Dr. Nagla El-Melegy: Protein Metabolism

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Questions and Answers

Where does oxidative deamination primarily take place?

  • Liver and kidney (correct)
  • Muscles and pancreas
  • Lungs and stomach
  • Brain and heart

What is the main reason for oxidative deamination?

  • To synthesize glucose
  • To provide NH3 for urea synthesis (correct)
  • To produce amino acids
  • To generate energy for the body

What is another outcome of oxidative deamination?

  • Production of fatty acids
  • Synthesis of cholesterol
  • Generation of ATP
  • Formation of α-keto acids (correct)

What is the role of α-keto acids in the body?

<p>Participating in a variety of reactions (A)</p> Signup and view all the answers

What is the byproduct of oxidative deamination that is used for energy generation?

<p>α-keto acids (A)</p> Signup and view all the answers

What is the significance of urea synthesis in the context of oxidative deamination?

<p>It detoxifies the body by removing NH3 (A)</p> Signup and view all the answers

What is the purpose of transamination in the context of amino acid metabolism?

<p>To convert excess amino acids into energy (A)</p> Signup and view all the answers

What is the result of transamination in terms of nitrogen concentration?

<p>Nitrogen is concentrated in glutamate (C)</p> Signup and view all the answers

What are the two types of processes involved in amino acid metabolism?

<p>Catabolism and anabolism (A)</p> Signup and view all the answers

What is the role of transamination in managing excess amino acids?

<p>It breaks down excess amino acids into energy (B)</p> Signup and view all the answers

What is the overall goal of amino acid metabolism?

<p>To generate energy from amino acids (B)</p> Signup and view all the answers

What is the typical range of amino acids found in proteins?

<p>50 to 10,000 (D)</p> Signup and view all the answers

What is a characteristic feature of amino acids?

<p>Presence of NH2 group (D)</p> Signup and view all the answers

What is the role of a-ketoglutarate in transamination reactions?

<p>Amino group acceptor (B)</p> Signup and view all the answers

What determines the sequence of amino acids in a protein?

<p>Specific bodily DNA (C)</p> Signup and view all the answers

What is the product of the transamination reaction catalyzed by aminotransferases?

<p>New keto acid and new amino acid (B)</p> Signup and view all the answers

Where are aminotransferases active?

<p>Both in cytoplasm and mitochondria (B)</p> Signup and view all the answers

What is the classification of a chain of 3 amino acids?

<p>Tripeptide (A)</p> Signup and view all the answers

What elements make up an amino acid?

<p>Carbon, hydrogen, oxygen, nitrogen (B)</p> Signup and view all the answers

What is the function of the PLP cofactor in transamination reactions?

<p>Catalyzing the reaction (C)</p> Signup and view all the answers

What is the general structure of an amino acid, as shown in the diagram?

<p>NH2 - C - COOH (D)</p> Signup and view all the answers

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Study Notes

Amino Acids

  • Amino acids are organic acids that contain an NH2 group.
  • They are composed of carbon, hydrogen, oxygen, and nitrogen.
  • Chains of amino acids are classified as:
    • Peptides: fewer than 50 amino acids
    • Dipeptides: 2 amino acids
    • Tripeptides: 3 amino acids
    • Polypeptides: more than 10 amino acids
    • Proteins: more than 50 amino acids (typically 100 to 10,000 amino acids linked together)

Transamination

  • Transamination is the reversible transfer of an amino group (in the form of ammonia) from an α-amino acid to an α-keto acid.
  • It forms a new amino acid and a new α-keto acid.
  • This process occurs mostly in the liver and kidney.
  • Transamination involves both catabolism (degradation) and anabolism (synthesis) of amino acids.
  • It diverts excess amino acids towards energy generation.
  • The amino acids undergo transamination to finally concentrate nitrogen in glutamate.

Metabolism of Amino Acids

  • Amino acids undergo certain common reactions, including transamination followed by deamination for the liberation of ammonia.
  • This process is involved in the production of non-essential amino acids.
  • The purpose of oxidative deamination is to provide NH3 for urea synthesis and α-keto acids for a variety of reactions, including energy generation.

Aminotransferases

  • Aminotransferases are active both in the cytoplasm and mitochondria.
  • They catalyze transamination reactions, where α-ketoglutarate acts as an amino group acceptor.
  • The reaction involves the transfer of an amino group from an amino acid to an α-keto acid, resulting in a new amino acid and a new keto acid.

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