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Questions and Answers
What is the primary function of enzymes in a chemical reaction?
What is the primary function of enzymes in a chemical reaction?
Enzymes are least effective when conditions are optimal.
Enzymes are least effective when conditions are optimal.
False
What is formed during the catalytic event of an enzyme action?
What is formed during the catalytic event of an enzyme action?
Enzyme-substrate complex
Enzymes reduce the energy needed to initiate __________ reactions.
Enzymes reduce the energy needed to initiate __________ reactions.
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Match the following enzymes with their types:
Match the following enzymes with their types:
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What is the primary function of enzymes?
What is the primary function of enzymes?
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Enzymes are consumed during the reactions they catalyze.
Enzymes are consumed during the reactions they catalyze.
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What is the term used to describe the region of the enzyme where the substrate binds?
What is the term used to describe the region of the enzyme where the substrate binds?
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Enzymes exhibit __________ specificity, meaning they catalyze a single reaction or closely related reactions.
Enzymes exhibit __________ specificity, meaning they catalyze a single reaction or closely related reactions.
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Match the enzyme to its feature:
Match the enzyme to its feature:
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Which of the following statements about enzyme activity conditions is true?
Which of the following statements about enzyme activity conditions is true?
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The active site of an enzyme is always a large region of the enzyme.
The active site of an enzyme is always a large region of the enzyme.
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What phenomenon refers to the ability of the enzyme to preferentially bind one molecule over others?
What phenomenon refers to the ability of the enzyme to preferentially bind one molecule over others?
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What does the Michaelis-Menten constant (KM) indicate?
What does the Michaelis-Menten constant (KM) indicate?
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What is the role of prosthetic groups?
What is the role of prosthetic groups?
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A high KM value suggests a strong binding between substrate and enzyme.
A high KM value suggests a strong binding between substrate and enzyme.
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Apoenzyme is the active form of an enzyme.
Apoenzyme is the active form of an enzyme.
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What happens to the rate of catalysis as substrate concentration ([S]) increases?
What happens to the rate of catalysis as substrate concentration ([S]) increases?
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What term is used for an enzyme combined with its cofactor?
What term is used for an enzyme combined with its cofactor?
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At ___________, enzyme molecules are almost all occupied.
At ___________, enzyme molecules are almost all occupied.
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Match the types of enzymes with their definitions:
Match the types of enzymes with their definitions:
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Succinate dehydrogenase requires _____ as a cofactor.
Succinate dehydrogenase requires _____ as a cofactor.
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Which of these enzymes is classified as a Transferase?
Which of these enzymes is classified as a Transferase?
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Which of the following describes Michaelis-Menten kinetics?
Which of the following describes Michaelis-Menten kinetics?
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Allosteric enzymes obey Michaelis-Menten kinetics.
Allosteric enzymes obey Michaelis-Menten kinetics.
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An increase in substrate concentration always leads to a linear increase in the reaction rate.
An increase in substrate concentration always leads to a linear increase in the reaction rate.
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What is the primary role of coenzymes?
What is the primary role of coenzymes?
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What type of reaction do oxidoreductases catalyze?
What type of reaction do oxidoreductases catalyze?
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Lyases catalyze reactions involving the _____ or removal of groups.
Lyases catalyze reactions involving the _____ or removal of groups.
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The reaction mechanism involves the formation of an ____________ complex.
The reaction mechanism involves the formation of an ____________ complex.
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Match the enzyme classifications with their examples:
Match the enzyme classifications with their examples:
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What does Vmax represent in enzyme kinetics?
What does Vmax represent in enzyme kinetics?
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Michaelis-Menten kinetics can be applied to enzymes that do not follow a hyperbolic saturation curve.
Michaelis-Menten kinetics can be applied to enzymes that do not follow a hyperbolic saturation curve.
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What is a common feature of allosteric enzymes?
What is a common feature of allosteric enzymes?
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Cofactors can only be organic compounds.
Cofactors can only be organic compounds.
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What is the main difference between simple enzymes and holoenzymes?
What is the main difference between simple enzymes and holoenzymes?
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What is the primary function of ligases?
What is the primary function of ligases?
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KM is a measure of the __________ of the enzyme-substrate complex.
KM is a measure of the __________ of the enzyme-substrate complex.
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An enzyme's name often ends in _____ to indicate its function.
An enzyme's name often ends in _____ to indicate its function.
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Match the following terms with their definitions:
Match the following terms with their definitions:
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What type of reaction do hydrolases catalyze?
What type of reaction do hydrolases catalyze?
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Study Notes
Enzymes Overview
- Enzymes are proteins that act as biological catalysts, accelerating biochemical reactions significantly.
- They exhibit high specificity, catalyzing either a single reaction or closely related reactions.
Properties of Enzymes
- Enzymes are globular proteins with a three-dimensional shape that determines function.
- They lower the activation energy needed for reactions, thus speeding up the process without being consumed.
- Each enzyme has an active site specific to its substrate, where the conversion of substrates to products occurs.
Mechanism of Enzyme Action
- Carbonic anhydrase demonstrates enzyme efficiency, accelerating the reaction from CO2 and H2O to H2CO3 from 0.13 to 1,000,000 molecules per second.
- The active site, a small cluster of amino acids, creates a microenvironment for substrate binding and catalysis.
Enzyme Specificity and Affinity
- Specificity refers to an enzyme's ability to preferentially bind to a specific substrate.
- Affinity measures the strength of the binding interaction between enzyme and substrate.
Enzyme Sensitivity and Optimal Conditions
- Enzymes operate best under optimal conditions regarding temperature, pH, and salt concentration.
- Variability in enzyme sensitivity impacts their effectiveness across different environments.
Catalytic Process
- Enzymes facilitate the formation of a transition state through the formation of an enzyme-substrate complex (ES).
- They change the reaction rate but not the reaction itself.
Enzyme Kinetics
- Michaelis-Menten kinetics studies the relationship between substrate concentration and reaction velocity (V0).
- Vmax indicates the maximum reaction rate achieved by an enzyme at saturation point when most active sites are occupied.
- The Michaelis-Menten constant (KM) defines substrate concentration required for half-maximal velocity, indicating binding strength.
Enzymes and Cofactors
- Many enzymes, known as holoenzymes, require cofactors for activity.
- Cofactors can be organic (coenzymes like vitamins) or inorganic (metal ions such as Zn2+).
- Apoenzymes refer to the inactive protein portion of an enzyme without its cofactor.
Allosteric Regulation
- Allosteric enzymes possess multiple binding sites; substrate binding can influence the activity of other sites.
- They do not follow simple Michaelis-Menten kinetics and often exhibit a sigmoidal reaction rate curve.
Classification of Enzymes
- Enzymes are classified based on the reaction type they catalyze and commonly end in "ase."
- Major classes include:
- Oxidoreductases: Involved in oxidation-reduction reactions (e.g., alcohol dehydrogenase).
- Transferases: Transfer functional groups between molecules (e.g., glycerokinase).
- Isomerases: Rearrange functional groups within a molecule (e.g., maleate isomerase).
- Hydrolases: Catalyze hydrolytic cleavage (e.g., carboxypeptidase A).
- Lyases: Add or remove groups form molecules (e.g., pyruvate decarboxylase).
- Ligases: Join two molecules together (e.g., pyruvate carboxylase).
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Description
This quiz covers the specificity and binding affinities of enzymes, focusing on endopeptidases and exopeptidases. Test your knowledge on the structure and function of various enzymes, including pepsin, chymotrypsin, and trypsin. Gain a deeper understanding of enzyme kinetics and peptide bonds.
