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Biological Psychology > Amino Acid Oxidation & the Urea Cycle (Biochemistry) > Flashcards

Amino Acid Oxidation & the Urea Cycle (Biochemistry) Flashcards

1
Q

What many amino acids are hydrophobic?

A

9

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2
Q

How many hydrophillic amino acids are there?

A

6

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3
Q

What are the charged amino acids that are acidic (negatively charged)

A
  • Aspartic acid
  • Glutamic acid
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4
Q

What are the charged amino acids that are basic (positively charged)

A
  • Lysine
  • Arginine
  • Histidine
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5
Q

What is Autophagy?

A

Cells break down their own components

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6
Q

Why does Autophagy occur?

A
  • Shortage of nutrients
  • Break down worn out organelles
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7
Q

What occurs to dietary amino acids that exceed body’s protein syntehsis?

A

They are degraded

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8
Q

Where does protein degradation happen?

A

In the gastrointestinal track

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9
Q

What is the function of pepsin?

A

Cutting protein into peptides in the stomach

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10
Q

Where does Trypsin and chymotrypsin cut proteins or large peptides?

A

Small intestine

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11
Q

What does aminopeptidase and carboxypeptidase A and B does to peptide in the small intestine

A

Degrade peptide into amino acids

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12
Q

What is the transportation pathway for amino acids?

A

Intestinal epithelium -> Blood -> Liver

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13
Q

What aare the issues with amino group metabolism?

A

Produce ammonium (NH4+) which is toxic

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14
Q

What removes alpha amino acids in Enzymatic transamination?

A

Aminotransferases

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15
Q

What does all aminotransferases require?

A

Pyridoxal phosphate cofactor

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16
Q

What is L-Glutamate function in Enzymatic Transamination?

A

Act as a temporary storage of nitrogen

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17
Q

What alpha - ketoglutarate accepts amino groups with?

A

L-glutamate

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18
Q

What is Glutamine?

A

Non toxic transport form of ammonia

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19
Q

What is released when Glutamine enters liver mitochondrias?

A

Ammonium ion

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20
Q

What is the Glucose-Alanine Cycle?

A

Excess nitrogen in extrahepatic tissues travels to the liver as amino acids

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21
Q

How is pyruvate coverted to alanine?

A

Recieving an amino group from glutamate

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22
Q

In pyruvate what is ammonium group replaced by?

A

Oxygen

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23
Q

What happens in Glutamate Dehydrogenase Reaction?

A

Two-electron oxidation of glutamate followed by hydrolysis

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24
Q

What is the net process of glutamate?

A

Oxidative deamination

25
Q

Where does Glutamate Dehydrogenase Reaction occur?

A

In the mitochondrial matrix

26
Q

What can be used as an electron acceptor in Glutamate Dehydrogenase Reaction?

A

NAD+ or NADP+

27
Q

What do aquatic vertebrates release into the environment?

A

Ammonia

28
Q

What are the methods of ammonia release into the environment by aquatic vertebrates?

A
  • Passive diffusion from epithelial cells
  • Active transport via gills
29
Q

What does terrestrial vertebrates and sharks excrete?

A

Urea

30
Q

What does birds and reptiles excrete?

A

Uric acid

31
Q

What are the upsides to urea?

A
  • Less toxic than ammona
  • Very soluble
32
Q

What are the upsids to uric acid?

A
  • Insouble
  • Excretion as paste allows to conserve water
33
Q

What are ammonotelic anaimals?

A

Most aquatic vertebrates (e.g bony fishes)

34
Q

What are ureotelic animals?

A

Terrestrial vertebrates and sharks

35
Q

What are uricotelic animals?

A

Birds and reptiles

36
Q

What is the purpose of synthesis of carbamoyl phosphate?

A

Recapturing ammonia

37
Q

What is the 1st step of the urea cycle?

A

Carbamoyl phosphate donates carbamoyl group to Ornithine

38
Q

What is the second 2nd step of the urea cycle?

A

Entry of Aspartate into the urea cycle
- Requires ATP and move through an intermediate step

39
Q

What is the second nitrogen acquiring reaction catalysed by?

A

Argininosuccinate synthetase

40
Q

What is step 3 in urea cycle?

A

Argininosuccinate is cleaved releasing fumarate & arginine

41
Q

What is the enzyme in step 3 of the urea cycle?

A

Argininosuccinase

42
Q

What is the side reaction in step 3 of the urea cycle?

A

Can enter mitochodnria to join the pool of citric cycle intermediates

43
Q

Arginine is cleaved to release urea and Ornithine. What stage of the urea cycle is this?

A

Step 4

44
Q

What is the catalystic in stage 4 of the urea cycle

A

Arginase

45
Q

How is the Urea Cycle regulated?

A
  • Protein rich diet
  • Starvation
46
Q

What is the long term to urea cycle regulation?

A

Regulation of the 4 urea cycle enzymes and carbamoyl synthetse I in the liver (Higher synthesis rates in starving animals)

47
Q

What is the short term regulation to urea cycle?

A

Activationr egulation of carbamoyl synthetase I via N-acetylglutamate synthase

48
Q

What links the urea and citric acid cycle?

A

Arginosuccinate Shunt

49
Q

How much does Arginosuccinate Shunt save?

A

3 ATP

50
Q

What are the amino acids that are used in Acetyl-CoA?

A

Leu (Leucine),
Ile (Isoleucine),
Thr (Threonine),
Lys (Lysine),
Phe (Phenylalanine),
Trp(Tryptophan),
Tyr (Tyrosine)

51
Q

What are the amino acids used in pyrvuate?

A

Ala (Alanine),
Thr (Threonine),
Trp(Tryptophan),
Cys (Cysteine),
Gly (Glyine),
Ser (Serine),

52
Q

What is the amino acids used in succinyl-CoA?

A

Met (Methionine)
Val (Valine)
Ile (Isoleucine),
Thr (Threonine),

53
Q

What are the amino acids used in alpha-ketoglutarate

A

Arg (Arginine)
Glu (Glutamic acid)
Gln (Glutamine)
His (Histidine)
Pro (Proline)

54
Q

What are the two amino acids used in fumarate?

A

(Phe) Phenylalanine
(Tyr) Tyrosine

55
Q

What molecules are ketogenic?

A
  • Acetoacetyl-CoA
  • Acetyl-CoA
56
Q

What molecules are Glucogenic?

A
  • Pyruvate
  • OXaloacetate
  • Fumarate
  • Succinyl-CoA
  • Alpha-Ketoglutarate
57
Q

What amino acids are exclusively ketogenic?

A

Lecuine, Lysine

58
Q

What molecule is exclusively Glucogenic?

A

Arginine,

59
Q

What amino acid is both ketogenic and glucogenic?

A

Phenylalanine, Tryptophan, Isoleucine, TYrosine

Biological Psychology (10 decks)

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