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This deck focuses on Enzymes, giving you a quick way to review the definitions, rules, and examples that matter most for AP Biology.
AP Biology Flashcards: Enzymes
Study Enzymes in AP Biology with focused flashcards that help you recognize the idea, recall the key rule, and apply it in practice-style prompts.
AP Biology
Enzymes
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Define the term 'apoenzyme'.
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ANSWER
Inactive enzyme lacking its cofactor. Requires cofactor binding to become catalytically active.
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Flashcard 1: Define the term 'apoenzyme'.
Answer: Inactive enzyme lacking its cofactor. Requires cofactor binding to become catalytically active.
Flashcard 2: Identify the term for the protein component of an enzyme without its cofactor.
Answer: Apoenzyme. The protein part that needs cofactors to become fully functional.
Flashcard 3: Which term describes enzymes that remain unchanged after a reaction?
Answer: Reusable. Enzymes are not consumed and can catalyze multiple reaction cycles.
Flashcard 4: Which enzyme is responsible for breaking down proteins?
Answer: Protease. Cleaves peptide bonds in proteins during digestion.
Flashcard 5: What effect does enzyme concentration have on reaction rate?
Answer: Increases rate until substrate saturation. More enzymes mean more active sites until all substrate is bound.
Flashcard 6: Identify the type of inhibition where an inhibitor binds to the active site.
Answer: Competitive inhibition. Inhibitor competes with substrate for the same binding site.
Flashcard 7: What is the primary function of enzymes in biological systems?
Answer: Catalysts that lower activation energy of reactions. They speed up reactions by reducing the energy barrier needed to start them.
Flashcard 8: What is the term for a non-protein molecule aiding enzyme function?
Answer: Cofactor. Inorganic helper molecule essential for proper enzyme function.
Flashcard 9: Which factor does not affect enzyme activity: temperature, pH, or light?
Answer: Light. Light doesn't directly affect enzyme structure or chemical activity.
Flashcard 10: What is the term for the minimum energy required to start a reaction?
Answer: Activation energy. Energy barrier that enzymes lower to speed up reactions.
Flashcard 11: Identify the term for enzyme helpers that are small organic molecules.
Answer: Coenzymes. Organic molecules like vitamins that assist in enzyme catalysis.
Flashcard 12: Identify the term for a molecule that decreases enzyme activity.
Answer: Inhibitor. Reduces enzyme function through competitive or non-competitive mechanisms.
Flashcard 13: What is the role of an allosteric site in enzyme regulation?
Answer: Site for non-competitive inhibitors or activators. Regulatory binding site separate from the active site.
Flashcard 14: Which term describes the enzyme-substrate complex transition state?
Answer: Transition state. High-energy intermediate formed during the enzyme-catalyzed reaction.
Flashcard 15: What is the effect of non-competitive inhibitors on Vmax?
Answer: Decreases Vmax. Cannot reach the same maximum rate as uninhibited enzyme.
Flashcard 16: Which term describes the enzyme-substrate complex transition state?
Answer: Transition state. High-energy intermediate formed during the enzyme-catalyzed reaction.
Flashcard 17: What type of macromolecule are enzymes typically classified as?
Answer: Proteins. Made of amino acid chains folded into specific 3D structures.
Flashcard 18: What happens to enzyme activity when pH is altered from optimal?
Answer: Activity decreases. pH changes alter enzyme shape and charge distribution at the active site.
Flashcard 19: What is the primary factor determining enzyme specificity?
Answer: Shape of the active site. Complementary shape between active site and substrate ensures selectivity.
Flashcard 20: Identify the type of inhibition where an inhibitor binds to the active site.
Answer: Competitive inhibition. Inhibitor competes with substrate for the same binding site.
Flashcard 21: What does 'substrate saturation' refer to in enzyme kinetics?
Answer: Point where increasing substrate does not increase rate. All enzyme active sites are occupied, creating maximum reaction rate.
Flashcard 22: What is the effect of enzyme concentration on reaction rate if substrate is limited?
Answer: No effect. Substrate becomes the limiting factor, not enzyme availability.
Flashcard 23: What is the primary structural unit of an enzyme?
Answer: Amino acids. Linked amino acids form the backbone of all enzyme structures.
Flashcard 24: Identify the term for the protein component of an enzyme without its cofactor.
Answer: Apoenzyme. The protein part that needs cofactors to become fully functional.
Flashcard 25: What is the result of enzyme denaturation?
