Biochemistry: Enzymes and Metabolic Reactions
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Questions and Answers

What is the term for the protein component of an enzyme that requires a cofactor to be active?

  • Substrate
  • Apoenzyme (correct)
  • Active site
  • Holoenzyme
  • Which term describes a substance that reduces the rate of an enzyme-catalyzed reaction?

  • Inhibitor (correct)
  • Cofactor
  • Activator
  • Substrate
  • What units are used to measure enzyme activity?

  • Micromoles per minute (correct)
  • Molar per second
  • Milliliters per hour
  • Grams per liter
  • What does 'Km' represent in enzyme kinetics?

    <p>The affinity of the enzyme for the substrate (D)</p> Signup and view all the answers

    What term describes the temperature at which an enzyme shows maximum activity?

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

    Which of the following is NOT a factor affecting enzyme activity?

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

    A thermophilic bacterial enzyme would likely have its optimum temperature closest to which temperature?

    <p>70°C (C)</p> Signup and view all the answers

    What does a low Km indicate about an enzyme?

    <p>High substrate affinity (B)</p> Signup and view all the answers

    What is the primary function of a catalyst in a chemical reaction?

    <p>To decrease the activation energy of the reaction. (D)</p> Signup and view all the answers

    Which of the following best describes the relationship between enzymes and the equilibrium of a chemical reaction?

    <p>Enzymes do not change the reaction's equilibrium. (D)</p> Signup and view all the answers

    What is the primary difference between an enzyme and a ribozyme?

    <p>Enzymes are primarily made of protein, while ribozymes are made of RNA. (C)</p> Signup and view all the answers

    Which statement correctly explains the concept of enzyme 'specificity'?

    <p>An enzyme will typically catalyze a single type of reaction using a specific molecule or chemically related molecules. (B)</p> Signup and view all the answers

    According to the enzyme classification system, what type of enzyme is 'hydrolase'?

    <p>An enzyme that catalyzes hydrolysis reactions. (A)</p> Signup and view all the answers

    What is the purpose of the serial number in the EC number system for enzymes?

    <p>To indicate the specific reaction catalyzed by the enzyme within its subclass. (A)</p> Signup and view all the answers

    If an enzyme-catalyzed reaction is said to be '10^6 times faster than uncatalyzed reactions', which enzyme is most likely being described?

    <p>Carbonic anhydrase. (C)</p> Signup and view all the answers

    An enzyme is found to be using chemically related molecules as its substrates. Which aspect of enzyme properties is described here?

    <p>Substrate specificity. (A)</p> Signup and view all the answers

    Flashcards

    Apoenzyme

    The protein component of an enzyme.

    Cofactor

    The non-protein component of an enzyme, often a metal ion or organic molecule.

    Holoenzyme

    The active form of an enzyme, containing both the protein (apoenzyme) and non-protein (cofactor) components.

    Active Site

    The site on an enzyme where the substrate binds and the chemical reaction takes place.

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    Enzyme Activity

    The speed at which an enzyme converts a substrate to a product.

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    Optimum Temperature

    The temperature at which an enzyme exhibits maximum activity.

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    Optimum pH

    The pH at which an enzyme exhibits maximum activity.

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    Inhibitor

    Any substance that slows down or inhibits the rate of an enzyme-catalyzed reaction.

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    Enzymes

    Biological catalysts that speed up chemical reactions in living organisms.

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    What are enzymes made of?

    Enzymes are primarily proteins, but some are made of RNA, called ribozymes.

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    Do enzymes change the outcome of a reaction?

    While enzymes make reactions happen faster, they don't change the final outcome of the reaction.

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    What is enzyme specificity?

    Each enzyme typically works with only one or a few specific molecules called substrates. This means they have high specificity.

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    How are enzymes classified?

    Enzymes can be categorized into six main classes based on the type of reaction they catalyze, each with an assigned EC number.

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    How efficient are enzymes?

    Enzymes are incredibly efficient, accelerating reactions by factors of 10^3 to 10^8 times faster than without the enzyme.

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    What is Activation Energy?

    The activation energy is the minimum amount of energy needed to start a chemical reaction.

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    What are catalysts?

    Catalysts, like enzymes, are substances that speed up reactions by lowering the activation energy needed to start the reaction. They are not used up in the process.

