Podcast
Questions and Answers
What type of bonding do irreversible inhibitors typically utilize to inhibit enzymes?
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?
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?
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?
What distinguishes non-competitive inhibitors from competitive inhibitors?
What common feature is shared by both competitive and non-competitive inhibitors?
What common feature is shared by both competitive and non-competitive inhibitors?
What role do enzymes play in a chemical reaction?
What role do enzymes play in a chemical reaction?
What defines the specificity of an enzyme?
What defines the specificity of an enzyme?
What is the active site of an enzyme?
What is the active site of an enzyme?
What happens during the induced fit of a substrate to an enzyme?
What happens during the induced fit of a substrate to an enzyme?
How does the presence of an enzyme affect the change in free energy ( extDelta G) of a reaction?
How does the presence of an enzyme affect the change in free energy ( extDelta G) of a reaction?
Which factor is NOT associated with the enzyme activity?
Which factor is NOT associated with the enzyme activity?
What is the result of an enzyme binding to its substrate?
What is the result of an enzyme binding to its substrate?
What occurs during the course of a reaction that is facilitated by an enzyme?
What occurs during the course of a reaction that is facilitated by an enzyme?
What is the primary role of feedback inhibition in metabolic pathways?
What is the primary role of feedback inhibition in metabolic pathways?
Which of the following serves as an example of feedback inhibition in catabolic pathways?
Which of the following serves as an example of feedback inhibition in catabolic pathways?
In the synthesis of isoleucine, what happens when isoleucine levels are high?
In the synthesis of isoleucine, what happens when isoleucine levels are high?
What is the consequence of feedback inhibition for anabolic pathways?
What is the consequence of feedback inhibition for anabolic pathways?
Which of the following best describes feedback inhibition?
Which of the following best describes feedback inhibition?
Which molecule is directly responsible for inhibiting the isoleucine synthesis pathway?
Which molecule is directly responsible for inhibiting the isoleucine synthesis pathway?
How does feedback inhibition prevent metabolic waste?
How does feedback inhibition prevent metabolic waste?
What is a common feature of feedback inhibition in both catabolic and anabolic pathways?
What is a common feature of feedback inhibition in both catabolic and anabolic pathways?
What does free energy represent in a living system?
What does free energy represent in a living system?
What does a negative free-energy change (ΔG < 0) indicate about a reaction?
What does a negative free-energy change (ΔG < 0) indicate about a reaction?
In an endergonic reaction, what is true about the free energy?
In an endergonic reaction, what is true about the free energy?
How can the free-energy change (ΔG) of a reaction be calculated?
How can the free-energy change (ΔG) of a reaction be calculated?
Which reaction type primarily releases free energy as a byproduct?
Which reaction type primarily releases free energy as a byproduct?
Which of the following is true for exergonic reactions?
Which of the following is true for exergonic reactions?
What is the relationship between Ginitial and Gfinal in a reaction with ΔG < 0?
What is the relationship between Ginitial and Gfinal in a reaction with ΔG < 0?
What indicates a reaction is spontaneous?
What indicates a reaction is spontaneous?
What occurs when substrates enter the enzyme's active site?
What occurs when substrates enter the enzyme's active site?
How do substrates interact with the enzyme's active site?
How do substrates interact with the enzyme's active site?
What is the role of the active site during the catalytic reaction?
What is the role of the active site during the catalytic reaction?
What happens after the catalytic reaction is complete?
What happens after the catalytic reaction is complete?
Which statement best describes how the enzyme environment contributes to reactions?
Which statement best describes how the enzyme environment contributes to reactions?
Which of the following best describes the 'induced fit' model of enzyme action?
Which of the following best describes the 'induced fit' model of enzyme action?
What is an essential factor that allows enzymes to speed up chemical reactions?
What is an essential factor that allows enzymes to speed up chemical reactions?
Which component of the enzyme is primarily responsible for catalyzing the reaction?
Which component of the enzyme is primarily responsible for catalyzing the reaction?
What is the primary function of competitive inhibitors in enzyme activity?
What is the primary function of competitive inhibitors in enzyme activity?
Which statement is true about non-competitive inhibitors?
Which statement is true about non-competitive inhibitors?
What happens to enzyme activity when a competitive inhibitor is present?
What happens to enzyme activity when a competitive inhibitor is present?
What is a characteristic of non-competitive inhibition?
What is a characteristic of non-competitive inhibition?
How do competitive inhibitors affect substrate binding?
How do competitive inhibitors affect substrate binding?
Which of the following is NOT a characteristic of competitive inhibitors?
Which of the following is NOT a characteristic of competitive inhibitors?
What is the result of a non-competitive inhibitor binding to an enzyme?
What is the result of a non-competitive inhibitor binding to an enzyme?
Which of the following best describes how competitive inhibition works?
Which of the following best describes how competitive inhibition works?
Flashcards
Free Energy
Free Energy
The ability of a living system to perform work under cellular conditions.
Free-Energy Change (ΔG)
Free-Energy Change (ΔG)
The change in free energy during a reaction, indicating whether it will occur spontaneously or requires energy input.
Exergonic Reactions
Exergonic Reactions
Reactions that release free energy and occur spontaneously.
Endergonic Reactions
Endergonic Reactions
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Reactants
Reactants
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Products
Products
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Energy Change (ΔG)
Energy Change (ΔG)
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Progress of the reaction
Progress of the reaction
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Substrate
Substrate
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Enzyme-substrate complex
Enzyme-substrate complex
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Substrate Specificity
Substrate Specificity
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Active site
Active site
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Induced fit of a substrate
Induced fit of a substrate
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Effect of an enzyme on reaction rate
Effect of an enzyme on reaction rate
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Activation energy (EA)
Activation energy (EA)
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Change in free energy (∆G)
Change in free energy (∆G)
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Induced Fit
Induced Fit
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Catalysis
Catalysis
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Catalytic Cycle
Catalytic Cycle
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Optimal pH for an Enzyme
Optimal pH for an Enzyme
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Competitive Inhibitor
Competitive Inhibitor
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Non-competitive Inhibitor
Non-competitive Inhibitor
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Irreversible Enzyme Inhibitor
Irreversible Enzyme Inhibitor
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Reversible Enzyme Inhibitor
Reversible Enzyme Inhibitor
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Enzyme-Substrate Binding
Enzyme-Substrate Binding
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Feedback Inhibition
Feedback Inhibition
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Purpose of Feedback Inhibition
Purpose of Feedback Inhibition
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How Feedback Inhibition Works
How Feedback Inhibition Works
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ATP as a Feedback Inhibitor
ATP as a Feedback Inhibitor
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Tryptophan Synthesis Inhibition
Tryptophan Synthesis Inhibition
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Substrate Binding in Feedback Inhibition
Substrate Binding in Feedback Inhibition
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Isoleucine Binding in Feedback Inhibition
Isoleucine Binding in Feedback Inhibition
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Importance of Feedback Inhibition
Importance of Feedback Inhibition
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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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Description
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.