Transamination Overview and Mechanism
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Questions and Answers

What is the primary function of transamination?

  • To produce ATP
  • To synthesize fatty acids
  • To break down glucose
  • To transfer an amino group from an amino acid to an α-keto acid (correct)
  • Transamination is an irreversible reaction.

    False

    What is the name of the enzyme that catalyzes transamination reactions?

    aminotransferase

    The cofactor required for transamination is ______, which is derived from vitamin B6.

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

    Match the following enzyme with their specific actions in transamination.

    <p>ALT = Catalyzes the reaction of alanine to pyruvate AST = Catalyzes the reaction of aspartate to oxaloacetate</p> Signup and view all the answers

    What is the role of glutamate in transamination?

    <p>It serves as a temporary reservoir for amino groups</p> Signup and view all the answers

    Keto acids produced in transamination can only be used for energy production.

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

    What type of molecule is transferred during transamination?

    <p>An amino group (-NH₂)</p> Signup and view all the answers

    Transamination is a process that only occurs during amino acid synthesis.

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

    Besides converting them to other compounds, what is one fate of the keto acids produced by transamination?

    <p>energy production</p> Signup and view all the answers

    The enzyme ALT catalyzes the reaction of alanine to ______.

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

    Match the enzyme with the reaction each catalyzes:

    <p>ALT = Alanine → Pyruvate AST = Aspartate → Oxaloacetate</p> Signup and view all the answers

    What is the primary role of pyridoxal phosphate (PLP) in transamination reactions?

    <p>It serves as a cofactor required for the enzyme’s activity.</p> Signup and view all the answers

    Glutamate donates its amino group directly to the urea cycle for excretion.

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

    What is the main outcome of transamination?

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

    Transamination plays a critical role in generating non-essential amino acids.

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

    What reaction occurs when alanine and α-ketoglutarate undergo transamination?

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

    The cofactor required for transamination is ______.

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

    Match the following enzymes with the reactions they catalyze:

    <p>ALT = Alanine → Pyruvate AST = Aspartate → Oxaloacetate ALDH = Glutamate → α-Ketoglutarate LDH = Pyruvate → Lactate</p> Signup and view all the answers

    What role does glutamate play in the urea cycle?

    <p>It serves as a temporary reservoir for amino groups</p> Signup and view all the answers

    Which of the following statements about transamination is true?

    <p>It involves the transfer of an amino group from an amino acid to an α-keto acid.</p> Signup and view all the answers

    Name the enzyme responsible for catalyzing the reaction of aspartate to oxaloacetate.

    <p>AST (Aspartate Aminotransferase)</p> Signup and view all the answers

    Match the following keto acids with their potential fates:

    <p>Pyruvate = Used in gluconeogenesis or energy production Oxaloacetate = Precursor for glucose or entry into Krebs Cycle Acetyl-CoA = Used in fatty acid synthesis α-ketoglutarate = Participates in the Krebs cycle</p> Signup and view all the answers

    Which process does glutamate undergo to donate the amino group for urea cycle excretion?

    <p>Oxidative deamination</p> Signup and view all the answers

    What is formed when alanine undergoes transamination with α-ketoglutarate?

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

    Study Notes

    Transamination Overview

    • Transamination is the transfer of an amino group (-NH₂) from an amino acid to an α-keto acid.
    • This process allows the body to interconvert amino acids and keto acids.
    • The reaction is catalyzed by enzymes called aminotransferases (or transaminases).
    • A cofactor, pyridoxal phosphate (PLP), derived from vitamin B6, is essential for the reaction.

    Purpose of Transamination

    • Transamination is a reversible process, used in both the synthesis and degradation of amino acids.
    • It's critical for generating non-essential amino acids.
    • It prepares amino groups for excretion via the urea cycle by transferring them to glutamate.
    • Crucially, this process is used in the synthesis and degradation of amino acids.

    Transamination Reaction Mechanism

    • An amino acid reacts with α-ketoglutarate, forming a keto acid and glutamate.
    • Example: Alanine + α-ketoglutarate ↔ Pyruvate + Glutamate

    Key Enzymes in Transamination

    • Alanine aminotransferase (ALT) catalyzes the conversion of alanine to pyruvate.
    • Aspartate aminotransferase (AST) catalyzes the conversion of aspartate to oxaloacetate.

    Glutamate's Role

    • Glutamate acts as a temporary store for amino groups.
    • It delivers these amino groups to the urea cycle through oxidative deamination.
    • Glutamate serves as a temporary reservoir for amino groups, donating them to the urea cycle.

    Fate of Keto Acids

    • Keto acids can be used for energy production in the Krebs cycle.
    • They can also be converted into glucose or lipids.

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    Description

    This quiz covers the fundamental aspects of transamination, including its purpose, mechanisms, and key enzymes involved in the process. Understand how amino groups are transferred and the significance of this biochemical reaction in the synthesis of non-essential amino acids. Test your knowledge on the role of pyridoxal phosphate and notable enzymes like alanine aminotransferase.

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