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GOB Chemistry: Enzyme Regulation, Vitamins, and Serological Testing

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Terms in this set (22)

  • 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 are the main types of enzyme regulation in metabolic pathways?

    Enzyme regulation includes feedback control, allosteric control, genetic control, covalent modification, and zymogen activation.

  • What is allosteric regulation?

    Binding of a molecule at a site other than the active site that changes enzyme activity; can be positive (activator) or negative (inhibitor).

  • What is feedback control in enzyme regulation?

    A product of a metabolic pathway acts as an allosteric regulator of an enzyme earlier in the pathway, either inhibiting (negative) or enhancing (positive) its activity.

  • What is covalent modification in enzyme regulation?

    Addition or removal of chemical groups (e.g., phosphate) on amino acid residues that activate or deactivate enzymes.

  • What are zymogens?

    Inactive enzyme precursors that require cleavage of a protein segment to become active enzymes.

  • What is genetic control of enzyme activity?

    Regulation of enzyme levels by turning genes on or off, affecting enzyme synthesis and degradation.

  • Which vitamins are fat-soluble and which are water-soluble?

    Fat-soluble vitamins: A, D, E, K; Water-soluble vitamins: B-complex and C.

  • Why are vitamins classified as fat-soluble or water-soluble?

    Fat-soluble vitamins are hydrophobic and stored in the liver; water-soluble vitamins are hydrophilic, not stored, and often form coenzymes.

  • What is a coenzyme?

    An organic molecule derived from vitamins that binds to enzymes and is required for catalytic activity.

  • Which vitamins become coenzymes?

    Most water-soluble vitamins (B-complex and C) become coenzymes, e.g., B1 (TPP), B2 (FAD, FMN), B3 (NAD+), B5 (CoA), B6 (PLP), B7 (Biotin), B9 (THF), B12 (Methylcobalamin).

  • What is the biological function of Vitamin A?

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

  • What is the function of Vitamin D?

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

  • What is the role of Vitamin K?

    Vitamin K is essential for prothrombin formation, which is vital for blood clotting and bone metabolism.

  • How can enzyme tests in blood diagnose organ damage?

    Elevated levels of specific enzymes (e.g., AST, ALT, LDH, CK) in blood indicate damage to organs like liver, heart, or pancreas.

  • What protein class is used in lateral flow assays for COVID-19 detection?

    Antibodies are used on the test strip to bind specifically to the SARS-CoV-2 spike protein antigen.