Answer: Loss of structure and function. Heat or pH extremes unfold the protein, destroying active site shape.
Flashcard 26: Identify the term for enzymes with multiple forms that catalyze the same reaction.
Answer: Isozymes. Different enzyme variants that perform the same catalytic function.
Flashcard 27: What is the effect of temperature on enzyme activity?
Answer: Increases activity up to an optimal point; then decreases. Heat increases molecular motion but denatures enzymes at extreme temperatures.
Flashcard 28: What is the term for a reaction rate plateau despite increased substrate?
Answer: Saturation. Maximum rate reached when all enzymes are working at full capacity.
Flashcard 29: Which part of the enzyme is altered during feedback inhibition?
Answer: Allosteric site. End product binds here to inhibit the enzyme that produces it.
Flashcard 30: Identify the part of the enzyme where substrate molecules bind.
Answer: Active site. This binding region has a specific shape complementary to the substrate.
Flashcard 31: Which term describes the specific 3D arrangement of an enzyme?
Answer: Conformation. 3D shape determines function and substrate binding specificity.
Flashcard 32: What is the primary factor determining enzyme specificity?
Answer: Shape of the active site. Complementary shape between active site and substrate ensures selectivity.
Flashcard 33: What is the role of a coenzyme in enzyme activity?
Answer: Organic cofactor aiding enzyme function. Works as a temporary carrier of atoms or functional groups.
Flashcard 34: What is the role of an allosteric site in enzyme regulation?
Answer: Site for non-competitive inhibitors or activators. Regulatory binding site separate from the active site.
Flashcard 35: Which factor does not affect enzyme activity: temperature, pH, or light?
Answer: Light. Light doesn't directly affect enzyme structure or chemical activity.
Flashcard 36: What is the primary structural unit of an enzyme?
Answer: Amino acids. Linked amino acids form the backbone of all enzyme structures.
Flashcard 37: State the effect of a non-competitive inhibitor on enzyme activity.
Answer: Reduces activity regardless of substrate concentration. Binds to allosteric site, changing enzyme shape and reducing function.
Flashcard 38: Which molecule acts as a common coenzyme in redox reactions?
Answer: NAD+. Essential electron carrier in cellular respiration and metabolism.
Flashcard 39: What is the effect of non-competitive inhibitors on Vmax?
Answer: Decreases Vmax. Cannot reach the same maximum rate as uninhibited enzyme.
Flashcard 40: Which molecule acts as a common coenzyme in redox reactions?
Answer: NAD+. Essential electron carrier in cellular respiration and metabolism.
Flashcard 41: What is the primary function of enzymes in biological systems?
Answer: Catalysts that lower activation energy of reactions. They speed up reactions by reducing the energy barrier needed to start them.
Flashcard 42: Identify the term for a molecule that decreases enzyme activity.
Answer: Inhibitor. Reduces enzyme function through competitive or non-competitive mechanisms.
Flashcard 43: What does 'substrate saturation' refer to in enzyme kinetics?
Answer: Point where increasing substrate does not increase rate. All enzyme active sites are occupied, creating maximum reaction rate.
Flashcard 44: Which enzyme catalyzes the breakdown of hydrogen peroxide?
Answer: Catalase. Converts toxic H2O2 into harmless water and oxygen.
Flashcard 45: What is the result of enzyme denaturation?
Answer: Loss of structure and function. Heat or pH extremes unfold the protein, destroying active site shape.
Flashcard 46: Name an enzyme that breaks down starch into sugar.
Answer: Amylase. Breaks down starch into maltose and glucose for energy.
Flashcard 47: What effect does enzyme concentration have on reaction rate?
Answer: Increases rate until substrate saturation. More enzymes mean more active sites until all substrate is bound.
Flashcard 48: Which term describes enzymes that remain unchanged after a reaction?
Answer: Reusable. Enzymes are not consumed and can catalyze multiple reaction cycles.
Flashcard 49: Identify the term for enzymes with multiple forms that catalyze the same reaction.
Answer: Isozymes. Different enzyme variants that perform the same catalytic function.
Flashcard 50: What type of macromolecule are enzymes typically classified as?
Answer: Proteins. Made of amino acid chains folded into specific 3D structures.
Flashcard 51: Which term describes the enzyme's specificity to its substrate?
Answer: Lock and key model. Describes how enzyme shape perfectly matches its specific substrate.
Flashcard 52: What happens to enzyme activity when pH is altered from optimal?
