Mode of Action of Enzymes (Cambridge (CIE) AS Biology): Flashcards

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  • Define enzyme.

Cards in this collection (32)

  • Define enzyme.

    An enzyme is a biological catalyst that increases the rate of a reaction and remains unchanged at the end of the reaction.

  • What type of protein are all enzymes?

    All enzymes are globular proteins.

  • Define intracellular enzyme.

    An enzyme that catalyses reactions inside the cell in which it is made.

  • Define extracellular enzyme.

    An enzyme that is secreted from the cell to catalyse reactions outside the cell.

  • Give one example of an extracellular enzyme and where it acts.

    Amylase — secreted into the gut, where it digests starch outside cells.

  • Enzymes are globular proteins that act as biological .

    Enzymes are globular proteins that act as biological catalysts.

  • True or False?

    Enzymes are used up during the reactions they catalyse.

    False.

    Enzymes remain unchanged at the end of a reaction and can be reused.

  • Define active site.

    A region on an enzyme with a specific shape to which the substrate binds.

  • Define enzyme-substrate complex.

    The structure formed when a substrate binds to the active site of an enzyme.

  • Define activation energy.

    The minimum energy needed for a reaction to take place.

  • How do enzymes speed up reactions?

    They lower the activation energy of the reaction.

  • What is meant by enzyme specificity?

    Each enzyme catalyses only one type of reaction, because its active site is complementary to only one substrate.

  • Enzymes speed up reactions by lowering the energy.

    Enzymes speed up reactions by lowering the activation energy.

  • Why is an enzyme specific to only one substrate?

    The shape of its active site is complementary to only that substrate's shape.

  • Define the lock-and-key hypothesis.

    A model in which the substrate is complementary in shape to the active site and fits into it like a key into a lock.

  • Define the induced-fit hypothesis.

    A model in which the active site is not exactly complementary at first, but changes shape slightly to fit closely around the substrate.

  • How does the induced-fit hypothesis differ from the lock-and-key hypothesis?

    In lock-and-key, the active site is already complementary to the substrate.

    In induced-fit, the active site moulds/changes shape around the substrate as it binds.

  • In the induced-fit model, what happens to the active site when the substrate binds?

    It changes shape to fit more closely around the substrate, forming an enzyme-substrate complex.

  • In the hypothesis, the active site changes shape to fit the substrate.

    In the induced-fit hypothesis, the active site changes shape to fit the substrate.

  • True or False?

    In the lock-and-key hypothesis, the active site changes shape when the substrate binds.

    False.

    That describes the induced-fit hypothesis. In lock-and-key, the active site is already complementary to the substrate.

  • What are the two general ways to measure the progress of an enzyme-catalysed reaction?

    Measure the rate of formation of product, or the rate of disappearance of substrate.

  • How can the activity of catalase be measured?

    By measuring the rate of formation of product — the volume of oxygen produced from the breakdown of hydrogen peroxide.

  • How can the activity of amylase be measured?

    By measuring the rate of disappearance of substrate — how quickly starch is broken down.

  • Define enzyme activity.

    The rate at which an enzyme converts substrate into product.

  • Catalase activity can be measured by collecting the gas produced.

    Catalase activity can be measured by collecting the oxygen gas produced.

  • When using amylase and starch, how can the end of the reaction be detected?

    When iodine solution no longer turns blue-black, showing that all the starch has been digested.

  • Define colorimeter.

    A device that measures the absorbance (or transmission) of light passing through a coloured solution.

  • When is a colorimeter useful for measuring the progress of an enzyme-catalysed reaction?

    When the reaction involves a colour change.

  • How does a colorimeter measure the progress of such a reaction?

    It measures the change in absorbance of light as the colour of the solution changes over time.

  • Why is a calibration curve produced before using a colorimeter?

    To convert absorbance readings into a concentration of product or substrate.

  • A colorimeter measures the of light passing through a coloured solution.

    A colorimeter measures the absorbance of light passing through a coloured solution.

  • True or False?

    A colorimeter can be used to follow any enzyme-catalysed reaction.

    False.

    A colorimeter can only follow reactions that involve a colour change.

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