Biochemistry: Enzyme Inhibition Quiz
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Questions and Answers

What type of bonding do irreversible inhibitors typically utilize to inhibit enzymes?

  • Covalent bonding (correct)
  • Ionic bonding
  • Hydrogen bonding
  • Hydrophobic interactions

Which enzyme is primarily active at a low pH in the stomach?

  • Amylase
  • Pepsin (correct)
  • Lipase
  • Trypsin

Which of the following compounds is known as an irreversible inhibitor that affects the nervous system?

  • Sarin (correct)
  • Atorvastatin
  • Ibuprofen
  • Penicillin

What distinguishes non-competitive inhibitors from competitive inhibitors?

<p>They bind to the enzyme regardless of substrate presence. (B)</p> Signup and view all the answers

What common feature is shared by both competitive and non-competitive inhibitors?

<p>Both types involve weak bonds in their interactions. (D)</p> Signup and view all the answers

What role do enzymes play in a chemical reaction?

<p>They lower the activation energy required for the reaction. (B)</p> Signup and view all the answers

What defines the specificity of an enzyme?

<p>The 3D shape of the enzyme and its active site. (A)</p> Signup and view all the answers

What is the active site of an enzyme?

<p>The location where the enzyme binds its substrate. (D)</p> Signup and view all the answers

What happens during the induced fit of a substrate to an enzyme?

<p>The active site undergoes a shape change to better fit the substrate. (B)</p> Signup and view all the answers

How does the presence of an enzyme affect the change in free energy ( extDelta G) of a reaction?

<p>It has no effect on the overall extDelta G of the reaction. (D)</p> Signup and view all the answers

Which factor is NOT associated with the enzyme activity?

<p>The molecular weight of the substrate. (A)</p> Signup and view all the answers

What is the result of an enzyme binding to its substrate?

<p>An enzyme-product complex is formed. (A)</p> Signup and view all the answers

What occurs during the course of a reaction that is facilitated by an enzyme?

<p>The enzyme increases the speed of reaching equilibrium. (A)</p> Signup and view all the answers

What is the primary role of feedback inhibition in metabolic pathways?

<p>To stop the cell from wasting resources by overproducing end products (B)</p> Signup and view all the answers

Which of the following serves as an example of feedback inhibition in catabolic pathways?

<p>ATP inhibiting further ATP production (B)</p> Signup and view all the answers

In the synthesis of isoleucine, what happens when isoleucine levels are high?

<p>Isoleucine binds to the allosteric site of enzyme 1, inhibiting the pathway (B)</p> Signup and view all the answers

What is the consequence of feedback inhibition for anabolic pathways?

<p>They are inhibited by their respective end products, conserving energy (C)</p> Signup and view all the answers

Which of the following best describes feedback inhibition?

<p>An end product inhibits the function of the metabolic pathway producing it (D)</p> Signup and view all the answers

Which molecule is directly responsible for inhibiting the isoleucine synthesis pathway?

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

How does feedback inhibition prevent metabolic waste?

<p>By turning off metabolic pathways when sufficient end products are present (A)</p> Signup and view all the answers

What is a common feature of feedback inhibition in both catabolic and anabolic pathways?

<p>It involves the allosteric interaction with one of the enzymes (A)</p> Signup and view all the answers

What does free energy represent in a living system?

<p>The energy that can do work under cellular conditions (B)</p> Signup and view all the answers

What does a negative free-energy change (ΔG < 0) indicate about a reaction?

<p>The reaction is exergonic and releases energy (B)</p> Signup and view all the answers

In an endergonic reaction, what is true about the free energy?

<p>ΔG is greater than 0, indicating energy is required (B)</p> Signup and view all the answers

How can the free-energy change (ΔG) of a reaction be calculated?

<p>By subtracting Gfinal from Ginitial (B)</p> Signup and view all the answers

Which reaction type primarily releases free energy as a byproduct?

<p>Catabolic reactions (C)</p> Signup and view all the answers

Which of the following is true for exergonic reactions?

