Enzyme Regulation Overview
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Questions and Answers

What is the function of regulatory enzymes in a metabolic pathway?

  • To catalyze reactions faster than normal enzymes
  • To adjust the overall rate of the pathway (correct)
  • To serve as substrates for other enzymes
  • To perform irreversible reactions
  • Which enzymes are often referred to as key enzymes in metabolic pathways?

  • Enzymes that are involved in reversible reactions
  • Enzymes that are produced in large quantities
  • Enzymes that catalyze all reactions
  • Rate limiting enzymes (correct)
  • How does long-term regulation of enzymes occur?

  • By altering the enzyme's catalytic activity
  • By controlling the number or concentration of enzyme molecules (correct)
  • By activating all enzymes at once
  • By changing the temperature of the environment
  • What distinguishes short-term regulation of enzymes from long-term regulation?

    <p>It occurs over seconds to minutes (A)</p> Signup and view all the answers

    Which statement about the reactions catalyzed by regulatory enzymes is correct?

    <p>They are usually irreversible and key to metabolic control. (C)</p> Signup and view all the answers

    What process increases the rate of transcription of an enzyme's gene?

    <p>Induction (B)</p> Signup and view all the answers

    Which factor can act as a repressor in enzyme synthesis?

    <p>Product (D)</p> Signup and view all the answers

    What is the definition of enzyme turnover?

    <p>The balance between enzyme synthesis and degradation (C)</p> Signup and view all the answers

    What type of regulation involves a non-covalent bond at an allosteric site?

    <p>Allosteric regulation (D)</p> Signup and view all the answers

    Which of the following statements is true about allosteric enzymes?

    <p>They exhibit cooperativity with their substrates. (A)</p> Signup and view all the answers

    What role does a lack of substrate play in enzyme degradation?

    <p>It makes the enzyme more susceptible to proteolysis. (A)</p> Signup and view all the answers

    What best defines the process of repression in enzyme regulation?

    <p>Decreasing enzyme synthesis in response to certain products. (C)</p> Signup and view all the answers

    Which of the following is NOT a mechanism of catalytic regulation?

    <p>Transcriptional activation (D)</p> Signup and view all the answers

    What is the main effect of an allosteric inhibitor on an enzyme?

    <p>It changes the shape of the enzyme to prevent substrate binding. (B)</p> Signup and view all the answers

    Which modification is most commonly used in reversible covalent modification of enzymes?

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

    Why are zymogens released from the pancreas as inactive forms?

    <p>To prevent premature activation and cell damage. (B)</p> Signup and view all the answers

    What does the term 'irreversible covalent modification' refer to in enzyme regulation?

    <p>Permanent alterations that prevent the enzyme from functioning. (A)</p> Signup and view all the answers

    Which amino acids are commonly involved in phosphorylation processes?

    <p>Serine, Threonine, and Tyrosine (C)</p> Signup and view all the answers

    How does allosteric modification primarily affect enzyme activity?

    <p>It induces structural changes that affect substrate binding. (B)</p> Signup and view all the answers

    What is one consequence of allosteric activation of an enzyme?

    <p>It can increase the enzyme's catalytic activity. (A)</p> Signup and view all the answers

    What is an allosteric molecule's key characteristic?

    <p>It interacts with the enzyme non-covalently. (A)</p> Signup and view all the answers

    Flashcards

    Regulatory enzyme

    An enzyme that controls the rate of a metabolic pathway.

    Metabolic pathway

    A sequence of enzyme-catalyzed reactions.

    Enzyme regulation

    Controlling the activity of enzymes in a metabolic pathway.

    Long-term regulation

    Controlling enzyme concentration by changing the rate of enzyme synthesis/degradation.

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    Short-term regulation

    Controlling enzyme activity and not affecting the concentration or amount.

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    Enzyme Induction

    Increased enzyme synthesis, stimulated by an inducer (often the substrate or hormone).

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    Enzyme Repression

    Decreased enzyme synthesis, in response to a repressor (often the product or hormone).

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    Enzyme Degradation

    Breakdown of enzyme protein, altering enzyme availability.

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    Allosteric Regulation

    Enzyme activity changes due to binding of a molecule (effector or modifier) at a site other than the active site.

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    Allosteric Enzyme

    Enzyme with multiple binding sites, including an active site and an allosteric site, which affects enzyme activity.

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    Enzyme Turnover

    The rate of synthesis and degradation of an enzyme, which may control the number of enzyme molecules.

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    Inducer

    A molecule that stimulates enzyme synthesis.

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    Repressor

    A molecule that inhibits enzyme synthesis.

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    Allosteric Inhibition

    End product binding to an enzyme, causing a conformational change and inhibiting its activity.

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    Allosteric Modifier

    Molecule that binds to an enzyme away from the active site, affecting its activity.

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    Reversible Covalent Modification

    Enzyme activity changes due to addition or removal of a chemical group (like phosphate), often used to regulate activity.

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    Phosphorylation

    Adding a phosphate group to a protein, typically altering its enzymatic activity.

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    Irreversible Covalent Modification

    Enzyme activity change through irreversible chemical bonding (e.g., cleavage of a peptide).

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    Zymogen

    Inactive precursor of an enzyme, activated by proteolytic cleavage (breaking a protein).

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    Pancreatic Enzymes

    Digestive enzymes produced by the pancreas, released in inactive form (zymogens).

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    Proteolytic Cleavage

    The process of breaking a protein into smaller pieces by enzymatic means.

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    Study Notes

    Enzyme Regulation

    • Enzymes are crucial in cellular metabolism, working together in sequential pathways
    • The product of one enzyme serves as the substrate for the next in the pathway
    • Regulatory enzymes control the overall rate of these metabolic pathways to meet the cell's demands
    • The rate-limiting enzyme determines the speed of the overall pathway

    Types of Enzyme Control

    • Control of enzyme quantity: This long-term regulation (hours to days) involves controlling how many enzyme molecules are present
      • Enzyme synthesis at the gene level: Induction (increasing enzyme production in response to a substrate or hormone) and repression (decreasing enzyme production in response to a repressor or product) are crucial mechanisms
      • Enzyme degradation: Loss of enzyme by proteolysis occurs when the enzyme is no longer needed
    • Control of enzyme activity (short-term): Quick changes (seconds to minutes) to the activity of enzymes are essential
      • Allosteric regulation: A molecule binds to a specific site on the enzyme, causing a shape change, altering activity
        • Feed-back inhibition: The final product of a pathway inhibits an earlier enzyme in the pathway, regulating its rate
        • Activator molecules can enhance enzyme activity.
      • Reversible covalent modification: Chemical adjustments like phosphorylation (adding a phosphate group) or dephosphorylation (removing a phosphate group) that rapidly shift enzyme activity
      • Irreversible covalent modification (proteolytic cleavage): This results in an inactive zymogen being cleaved to form an active enzyme; often involved in digestive enzymes to prevent damage to the producing cells.

    Allosteric Regulation

    • Allosteric enzymes have two binding sites:
      • An active site where the substrate binds
      • An allosteric site where a regulator (effector or modifier) binds. This binding by the effector (positive or negative) alters the active site's shape, enhancing or inhibiting its catalytic activity
    • This process is often non-covalent but rapidly reversible

    Feed-back Inhibition

    • End products accumulate, they bind to allosteric sites on regulatory enzymes, thereby inhibiting the enzymes and halting further synthesis in the metabolic pathway
    • This helps in regulating metabolic processes and preventing unnecessary build-up of molecules

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