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**Biochemistry > Amino Acid Metabolism: Oxidation And Urea > Flashcards

Amino Acid Metabolism: Oxidation And Urea Flashcards

1
Q

Name the 4 fates of Dietary Amino Acids

A
  1. Protein Synthesis
  2. Energy Production (Citric Acid Cycle)
  3. Biosynthesis
  4. Urea Excretion
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2
Q

Name the 3 drivers of Protein Oxidation

A
  1. Normal synthesis and degradation
  2. Protein rich diet
  3. Starvation or diabetes Mellitus
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3
Q

What does CCK do?

A

Stimulates zymogen release from the pancreas.

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4
Q

What does secretin do?

A

Stimulates the release of bicarbonate from the pancreas

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5
Q

Describe Pepsin

A
  • It is a Protease

- Hydrolyzes Phe, Trp, and Tyr polypeptide bonds

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6
Q

What is stimulated by Gastrin Secretion?

A
  1. Causes chief cells to release Pepsinogen

2. HCL release (parietal cells)

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7
Q

How are cytoplasmic proteins broken down?

A

Tagged with ubiquitin and taken to proteosome

Lysosomes also break down proteins but not as much

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8
Q

What leads to Gastrin secretion?

A

Presence of Dietary proteins

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9
Q

Define Zymogen

A

An enzyme precursor that requires a biochemical change for activation, typically cleavage

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10
Q

In a low pH environment what happens to pepsinogen?

A

It is activated and becomes pepsin

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11
Q

Name 3 Pancreatic Zymogens and what they are cleaved to when they become activated

A
  1. Trypsinogen: Trypsin
  2. Chymotrypsinogen: chymotrypsin
  3. Procarboxypeptidase A and B: Carboxypeptidase A and B
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12
Q

What is the basic strategy for amino group catabolism in the liver?

A

Separate the amine group, leave the carbon chain

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13
Q

_________ is the source of most amino acids

A

Diet

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14
Q

Most amino acid catabolism occurs in _________

A

The liver

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15
Q

Name the 4 metabolically important amino acids

A
  1. Glutamate
  2. Glutamine
  3. Aspartate
  4. Alanine
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16
Q

What are the 4 Metabolically important amino acids used as?

A
  1. Amine group carriers
  2. Precursors and common metabolites
  3. Entry and exit molecules from the citric acid cycle
17
Q

How are amine groups stabilized?

A

As urea or uric acid for excretion

18
Q

Name two common amino acid catabolism reactions

A
  1. Transaminase Reactions

2. One-Carbon Transfers

19
Q

What is PLP?

A
  • Pyridoxal Phosphate
  • It is a common coenzyme
  • It is a carrier of amino groups
  • Also Vitamin B6 (Essential Vitamin)

*From his slides it looks like it is particularly involved in Transaminase reactions

20
Q

T/F Glutamine is Toxic

A

FALSE: it is non-toxic

21
Q

How is Intra cellular ammonia buffered?

A

By converting glutamate to glutamine

22
Q

Describe the urea cycle.

A
  1. Forms urea, a stable amine-rich molecule that can safely excrete nitrogen
  2. Requires enzymes within the mitochondria and cytoplasm
  3. There are 4 steps and 5 structural changes
  4. ATP-Dependent
  5. Ornithine is absolutely essential
23
Q

What 3 molecules enter into first stages of urea cycle?

A
  1. Glutamine
  2. Glutamate
  3. Alanine
24
Q

How is urea cycle regulated?

A

Two levels of regulation:

  1. Increased synthesis of
    • Ornithine Transcarbomoylase
    • Arginosuccinate synthetase
    • Arginosuccinase
    • Arginase
  2. Allosteric carbonyl phosphate synthetase 1 regulation
25
Q

Name the 6 amino acids degraded to pyruvate

A
  1. Tryptophan
  2. Alanine
  3. Cysteine
  4. Serine
  5. Glycine
  6. Threonine
26
Q

Name the 7 amino acids that are degraded to Acetyl-CoA

A
  1. Tryptophan
  2. Lysine
  3. Phenylalanine
  4. Tyrosine
  5. Leucine
  6. Isoleucine
  7. Threonine
27
Q

Name the 5 amino acids degraded to alpha ketoglutarate

A
  1. Glutamate
  2. Glutamine
  3. Proline
  4. Arginine
  5. Histidine
28
Q

Name the 4 amino acids degraded so Succinyl-CoA

A
  1. Methionine
  2. Isoleucine
  3. Valine
  4. Threonine
29
Q

Name the 2 amino acids degraded to oxaloacetate

A
  1. Asparagine

2. Aspartate

30
Q

Which amino acids can be converted to Acetoacetyl-CoA prior to forming Acetyl-CoA

A
  1. Leucine
  2. Lysine
  3. Phenylalanine
  4. Tryptophan
  5. Tyrosine

**Biochemistry (6 decks)

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