Overall Protein Metabolism Quiz
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Questions and Answers

What are glucogenic amino acids primarily used for?

  • To synthesize exclusively non-essential amino acids
  • To form urea and ammonia
  • To yield pyruvate or intermediates of the citric acid cycle (correct)
  • To directly produce ketone bodies
  • Which amino acids are classified as exclusively ketogenic?

  • Leucine and lysine (correct)
  • Phenylalanine and tyrosine
  • Alanine and glutamine
  • Valine and isoleucine
  • How do ketogenic amino acids differ from glucogenic amino acids?

  • Their catabolism yields ketone bodies (correct)
  • They can directly produce glucose in the liver
  • They are not involved in energy production
  • They yield glucose instead of ketones
  • What is the primary end product of amino acid catabolism for glucogenic amino acids?

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

    Which of the following processes does not involve glucogenic amino acids?

    <p>Formation of amino acids</p> Signup and view all the answers

    Which compounds are formed from the catabolism of amino acids in the ketosis process?

    <p>Ketone bodies like acetoacetate</p> Signup and view all the answers

    What role do amino acids play in the synthesis of non-essential amino acids?

    <p>They can serve as precursors for various compounds</p> Signup and view all the answers

    The carbon skeletons of which amino acids cannot enter gluconeogenesis?

    <p>Leucine and lysine</p> Signup and view all the answers

    What is the primary consequence of hyperammonemia on the brain?

    <p>Reduced cellular oxidation</p> Signup and view all the answers

    Where does the formation of urea primarily occur in the body?

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

    What is the primary role of enteropeptidase in protein digestion?

    <p>To activate trypsinogen into trypsin</p> Signup and view all the answers

    Which component is produced in the mitochondria during the urea cycle?

    <p>Carbamoyl phosphate</p> Signup and view all the answers

    What constitutes a positive nitrogen balance in the body?

    <p>Protein intake is greater than protein excretion</p> Signup and view all the answers

    What happens to ammonia levels in cases of compromised liver function?

    <p>They exceed normal levels</p> Signup and view all the answers

    Which of the following is NOT a factor associated with negative nitrogen balance?

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

    What percentage of the amino group disposal occurs through the urea cycle?

    <p>80-90%</p> Signup and view all the answers

    Which of the following describes a function of urea in the body?

    <p>A metabolic end product</p> Signup and view all the answers

    Which enzymes are primarily involved in protein digestion in the small intestine?

    <p>Trypsin, chymotrypsin, and carboxypeptidase</p> Signup and view all the answers

    What primarily happens to amino acids after they are absorbed?

    <p>They undergo various metabolic reactions, including deamination</p> Signup and view all the answers

    What is the primary effect of ammonia on the central nervous system?

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

    What is nitrogen equilibrium?

    <p>When protein synthesis and degradation rates are equal</p> Signup and view all the answers

    Which intermediate is essential in the citric acid cycle and is affected by hyperammonemia?

    <p>α-ketoglutarate</p> Signup and view all the answers

    In which condition is a negative nitrogen balance most likely to occur?

    <p>During an acute illness or infection</p> Signup and view all the answers

    Which route is NOT typically associated with nitrogen excretion?

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

    What are the enzymes that catalyze transamination reactions commonly called?

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

    What does the presence of elevated plasma aminotransferases primarily indicate?

    <p>Damage to cells rich in these enzymes</p> Signup and view all the answers

    Which amino acid is primarily formed during transamination reactions involving alanine?

    <p>Glutamic acid</p> Signup and view all the answers

    In which organ are aminotransferases especially abundant?

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

    Which aminotransferases are particularly noted for their diagnostic value?

    <p>AST and ALT</p> Signup and view all the answers

    In which condition are aminotransferases likely to be most elevated?

    <p>Prolonged circulatory collapse</p> Signup and view all the answers

    What is the primary role of aspartate aminotransferase (AST) in amino acid metabolism?

    <p>To transfer amino groups to oxaloacetate</p> Signup and view all the answers

    What primary transport mechanism for ammonia is used by muscle?

    <p>Transamination of pyruvate to form alanine</p> Signup and view all the answers

    What is the common reaction characteristic of aminotransferases?

    <p>They catalyze reversible reactions</p> Signup and view all the answers

    What is the role of glutaminase in the ammonia transport process?

