Amino Acid Pool and Nitrogen Metabolism
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Questions and Answers

What is the approximate amount of amino acids in a 70-kg man?

  • 1-2 kg
  • 400 g
  • 90-100 g (correct)
  • 12 kg
  • In healthy individuals, what is the state of the amino acid pool?

  • In a steady state (correct)
  • In a state of deficiency
  • In a state of excess
  • In a state of flux
  • What happens to amino acids not used in biosynthetic reactions?

  • They are converted to glucose
  • They are burned as a fuel (correct)
  • They are excreted
  • They are stored in the body
  • What is the purpose of protein degradation?

    <p>To remove abnormal or unneeded proteins</p> Signup and view all the answers

    What determines the concentration of protein in the cell for many proteins?

    <p>Rate of synthesis only</p> Signup and view all the answers

    What happens to the total amount of protein in the body in healthy adults?

    <p>It remains constant</p> Signup and view all the answers

    What type of modification can lead to preferential degradation of some proteins?

    <p>Ubiquitination</p> Signup and view all the answers

    What is the significance of N-terminal residues on protein half-life?

    <p>They influence protein half-life</p> Signup and view all the answers

    What occurs when the carbonyl group of the peptide bond is contributed by arginine or lysine?

    <p>Trypsin cleaves the peptide bond</p> Signup and view all the answers

    What is the significance of PEST sequences in proteins?

    <p>They target proteins for rapid degradation</p> Signup and view all the answers

    What is the function of enteropeptidase?

    <p>To convert trypsinogen to trypsin</p> Signup and view all the answers

    Why must dietary proteins be hydrolyzed in the intestine?

    <p>Because they are too large to be absorbed</p> Signup and view all the answers

    What is the result of enteropeptidase converting trypsinogen to trypsin?

    <p>An increase in proteolytic activity</p> Signup and view all the answers

    What is the role of cholecystokinin and secretin in pancreatic zymogen release?

    <p>They mediate the release and activation of pancreatic zymogens</p> Signup and view all the answers

    What is the typical daily intake of protein in the American diet?

    <p>70-100 g/day</p> Signup and view all the answers

    What is an exception to the rule that proteins are too large to be absorbed by the intestine?

    <p>Newborns' ability to absorb maternal antibodies</p> Signup and view all the answers

    What is the purpose of synthesizing pancreatic proteases as inactive zymogens?

    <p>To prevent the digestion of pancreatic cells</p> Signup and view all the answers

    What is the main function of trypsin in terms of activating other pancreatic zymogens?

    <p>It converts them to their active forms</p> Signup and view all the answers

    Where are D-amino acids found?

    <p>In plants and microorganisms</p> Signup and view all the answers

    What is the function of D-amino acid oxidase?

    <p>To degrade D-amino acids</p> Signup and view all the answers

    What is the byproduct of the reaction catalyzed by D-amino acid oxidase?

    <p>α-keto acids, ammonia, and hydrogen peroxide</p> Signup and view all the answers

    What is the purpose of glutamine synthetase?

    <p>To transport ammonia to the liver</p> Signup and view all the answers

    What is the fate of glutamine in the liver?

    <p>It is cleaved by glutaminase to produce glutamate and ammonia</p> Signup and view all the answers

    What is the significance of D-amino acid oxidase activity?

    <p>It is linked to increased susceptibility to schizophrenia</p> Signup and view all the answers

    What is the purpose of the glucose-alanine cycle?

    <p>To transport amino acids from muscle to liver</p> Signup and view all the answers

    What is the major disposal form of amino groups derived from amino acids?

    <p>Urea</p> Signup and view all the answers

    Where are the first two reactions of the urea cycle located?

    <p>Mitochondria</p> Signup and view all the answers

    What is the source of the carbon and oxygen in urea?

    <p>CO₂</p> Signup and view all the answers

    What is the enzyme responsible for the oxidative deamination of glutamate?

    <p>Glutamate dehydrogenase</p> Signup and view all the answers

    Where is urea produced and then transported to for excretion?

    <p>Liver and kidneys</p> Signup and view all the answers

    Study Notes

    Amino Acid Pool and Nitrogen Metabolism

    • The amino acid pool consists of approximately 90-100 g of amino acids, a small amount compared to the 12 kg of protein in the body of a 70-kg person
    • In healthy, well-fed individuals, the input to the amino acid pool is balanced by the output, resulting in a steady state and nitrogen balance

    Protein Turnover

    • Proteins in the body are constantly being synthesized and degraded to remove abnormal or unneeded proteins
    • Regulation of synthesis determines protein concentration in the cell, with degradation playing a minor role for some proteins
    • In healthy adults, the rate of protein synthesis is sufficient to replace degraded protein, maintaining a constant total amount of protein in the body

    Chemical Signals for Protein Degradation

    • Proteins have different half-lives, indicating that degradation is influenced by structural aspects of proteins
    • Chemical modifications, such as oxidation or ubiquitin tagging, can mark proteins for degradation
    • The nature of the N-terminal residue affects protein half-life, with serine resulting in long-lived proteins and aspartate in short-lived proteins
    • Proteins with PEST sequences (proline, glutamate, serine, and threonine) are rapidly degraded

    Digestion of Dietary Proteins

    • Most nitrogen in the diet comes from protein (70-100 g/day in the American diet)
    • Proteins must be hydrolyzed to di- and tripeptides and amino acids for absorption
    • Pancreatic proteases, such as trypsin, cleave proteins into smaller peptides and amino acids in the small intestine

    Activation of Pancreatic Zymogens

    • Pancreatic zymogens are activated by enteropeptidase, an enzyme on the luminal surface of intestinal mucosal cells
    • Trypsin, once activated, can convert other trypsinogen molecules to trypsin, creating a cascade of proteolytic activity

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    Description

    This quiz covers the concept of the amino acid pool, its size, and its role in whole-body nitrogen metabolism, including the steady state and nitrogen balance in healthy individuals.

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