Enzymology and Enzyme Structure
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Questions and Answers

What term describes the noncovalent binding of a specific metabolite to a site other than the active site to modulate enzyme activity?

  • Reversible covalent modification
  • Enzyme denaturation
  • Competitive inhibition
  • Allosteric regulation (correct)
  • Which of the following is the most common type of reversible covalent modification of enzyme activity?

  • Acetylation
  • Phosphorylation (correct)
  • Glycosylation
  • Methylation
  • What is the term for the protein portion of an enzyme, which requires other components to be active?

  • Prosthetic group
  • Apoenzyme (correct)
  • Coenzyme
  • Cofactor
  • Which of the following acts as a coenzyme that is essential for electron transfer in enzymatic reactions?

    <p>Coenzyme Q (D)</p> Signup and view all the answers

    Which of the following best describes an allosteric modulator?

    <p>A metabolite that binds to the allosteric site and alters enzyme activity (D)</p> Signup and view all the answers

    What role does the active site of an enzyme play in its function?

    <p>It binds the substrate molecule and facilitates its transformation. (C)</p> Signup and view all the answers

    Which statement best describes the specificity of enzymes?

    <p>Enzymes are highly specific, typically binding only one substrate. (C)</p> Signup and view all the answers

    What is the primary effect of enzymes on reaction activation energy?

    <p>They decrease the activation energy, facilitating the reaction. (B)</p> Signup and view all the answers

    In which stage of the enzymatic reaction does the E-S complex transform into a transition complex?

    <p>Transformation of the E-S complex. (D)</p> Signup and view all the answers

    How do enzymatic reactions differ from non-enzymatic reactions?

    <p>Enzymatic reactions occur at a faster rate with less energy input. (D)</p> Signup and view all the answers

    What can modulate the activity of enzymes?

    <p>Agents that modify the active site. (B)</p> Signup and view all the answers

    What is the primary purpose of coenzymes in enzymatic reactions?

    <p>To enhance enzyme activity and assist in substrate binding. (C)</p> Signup and view all the answers

    During an enzymatic reaction, what is formed immediately after the E-S complex?

    <p>Transition complex. (A)</p> Signup and view all the answers

    What does the rate or velocity of a reaction (V0) represent?

    <p>The number of substrate molecules converted to product per unit time (C)</p> Signup and view all the answers

    What occurs at maximum velocity (Vmax) in an enzymatic reaction?

    <p>All enzyme active sites are occupied by substrate (B)</p> Signup and view all the answers

    Which factor directly decreases substrate concentration during a reaction?

    <p>Formation of product from substrate (A)</p> Signup and view all the answers

    What is a regulatory enzyme's role within a metabolic pathway?

    <p>To activate or inhibit other enzymes and affect overall reaction rates (B)</p> Signup and view all the answers

    Which statement about enzymatic kinetics is true?

    <p>Enzymes exhibit optimal activity within specific temperature and pH ranges (A)</p> Signup and view all the answers

    What typically happens to reaction velocity (V0) as enzyme concentration increases?

    <p>V0 increases until a maximum velocity is reached (C)</p> Signup and view all the answers

    Which of the following is NOT a factor that affects reaction rate?

    <p>Time duration of the experiment (A)</p> Signup and view all the answers

    What is the consequence of having too high or too low pH for an enzyme's activity?

    <p>Enzyme activity may decrease or become denatured (A)</p> Signup and view all the answers

    Flashcards

    Enzyme

    A protein that speeds up a specific chemical reaction in living things.

    Active site

    The part of an enzyme where the substrate binds and the reaction happens.

    Substrate specificity

    Enzymes only bind to a particular substrate.

    Enzyme efficiency

    Enzymes increase the speed of reactions without being used up.

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    Enzyme regulation

    Changing how active an enzyme is.

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    Activation energy

    The energy needed to start a chemical reaction.

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    Enzyme-substrate complex

    The temporary complex formed when an enzyme binds to its substrate.

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    Enzymatic reaction

    A reaction accelerated by an enzyme.

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    Allosteric Regulation

    A way to control enzyme activity by binding a molecule at a site other than the active site, influencing the enzyme's shape and activity.

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    Allosteric site

    The specific site on an allosteric protein where a modulator or effector molecule binds, changing the enzyme's shape and activity.

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    Allosteric Modulator

    A small molecule that binds to an allosteric site of an enzyme, altering the enzyme's activity, either increasing (activator) or decreasing (inhibitor) it.

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    Reversible Covalent Modification

    A way to regulate enzyme activity where a molecule is covalently attached to the enzyme, changing its activity; this attachment can be reversed.

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    Phosphorylation

    A common type of reversible covalent modification where a phosphate group is added to an enzyme, changing its activity.

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    Enzymatic Kinetics

    The study of how the rate of an enzyme-catalyzed reaction changes in response to different conditions, like substrate concentration or temperature.

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    Reaction Rate (Velocity)

    The number of substrate molecules converted to product per unit of time. It indicates how quickly a reaction is happening.

