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lecture 11

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1/23
  • What is competitive enzyme inhibition?

    Competitive inhibition occurs when an inhibitor resembles the substrate and competes for the same active site on the enzyme.

  • How does noncompetitive inhibition affect enzyme activity?

    Noncompetitive inhibition involves an inhibitor binding to a separate site on the enzyme, changing the active site shape and preventing substrate binding.

  • What characterizes uncompetitive inhibition?

    Uncompetitive inhibition occurs when the inhibitor binds only to the enzyme-substrate complex, not to the free enzyme.

  • What is irreversible enzyme inhibition?

    Irreversible inhibition involves covalent modification of the enzyme, permanently inactivating it.

  • How does competitive inhibition affect Km and Vmax?

    Competitive inhibition increases Km (decreases affinity) but does not change Vmax.

  • How does noncompetitive inhibition affect Km and Vmax?

    Noncompetitive inhibition lowers Vmax but does not change Km.

  • How does uncompetitive inhibition affect Km and Vmax?

    Uncompetitive inhibition lowers both Km and Vmax by the same ratio.

  • What is allosteric regulation of enzymes?

    Allosteric regulation involves binding of molecules at sites other than the active site, which can either activate (positive) or inhibit (negative) enzyme activity.

  • What is feedback control in enzyme regulation?

    Feedback control uses a product of a metabolic pathway as an allosteric regulator to modulate the activity of an enzyme earlier in the pathway.

  • What is covalent modification in enzyme regulation?

    Covalent modification involves adding or removing chemical groups (e.g., phosphate) to amino acid residues, altering enzyme activity.

  • What are zymogens?

    Zymogens are inactive enzyme precursors that require cleavage of a protein segment to become active enzymes.

  • What is genetic control of enzyme regulation?

    Genetic control regulates enzyme levels by turning genes on or off, affecting enzyme synthesis.

  • What distinguishes fat-soluble from water-soluble vitamins?

    Fat-soluble vitamins are hydrophobic, stored in the liver, and mainly composed of carbon and hydrogen. Water-soluble vitamins are hydrophilic, contain OH and COOH groups, and are not stored in the body.

  • Name the fat-soluble vitamins.

    Fat-soluble vitamins include A (retinol), D (calciferol), E (α-tocopherol), and K (phylloquinone).

  • Name the water-soluble vitamins.

    Water-soluble vitamins include C (ascorbic acid) and the B-complex vitamins (B1, B2, B3, B5, B6, B7, B9, B12).

  • What is a coenzyme?

    A coenzyme is an organic molecule derived from vitamins that assists enzymes in catalysis by binding to the active site.

  • Which vitamins become coenzymes?

    Most water-soluble vitamins, especially B-complex vitamins and vitamin C, become coenzymes.

  • What is the biological function of Vitamin A?

    Vitamin A (retinol) supports vision, cell growth, differentiation, and acts as an antioxidant for lipids.

  • What is the function of Vitamin D?

    Vitamin D (calciferol) is essential for bone growth by increasing calcium and phosphate absorption and retention.

  • What is the role of Vitamin E?

    Vitamin E (α-tocopherol) is a strong antioxidant that prevents oxidative damage to lipids and cell membranes.

  • What is the function of Vitamin K?

    Vitamin K (phylloquinone) is required for prothrombin formation, essential in blood clotting and bone metabolism.

  • How can enzyme tests in blood indicate organ damage?

    Elevated levels of specific enzymes like AST, ALT, LDH, and CK in blood can indicate damage to liver, heart, or other organs.

  • What proteins are used in lateral flow assays for COVID-19 detection?

    Lateral flow assays use antibodies conjugated to tags to bind specifically to SARS-CoV-2 spike proteins for antigen detection.