Answer: Activity decreases. pH changes alter enzyme shape and charge distribution at the active site.
Flashcard 53: What is the role of a coenzyme in enzyme activity?
Answer: Organic cofactor aiding enzyme function. Works as a temporary carrier of atoms or functional groups.
Flashcard 54: Which enzyme is responsible for breaking down proteins?
Answer: Protease. Cleaves peptide bonds in proteins during digestion.
Flashcard 55: What is the term for a reaction rate plateau despite increased substrate?
Answer: Saturation. Maximum rate reached when all enzymes are working at full capacity.
Flashcard 56: What is the effect of competitive inhibitors on Km?
Answer: Increases Km. Requires higher substrate concentration to reach half-maximal velocity.
Flashcard 57: What is the effect of competitive inhibitors on Km?
Answer: Increases Km. Requires higher substrate concentration to reach half-maximal velocity.
Flashcard 58: State the effect of a non-competitive inhibitor on enzyme activity.
Answer: Reduces activity regardless of substrate concentration. Binds to allosteric site, changing enzyme shape and reducing function.
Flashcard 59: What is the term for a non-protein molecule aiding enzyme function?
Answer: Cofactor. Inorganic helper molecule essential for proper enzyme function.
Flashcard 60: What is the effect of temperature on enzyme activity?
Answer: Increases activity up to an optimal point; then decreases. Heat increases molecular motion but denatures enzymes at extreme temperatures.
Flashcard 61: Identify an example of an enzyme that operates optimally in acidic conditions.
Answer: Pepsin. Functions optimally at stomach pH around 1.5-2.0.
Flashcard 62: Identify the hypothesis describing enzyme-induced fit with substrates.
Answer: Induced fit model. Enzyme slightly changes shape to better accommodate the substrate.
Flashcard 63: Identify the type of inhibition that is reversible by increasing substrate concentration.
Answer: Competitive inhibition. Adding more substrate can overcome this type of inhibition.
Flashcard 64: Identify the term for enzyme helpers that are small organic molecules.
Answer: Coenzymes. Organic molecules like vitamins that assist in enzyme catalysis.
Flashcard 65: What is the term for the minimum energy required to start a reaction?
Answer: Activation energy. Energy barrier that enzymes lower to speed up reactions.
Flashcard 66: Identify the part of the enzyme where substrate molecules bind.
Answer: Active site. This binding region has a specific shape complementary to the substrate.
Flashcard 67: Name an enzyme that breaks down starch into sugar.
Answer: Amylase. Breaks down starch into maltose and glucose for energy.
Flashcard 68: What is the function of a prosthetic group in enzyme activity?
Answer: Tightly bound cofactor aiding enzyme function. Permanently attached cofactor that's part of the enzyme structure.
Flashcard 69: Identify the hypothesis describing enzyme-induced fit with substrates.
Answer: Induced fit model. Enzyme slightly changes shape to better accommodate the substrate.
Flashcard 70: Identify the type of inhibition that is reversible by increasing substrate concentration.
Answer: Competitive inhibition. Adding more substrate can overcome this type of inhibition.
Flashcard 71: What is the function of a prosthetic group in enzyme activity?
Answer: Tightly bound cofactor aiding enzyme function. Permanently attached cofactor that's part of the enzyme structure.
Flashcard 72: Which term describes the enzyme's specificity to its substrate?
Answer: Lock and key model. Describes how enzyme shape perfectly matches its specific substrate.
Flashcard 73: Which enzyme catalyzes the breakdown of hydrogen peroxide?
Answer: Catalase. Converts toxic H2O2 into harmless water and oxygen.
Flashcard 74: Identify an example of an enzyme that operates optimally in acidic conditions.
Answer: Pepsin. Functions optimally at stomach pH around 1.5-2.0.
Flashcard 75: What is the effect of enzyme concentration on reaction rate if substrate is limited?
Answer: No effect. Substrate becomes the limiting factor, not enzyme availability.
Flashcard 76: Define the term 'apoenzyme'.
Answer: Inactive enzyme lacking its cofactor. Requires cofactor binding to become catalytically active.
Flashcard 77: Which part of the enzyme is altered during feedback inhibition?
Answer: Allosteric site. End product binds here to inhibit the enzyme that produces it.
Flashcard 78: Which term describes the specific 3D arrangement of an enzyme?
Answer: Conformation. 3D shape determines function and substrate binding specificity.