

A

NAD or NADP
* flipped when alpha-keto -> glutamate

19
Q

What is the major transport form of ammonia & most abundant amino acid in the blood?

A

glutamine

20
Q

What are the characteristics of the glutamine synthetase reaction?

A
  • function: glutamate + NH4 -> glutamine
  • location: extra-hepatic tissues
21
Q

What si the key enzyme & required cofactor glutamine synthetase reactions?

A
  • enzyme: glutamine synthetase
  • cofactor: ATP
22
Q

What are the characteristics for the glutaminase reaction?

A
  • function: glutamine -> glutamate + NH4
  • location: liver mitochondria
  • enzyme: glutaminase
23
Q

What are the links to the TCA cycle from the urea cycle?

A
  • OAA
  • alpha-keto
  • fumarate
24
Q

What are the characteristics of the urea cycle?

A
  • function: disposal of nitrogen
  • location: mitochondria & cytosol in liver
  • rate limiting enzyme: carbamoyl phosphate synthetase 1
25
Q

What are the 2 ways used to enter the urea cycle?

A

carbamoyl phosphate & aspartate

26
Q

How is the urea cycle regulated?

A

at rate limiting step -> N-acetylglutamate = allosteric activator of CPS 1

27
Q

What is marasmus?

A
  • inadequate intake of both protein & caloric energy
  • symptom: loss of fat reserves & muscle mass
28
Q

What is Kwashiorkor syndrome?

A
  • inadequate intake of just protein
  • symptom: Easy hair pluckability, Pitting edema, Skin breakdown, Delayed wound healing