Enzyme Inhibition Overview
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Questions and Answers

Which of the following is NOT a characteristic that differentiates isoenzymes?

  • Structure
  • Affinity to substrate
  • Mobility in electric fields
  • Temperature stability (correct)
  • How many isoenzymes are present in lactate dehydrogenase?

  • Four
  • Six
  • Five (correct)
  • Three
  • Which type of regulation involves feedback methods?

  • Substrate level regulation
  • Enzyme inhibition
  • Allosteric regulation (correct)
  • Covalent modification
  • What can an elevation of plasma enzyme activity indicate?

    <p>Presence of a disease or tissue damage</p> Signup and view all the answers

    What is the purpose of measuring alanine aminotransferase (ALT) levels?

    <p>To indicate liver damage</p> Signup and view all the answers

    What is the primary effect of competitive inhibitors on enzyme kinetics?

    <p>They increase the Km value.</p> Signup and view all the answers

    Which type of inhibitor binds covalently or very tightly to the enzyme, leading to irreversible inactivation?

    <p>Irreversible inhibitors</p> Signup and view all the answers

    What is the typical characteristic of noncompetitive inhibitors regarding Km and Vmax?

    <p>They decrease Vmax and have no effect on Km.</p> Signup and view all the answers

    What is the role of allosteric sites in allosteric enzymes?

    <p>They bind activators or inhibitors, regulating enzyme activity.</p> Signup and view all the answers

    Which of the following is an example of a competitive inhibitor?

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

    What kind of inhibitors do not resemble the substrate and bind at a different site?

    <p>Noncompetitive inhibitors</p> Signup and view all the answers

    What effect do competitive inhibitors have on substrate concentration in overcoming inhibition?

    <p>They require higher substrate concentration to overcome inhibition.</p> Signup and view all the answers

    Which enzyme is inhibited by cyanide?

    <p>Cytochrome oxidase</p> Signup and view all the answers

    Study Notes

    Enzyme Inhibition

    • Enzyme inhibitors are compounds that reduce the speed of an enzyme-catalyzed reaction by binding to the enzyme.
    • Two main types of enzyme inhibitors exist: reversible and irreversible inhibitors.

    Reversible Inhibitors

    • These inhibitors bind non-covalently to the enzyme, allowing for dissociation.
    • Subcategories of reversible inhibitors include competitive inhibitors.

    Competitive Inhibitors

    • Competitive inhibitors compete with the substrate for binding to the enzyme's active site.
    • These inhibitors generally resemble the substrate in structure.
    • Increasing substrate concentration can overcome competitive inhibition.
    • Competitive inhibition increases the KM value, but does not alter Vmax.
    • Methotrexate is an example of a competitive inhibitor, which is an anticancer drug that inhibits the enzyme dihydrofolate reductase.

    Non-competitive Inhibitors

    • Non-competitive inhibitors bind to a site on the enzyme other than the active site, affecting the enzyme's ability to function.
    • Non-competitive inhibitors do not resemble the substrate.
    • Non-competitive binding reduces Vmax, but does not affect KM.
    • Cyanide is an example of a non-competitive inhibitor, which inhibits the enzyme cytochrome oxidase.

    Irreversible Inhibitors

    • Irreversible inhibitors bind covalently or very tightly to the enzyme's active site, permanently inactivating it.

    Allosteric Enzymes

    • Allosteric enzymes have multiple binding sites, including regulatory sites.
    • These sites can bind activators or inhibitors, affecting enzyme activity.
    • Allosteric enzymes are often involved in the initial steps of metabolic pathways and frequently catalyze irreversible reactions.

    Isoenzymes

    • Isoenzymes are enzymes that catalyze the same reaction but have different structures.
    • Isoenzymes vary in their structure and their affinity for the substrate.
    • Isoenzymes exhibit variations in their resistance to inhibitors and mobility in electrical fields (electrophoresis).
    • Lactate dehydrogenase (LDH) is an example, with five distinct isoenzymes having different subunit compositions.

    Regulation of Enzyme Activity

    • Allosteric regulation involves feedback and feed-forward mechanisms.
    • Covalent modification, including phosphorylation and dephosphorylation, also regulates enzyme activity.

    Enzymes in Clinical Diagnosis

    • Elevated enzyme activity in the blood may indicate tissue damage, which is frequently useful in diagnosis and prognosis.
    • Plasma enzymes are sensitive indicators of tissue damage or disease.
    • Alanine aminotransferase (ALT) levels can indicate liver damage when elevated.

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    Related Documents

    Enzymes 3 Lecture Notes PDF

    Description

    Explore the fascinating world of enzyme inhibition, focusing on both reversible and irreversible inhibitors. Learn about competitive and non-competitive inhibitors, their mechanisms, and examples of their applications in medicine. Understand how these inhibitors affect enzyme activity and the implications for various biological processes.

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