Nitrogen Metabolism Flashcards

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1
Q

Which three ways must amino acids be obtained from?

A

1) The diet
2) de novo synthesis
3) Recovered from Protein degradation

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2
Q

What is the first step for catabolism?

A

removal of alpha-amino acid group by transamination to form Ammonia and alpha-keto acid

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3
Q

What is the second phase of catabolism?

A

alhpa-keto acids are converted to metabolic pathway intermediates such as CO2, H2O, Glucose, fatty acids of Ketone bodies

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4
Q

Where does some ammonia go during catabolism?

A

Some ammonia is lose in urine but most becomes urea

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5
Q

How does nitrogen leave the body?

A

Urea or ammonia within faeces

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6
Q

What is the amino acid pool supplied by?

A
  • Amino acids from degraded body proteins
  • Amino acids from dietary proteins
  • Synthesis of nonessential amino acids from simple intermediates
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7
Q

How is the amino acid pool depleted?

A
  • Protein synthesis
  • Nitrogen-containing molecule precursors
  • Conversion to glucose, glycogen, fatty acids and ketone bodies
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8
Q

What is protein turnover?

A

The amount of protein hydrolysed and resynthesised each day

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9
Q

How is protein degraded?

A
  • ATP dependent ubiquitin-proteasome system (endogenous proteins)
  • ATP independent enzyme system of the lysosome (extracellular proteins)
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10
Q

What is the ubiquitin-proteasome proteolytic pathway?

A

Ubiquination is linkage of ubiquitin’s alpha-carboxyl group to amino group of lysine

the degradation is determined by the oxidation levels and PEST sequences

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11
Q

How does protein digestion occur?

A

Degraded by enzymes produced in stomach, pancreas & small intestine

Stomach secretes gastric juices containing:

  • Hydrochloric acid (denatures proteins)
  • Pepsin (acid-stable endopeptidase that releases amino acids and peptides)

Pancreas produces proteases: -Varying specificity for amino acid R-groups

Small intestine contains aminopeptidases (exopeptidases) which cleave at N-terminal residues to produce smaller peptides & free amino acids

Free amino acids are taken in by Na+ linked secondary transport system

Di- & Tri-peptides are taken in by H+ linked transport of hydrolysed into amino acids in the cytosol then released by facilitated diffusion

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12
Q

How many transport systems exist for amino acids?

A

7

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13
Q

What is transamination?

A

Amino group transferal to glutamate which can be oxidatively deaminated or used as an amino group donor so it is called a non-essential amino acid synthesis

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14
Q

Where are aminotransferases found and how are they involved in nitrogen removal?

A
  • found in cytosol and mitochondria of liver, kidney, intestine and muscle
  • Transfer amino groups and each aminotransferase is specific to one or a few amino group donors
  • Equilibrium close to 1 therefore reversible
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15
Q

What is oxidative deamination?

A

results in amino group release as ammonia which occurs in the liver or kidney
-also creates alpha-keto acids to enter energy metabolism

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16
Q

How can glutamate undergo rapid oxidative deamination?

A

Use of enzyme glutamate dehydrogenase

17
Q

What are the components of Urea?

A

major disposal method of amino acids

  • accounts for 90% of Nitrogen containing compounds in urine
  • 1 Nitrogen from free ammonia, other from aspartate
18
Q

What are the reactions of the Urea Cycle?

A

1) Ornithine & citrulline move across the inner membrane via co-transporter
2) Arginiosuccinate formation uses the last molecule of ATP
3) Fumarate is hydrated to malate

19
Q

What is the overall stoichiometry of the Urea Cycle?

A

Aspartate + NH3 + HCO3 + 3ATP +H20 = Urea + Fumarate + 2ADP + AMP + 2pi +PPi

20
Q

What are the problems with Ammonia in the body?

A

Level of ammonia must be kept very low as slightly elevated concentrations are toxic to the CNS

Symptoms include: tremors, speech slurring, drowsiness, blurred vision, coma, death

21
Q

What is acquired hyperammonemia:

A
  • Liver diseases (viral hepatitis, alcohol)

- Liver cirrhosis result in redirection of blood flow so blood ends up in circulation rather than liver

22
Q

What is congenital hyperammonemia?

A

Genetic deficiencies of urea cycle enzymes

23
Q

What compounds are formed due to the conversion of carbon skeletons?

A
  • Oxoloacetate
  • Pyruvate
  • alpha-ketoglutarate
  • fumarate
  • succinyl CoA
  • Acetyl CoA
  • Acetoacetate

These compounds result in:

  • Glucose
  • Lipid
  • Energy generation through TCA cycle
24
Q

What are the different classes of amino acids?

A
  • Glucogenic
  • Ketogenic
  • Both
25
Q

What are glucogenic amino acids?

A

-Catabolism yields pyruvate or TCA cycle intermediate

substrates for gluconeogenesis

26
Q

What are ketogenic amino acids?

A

-Catabolism yields acetoacetate or acetyl CoA or any carbon skeleton that can’t lead to glucose