    <p>To convert glutamine to glutamate and free ammonia in the liver</p> Signup and view all the answers

    In transamination involving pyruvic acid and α-ketoglutaric acid, which new product is formed?

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

    What is one outcome of ammonia toxicity in the body?

    <p>Shift in equilibrium towards glutamate formation</p> Signup and view all the answers

    What does a low level of aminotransferases in plasma typically signify?

    <p>Normal cellular function</p> Signup and view all the answers

    Which α-keto acid is frequently associated with the transamination reactions involving alanine?

    <p>α-Ketoglutaric acid</p> Signup and view all the answers

    Which cycle involves the conversion of alanine back to pyruvate in the liver?

    <p>Glucose-alanine cycle</p> Signup and view all the answers

    What is NOT a condition associated with elevated aminotransferases?

    <p>Frequent exercise</p> Signup and view all the answers

    Study Notes

    Overall Protein Metabolism

    • The body breaks down proteins into amino acids, which are then used for various purposes, including energy production, synthesis of new proteins, and production of other compounds.
    • Dietary protein is digested in the stomach and small intestine by proteolytic enzymes, producing amino acids.
    • Amino acids can be either glucogenic or ketogenic.
      • Glucogenic amino acids are broken down into intermediates that can be used for gluconeogenesis, the production of glucose.
      • Ketogenic amino acids are broken down into acetyl CoA and acetoacetyl CoA, which are used for ketogenesis, the production of ketone bodies.
    • Nitrogen balance is the difference between nitrogen intake and output.
      • Positive nitrogen balance occurs during growth, pregnancy, and muscular training.
      • Negative nitrogen balance occurs during starvation, malnutrition, gastrointestinal diseases, chronic hemorrhage, and increased protein catabolism.
    • Transamination reactions are catalyzed by aminotransferases, which transfer amino groups from an α-amino acid to an α-keto acid.
      • Alanine aminotransferase (ALT) transfers amino groups from alanine to α-ketoglutarate, producing pyruvate and glutamate.
      • Aspartate aminotransferase (AST) transfers amino groups from glutamate to oxaloacetate, producing aspartate and α-ketoglutarate.

    Diagnostic Value of Plasma Aminotransferases

    • Elevated plasma levels of aminotransferases indicate damage to cells rich in these enzymes.
    • Elevated AST and ALT are observed in liver diseases, such as hepatitis, toxic injury, and circulatory collapse.
    • Elevated aminotransferases can also be found in nonhepatic diseases, such as myocardial infarction and muscle disorders.

    Transport of Ammonia to the Liver

    • Ammonia is a toxic byproduct of amino acid metabolism.
    • Two mechanisms are used to transport ammonia to the liver:
      • Glutamine synthesis combines ammonia with glutamate to form glutamine, a nontoxic transport form. Glutamine is then transported to the liver and cleaved by glutaminase to produce glutamate and ammonia.
      • Glucose-alanine Cycle: Muscle transaminates pyruvate to form alanine, which is transported to the liver and converted back to pyruvate. The pyruvate can be used for gluconeogenesis.

    Ammonia Toxicity

    • Ammonia toxicity can result from a shift in the equilibrium of the glutamate dehydrogenase reaction, depleting α-ketoglutarate, an essential intermediate in the citric acid cycle. This leads to a decrease in ATP production.
    • The brain is particularly sensitive to hyperammonemia, as it relies on the citric acid cycle for energy production.

    Urea Cycle

    • The urea cycle is the principal pathway for ammonia disposal.
    • The cycle occurs primarily in the liver, with the first two reactions taking place in the mitochondria and the remaining three reactions occurring in the cytosol.
    • Urea, the end product of the urea cycle, is excreted by the kidneys.

    Hyperammonemia

    • Hyperammonemia is a medical emergency due to the neurotoxic effects of ammonia.
    • Causes of hyperammonemia include genetic defects in the urea cycle and liver disease.

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    Biochemistry of Proteins PDF

    Description

    Test your knowledge on overall protein metabolism, including the breakdown of proteins into amino acids, dietary protein digestion, and the roles of glucogenic and ketogenic amino acids. Explore concepts such as nitrogen balance and its significance in different physiological states. Perfect for students looking to deepen their understanding of biochemistry!

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