<p>They do not require a catalyst to proceed (D)</p> Signup and view all the answers

What is the relationship between Ginitial and Gfinal in a reaction with ΔG < 0?

<p>Ginitial is greater than Gfinal (D)</p> Signup and view all the answers

What indicates a reaction is spontaneous?

<p>A negative ΔG value (C)</p> Signup and view all the answers

What occurs when substrates enter the enzyme's active site?

<p>The enzyme changes shape to accommodate the substrates. (C)</p> Signup and view all the answers

How do substrates interact with the enzyme's active site?

<p>Through weak interactions like hydrogen bonds. (B)</p> Signup and view all the answers

What is the role of the active site during the catalytic reaction?

<p>To stabilize the transition state and lower activation energy. (B)</p> Signup and view all the answers

What happens after the catalytic reaction is complete?

<p>The products are released, and the active site is free for new substrates. (B)</p> Signup and view all the answers

Which statement best describes how the enzyme environment contributes to reactions?

<p>It provides a favorable microenvironment for the reaction. (D)</p> Signup and view all the answers

Which of the following best describes the 'induced fit' model of enzyme action?

<p>The active site molds itself around the substrate upon binding. (D)</p> Signup and view all the answers

What is an essential factor that allows enzymes to speed up chemical reactions?

<p>Lower activation energy through stabilizing the transition state. (D)</p> Signup and view all the answers

Which component of the enzyme is primarily responsible for catalyzing the reaction?

<p>The active site. (C)</p> Signup and view all the answers

What is the primary function of competitive inhibitors in enzyme activity?

<p>They bind to the active site of the enzyme. (A)</p> Signup and view all the answers

Which statement is true about non-competitive inhibitors?

<p>They cannot be overcome by adding more substrate. (A)</p> Signup and view all the answers

What happens to enzyme activity when a competitive inhibitor is present?

<p>The inhibition can be reversed by increasing substrate concentration. (C)</p> Signup and view all the answers

What is a characteristic of non-competitive inhibition?

<p>The inhibitor changes the enzyme's conformation. (A)</p> Signup and view all the answers

How do competitive inhibitors affect substrate binding?

<p>They compete with substrate for the active site. (D)</p> Signup and view all the answers

Which of the following is NOT a characteristic of competitive inhibitors?

<p>They permanently change the enzyme structure. (A)</p> Signup and view all the answers

What is the result of a non-competitive inhibitor binding to an enzyme?

<p>The substrate can still bind to the active site normally. (D)</p> Signup and view all the answers

Which of the following best describes how competitive inhibition works?

<p>It involves the inhibitor mimicking the substrate. (D)</p> Signup and view all the answers

Flashcards

Free Energy

The ability of a living system to perform work under cellular conditions.

Free-Energy Change (ΔG)

The change in free energy during a reaction, indicating whether it will occur spontaneously or requires energy input.

Exergonic Reactions

Reactions that release free energy and occur spontaneously.

Endergonic Reactions

Reactions that require free energy input and do not occur spontaneously.

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Reactants

The starting materials of a reaction.

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Products

The substances produced during a reaction.

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Energy Change (ΔG)

The energy difference between reactants and products in a reaction.

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Progress of the reaction

The rate at which a reaction proceeds.

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Substrate

The reactant that an enzyme acts upon.

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Enzyme-substrate complex

The enzyme binds to its specific substrate, forming a temporary complex. This complex is essential for the enzyme's action.

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Substrate Specificity

The ability of an enzyme to bind only to specific substrates, excluding other similar molecules. This is due to the enzyme's unique 3D shape.

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Active site

The region on the enzyme where the substrate binds. This area is specifically designed to recognize and interact with the substrate.

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Induced fit of a substrate

The enzyme's shape changes slightly upon substrate binding. This change helps bring the active site's chemical groups into ideal positions to catalyze the reaction.

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Effect of an enzyme on reaction rate

Enzymes speed up reactions by lowering the activation energy, which is the energy needed to start the reaction. The enzyme doesn't change the change in free energy (∆G) of the reaction.

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Activation energy (EA)

The amount of energy required for a chemical reaction to start.