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    What is V0?

    The initial reaction rate, measured at the beginning of the reaction when product concentration is low and substrate concentration is high.

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    Maximum Velocity (Vmax)

    The fastest rate a reaction can achieve when all enzyme active sites are occupied by substrate.

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    Factors Affecting Reaction Rate

    Conditions like enzyme concentration, substrate concentration, pH, and temperature can influence how fast a reaction proceeds.

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    Metabolic Pathway

    A series of linked enzymatic reactions where the product of one reaction becomes the substrate for the next.

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    Regulatory Enzyme

    An enzyme that controls the rate of a metabolic pathway by being activated or inhibited. It acts as a switch.

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    How do Metabolic Pathways change Rate?

    Changes in the activity of regulatory enzymes often determine the overall speed of a metabolic pathway.

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    Study Notes

    Enzymology

    • Enzymology is the study of enzymes
    • Enzymes are proteins that catalyze specific chemical reactions in biological systems
    • Enzymes increase the rate of reactions, lowering the activation energy required
    • Enzymes have a specific active site where the substrate binds

    Structure of Enzymes

    • Active site: the region of an enzyme surface that binds the substrate, also known as the catalytic site
    • Catalytic activity depends on the native protein conformation; the surface of the active site is lined with amino acid residues that bind the substrate and catalyze the chemical transformation
    • Enzymes increase the speed of reactions

    Enzymes Properties

    • High specificity; enzymes bind to only one substrate and catalyze a specific reaction
    • Efficiency: proximity creates tension between the substrate and catalytic residues; increase the reaction rate in mild conditions, compatible with life
    • Enzymatic reactions occur in specialized pockets called active sites
    • Under regulation: Some agents can modulate their activity by modifying the active site

    How Do Enzymes Work?

    • Enzymes lower the activation energy needed for a chemical reaction to occur
    • Enzymes decrease the energy needed to reach the intermediate state between reactants and products, improving reaction rates
    • Enzymes form a temporary complex (enzyme-substrate complex) with the substrate
    • Steps in an enzymatic reaction:
      • Enzyme-substrate complex formation
      • Transition-complex formation from the enzyme-substrate complex
      • Formation of the enzyme-product complex
      • Release of the product and the enzyme

    Enzymatic Kinetics

    • Study of the rate of reaction and how it changes in response to changes in experimental parameters
    • Rate or velocity of a reaction (V): number of substrate molecules converted to product per unit time

    Enzymatic Kinetics (External Factors)

    • Factors affecting reaction rate:
      • Enzyme concentration
      • Substrate concentration
      • pH
      • Temperature
      • Maximum velocity (Vmax): Maximum rate of a reaction when the enzyme is saturated with substrate

    Metabolic Pathways

    • Metabolic pathway: sequence of consecutive enzymatic reactions
    • Each pathway consists of several reactions with multiple enzymes.
    • Each pathway includes one or more enzymes with a significant effect on the rate (velocity) of the overall process.
    • Enzymes with a regulatory function are called regulatory enzymes; they undergo changes in activity through mechanisms like allosteric regulation or covalent modification
    • Changes in the rate of a metabolic pathway are caused by changes in the regulatory enzymes present within the specific pathway

    Regulators of Enzyme Activity (Allosteric Regulation)

    • Allosteric regulation: regulatory enzyme with catalytic activity modulated by non-covalent binding of a specific metabolite at a site different from the active site
    • Allosteric inhibitor: modulator that distorts the active site to inhibit enzymatic activity
    • Allosteric activator: modulator that distorts the active site to improve enzymatic activity

    Regulators of Enzyme Activity (Reversible Covalent Modification)

    • Reversible covalent modification: enzyme activity is modulated by covalent modifications (e.g., phosphorylation or dephosphorylation)
    • Phosphorylation: addition of a phosphate group to an amino acid residue within the enzyme; often a signal for increased activity
    • Dephosphorylation: removal of a phosphate group, typically leading to reduced activity
    • Hormonal signals like adrenaline, glucagon, or insulin often control these modifications

    Regulators of Enzyme Activity (Phosphorylation Cascade)

    • Phosphorylation cascade: series of proteins in a pathway where phosphorylation of one protein activates the next, amplifying the signal
    • Active Protein Kinase associates with the receptor and initiates a cascade of interactions between proteins

    Coenzymes

    • Coenzymes: complex organic or metalloorganic molecules; derive from vitamins (e.g., Coenzyme A, NADH, FADH2) or non-vitamins (e.g., Coenzyme Q, NTP)
    • Apoenzyme: protein component of an enzyme
    • Prosthetic group: non-protein component essential for enzyme function

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    Enzymology Lesson 5 PDF

    Description

    This quiz focuses on the study of enzymes, their structures, and properties. You will learn about active sites, catalytic activity, and the specificity and efficiency of enzymes in biological reactions. Test your knowledge on these essential biochemical catalysts.

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