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    Study Notes

    Enzymes

    • Enzymes are biocatalysts that speed up biochemical reactions
    • They are not consumed in the reaction
    • Enzymes lower the activation energy needed for a chemical reaction to occur
    • Enzymes are specific to the reaction and the substrate

    Learning Objectives

    • Describe enzymes and their common properties
    • List enzyme classifications in the correct order
    • Describe factors that change enzyme activity
    • Explain the relationship between Km and activity
    • Explain enzyme inhibition and inhibition types

    Metabolic Reactions

    • Enzymes facilitate both anabolic and catabolic reactions
    • Enzymes facilitate metabolic reactions by decreasing activation energy and increasing reaction rate
    • Enzymes can modify molecules
    • Enzymes can transport molecules

    Glycolysis

    • Glycolysis is a metabolic pathway involving reactions on molecules, catalyzed by enzymes such as Hexokinase (HK) and Phosphofructokinase (PFK), to break down glucose
    • Illustrated in detail on slide 4

    Enzyme Nomenclature: Classification

    • Enzymes are classified based on their catalytic function (EC numbers)
    • Includes classes like Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, Ligases, and Translocases
    • The classification system is standardized by the International Union of Biochemistry and Molecular Biology (IUBMB)

    Properties of Enzymes

    • Most enzymes are proteins (with exceptions like ribozymes)
    • Enzymes are highly specific for the substrates they act on and the reaction they catalyze
    • They increase reaction rates without altering the reaction equilibrium
    • The illustration on slide 9 displays substrate to reaction specificity

    Efficiency

    • Enzyme-catalyzed reactions are highly efficient, proceeding 103 to 108 times faster than uncatalyzed reactions
    • Enzymes like carbonic anhydrase are among the fastest known enzymes hydrating 106 molecules of CO2 per second

    Specificity

    • Reaction Specificity: A given enzyme catalyzes a specific type of reaction
    • Substrate Specificity: A given enzyme uses specific molecules or chemically related ones

    Enzyme Activity

    • Activity is measured as the speed (V)
    • It's the number of substrate molecules that become products in given time
    • The unit is the amount of substrate conversions in a minute, under optimal conditions

    Factors Affecting Enzyme Activity

    • Enzyme concentration: More enzyme, faster reaction
    • Substrate concentration: Up to a point, more substrate, faster reaction
    • Temperature: Optimal temperature for maximum activity
      • Humans (35-40°C); Thermophilic bacteria (70°C).
    • pH: Optimal pH for maximum enzyme activity
    • Inhibitors: Reduce enzyme activity

    Enzyme Concentration

    • Increase in enzyme concentration increases product concentration and reaction speed

    Substrate Concentration

    • Increase in substrate concentration increases reaction speed until saturation point is reached
    • Km (Michaelis-Menten constant): Substrate concentration at which reaction velocity is half of Vmax (maximum reaction rate)
    • Higher Km means lower affinity of enzyme for the substrate

    Temperature

    • Temperature affects enzyme activity, with an optimal temperature for each enzyme
    • Excessive heat can denature enzymes, reducing their ability to function

    pH

    • pH affects enzyme activity, with an optimal pH for each enzyme
    • Significant deviations from optimal pH can denature enzymes

    Inhibitors

    • Inhibitors decrease enzyme activity
    • Two main types: reversible and irreversible
    • Competitive inhibitors block the active site
    • Non-competitive inhibitors change the enzyme shape, making the active site unavailable

    Enzyme Kinetics and Km

    • Km represents the enzyme's affinity for its substrate
    • Low Km indicates high affinity

    Km, A Clinical Example

    • Enzyme Km values are clinically relevant; for example, alcohol dehydrogenase's Km value influences how quickly the body processes alcohol

    Regulation of Enzyme Activity

    • Enzymes are regulated in several ways, including enzyme synthesis, enzyme degradation and through modulation of the catalytic activity

    Regulation of Enzyme Activity (Continued)

    • Enzyme amount, enzyme modification, covalent modification, and compartments
    • Negative feedback, feed-forward activation, regulation through location
    • Phosphorylation/dephosphorylation; other modes of regulation, such as isozymes.

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    Description

    This quiz covers the role of enzymes as biocatalysts in biochemical reactions, focusing on their properties, classifications, and activities. It also explores glycolysis and the specific enzymes involved in the metabolic breakdown of glucose. Test your understanding of enzyme function and regulation through various questions.

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