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Change in free energy (∆G)

The difference in free energy between the reactants and products. It determines whether a reaction will occur spontaneously or not.

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Induced Fit

The active site of an enzyme changes shape to fit the substrate, like a hand adjusting to hold an object more securely.

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Catalysis

The process by which enzymes speed up chemical reactions by lowering activation energy.

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Catalytic Cycle

The series of steps involved in an enzyme-catalyzed reaction.

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Optimal pH for an Enzyme

The specific pH value at which an enzyme exhibits its highest activity.

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Competitive Inhibitor

A type of enzyme inhibitor that binds to the enzyme's active site, preventing the substrate from binding and blocking the reaction.

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Non-competitive Inhibitor

A type of enzyme inhibitor that binds to a site on the enzyme that is not the active site. This binding changes the enzyme's shape, making it less active.

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Irreversible Enzyme Inhibitor

Enzyme inhibitors that form strong covalent bonds with the enzyme, permanently inactivating it.

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Reversible Enzyme Inhibitor

Enzyme inhibitors that bind to enzymes through weak interactions, such as hydrogen bonds or ionic bonds. These bonds are easily broken, allowing the enzyme to regain its activity.

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Enzyme-Substrate Binding

A temporary bond that forms between an enzyme and its substrate.

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Feedback Inhibition

A regulatory mechanism where the end product of a metabolic pathway inhibits an earlier step in the same pathway.

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Purpose of Feedback Inhibition

Feedback inhibition prevents a cell from wasting resources by overproducing a substance.

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How Feedback Inhibition Works

In feedback inhibition, the end product binds to an allosteric site on an enzyme, changing its shape and reducing its activity.

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ATP as a Feedback Inhibitor

ATP, the energy currency of cells, can inhibit catabolic pathways that generate ATP.

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Tryptophan Synthesis Inhibition

The synthesis of tryptophan, an amino acid, is inhibited by tryptophan itself.

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Substrate Binding in Feedback Inhibition

The initial substrate in a pathway, such as threonine in isoleucine synthesis, binds to the active site of an enzyme.

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Isoleucine Binding in Feedback Inhibition

When isoleucine is present in sufficient amounts, it binds to an allosteric site on the enzyme threonine deaminase, preventing further threonine from binding.

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Importance of Feedback Inhibition

Feedback inhibition is a key regulatory mechanism that prevents cells from wasting resources and ensures the efficient production of essential substances.

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Study Notes

Introduction to Metabolism

  • Metabolism encompasses all chemical reactions in an organism.
  • These reactions involve energy storage (anabolic processes) and energy release (catabolic processes).
  • The energy source on Earth is sunlight.
  • Plants use photosynthesis to synthesize sugars using sunlight.
  • Living cells act as miniature factories converting energy in many ways.
  • An example of this is bioluminescence, in which organisms convert energy to light.
  • The sun provides energy for Producers (plants), Consumers (animals) and Decomposers (organisms that break down matter).

Energy Flow

  • Energy flows from the sun to producers to consumers to decomposers.

Metabolic Pathways

  • A metabolic pathway consists of multiple steps that begin with a specific molecule and end in a product.
  • Each step is catalyzed by a specific enzyme.
  • Metabolic pathways are regulated according to cellular needs.
  • Catabolic pathways break down complex molecules into simpler compounds releasing energy. Cellular respiration is an example of a catabolic pathway. This reaction releases energy for the cell.
  • Anabolic pathways build complex molecules from simpler ones consuming energy. Examples are photosynthesis and protein synthesis from amino acids.

Forms of Energy

  • Energy is the capacity to cause change.
  • Exists in various forms.
  • Some forms of energy can do work.
  • Life depends on a cell's ability to convert energy from one form to another.
  • Thermodynamics is the study of energy conversion.

Kinetic and Potential Energy

  • Kinetic energy is associated with motion.
  • Heat (thermal energy) is kinetic energy associated with the random motion of atoms or molecules.
  • Potential (chemical) energy is stored in the location or structure of matter. It includes chemical energy stored in molecular structure.

Laws of Thermodynamics

  • The first law states that energy can be transferred and transformed but not created or destroyed.
  • In the cheetah example, the chemical potential energy in the food is converted into the kinetic energy for the cheetah's movement.
  • The second law states that every energy transfer or transformation increases the entropy (disorder) of the universe. This is evident in the byproducts of metabolism, which are molecules.

Biological Order

  • Living organisms increase the entropy of the universe but decrease the entropy internally by maintaining order through energy consumption.

Free Energy

  • Organisms live by consuming free energy.
  • Free energy is a living system's energy that can do work under cellular conditions.
  • The free-energy change (ΔG) of a reaction predicts spontaneity.

Exergonic and Endergonic Reactions

  • Exergonic reactions are spontaneous and release free energy (ΔG < 0).
  • Endergonic reactions are non-spontaneous and absorb free energy from their surroundings (ΔG > 0).

Equilibrium and Metabolism

  • Reactions in a closed system eventually reach equilibrium (ΔG = 0).
  • Cells in our body are open systems with metabolic pathways that experience a constant flow of materials in and out, preventing them from reaching equilibrium.

ATP

  • ATP (adenosine triphosphate) is the cell's energy shuttle.
  • ATP stores energy in phosphate bonds.
  • ATP hydrolysis releases energy (ATP → ADP + Pi).
  • ATP synthesis stores energy (ADP + Pi → ATP).
  • ATP powers cellular work via energy coupling.
  • Cells use ATP to power mechanical, transport, and chemical work.

Enzymes

  • Enzymes are catalytic proteins that speed up metabolic reactions by lowering activation energy barriers.
  • Enzymes are catalysts, which speed up a reaction without being consumed by it.
  • Sucrase is the enzyme that catalyzes sucrose hydrolysis.

Activation Energy

  • Activation energy (EA) is the initial amount of energy needed to start a chemical reaction, which de-stabilizes the structure of reactants, allowing for more easy reaction to occur.
  • Heat can increase the energy of molecules, allowing them to collide frequently enough to start reactions.

Enzyme Activity and Factors

  • Enzymes have an optimal temperature for function. Extreme temperatures can denature enzymes, causing loss of structure and function.
  • Optimum pH levels exist for enzymatic activity. Denaturation also occurs outside of optimum pH levels, resulting in loss of function.
  • Cofactors such as inorganic metal ions and organic vitamins are required for enzymatic activity.

Enzyme Inhibitors

  • Irreversible inhibitors bind to enzymes covalently, permanently inhibiting their function.
  • Examples of irreversible inhibitors are some toxins, antibiotics, and poisons.
  • Reversible inhibitors bind weakly to enzymes, allowing the enzyme to regain activity.
  • Competitive inhibitors compete with substrates for the active site of an enzyme.
  • Non-competitive inhibitors bind to a different site on the enzyme, altering its shape and hindering its function.

Regulation of Enzyme Activity

  • A cell's metabolic pathways must be regulated to prevent waste of resources.
  • Enzyme regulation involves adjusting enzyme production or activity.
  • Feedback inhibition prevents pathways from making more of a product than necessary. The end product of a metabolic pathway inhibits the pathway.
  • Allosteric regulation is a type of reversible regulation where a regulatory molecule binds to a site different from the active site, affecting enzyme function.
  • Homeotropic allosteric regulation means that enzyme subunits are affected by the binding of a substrate and are either activated or inhibited by the substrate.
  • Heterotropic allosteric regulation means that an activator or inhibitor is affecting the activity of an enzyme even though it is not a substrate.

Specific Localization of Enzymes

  • Enzymes in the same pathway are often located near each other inside the cell, in complexes, in membranes, or in organelles.
  • Mitochondria are the sites of cellular respiration, containing many enzymes required for this process.

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Test your knowledge on enzyme inhibition mechanisms, including the differences between competitive and non-competitive inhibitors. Explore the characteristics of irreversible inhibitors and their effects on enzymes, as well as the specific enzymes active under varying pH conditions, such as in the stomach.

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