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Questions and Answers
What is the primary mechanism by which allosteric modulators regulate enzyme activity?
What is the primary mechanism by which allosteric modulators regulate enzyme activity?
- Direct interaction with the substrate
- Non-covalent binding to the active site
- Non-covalent binding to a site distinct from the active site (correct)
- Covalent modification of amino acid residues
Which of the following is an example of a reversible covalent modification that regulates enzyme activity?
Which of the following is an example of a reversible covalent modification that regulates enzyme activity?
- Coenzyme binding
- Allosteric activation
- Substrate binding
- Phosphorylation (correct)
What is the protein portion of an enzyme called?
What is the protein portion of an enzyme called?
- Cofactor
- Apoenzyme (correct)
- Coenzyme
- Prosthetic group
Which of these molecules serves as a coenzyme in electron transfer reactions?
Which of these molecules serves as a coenzyme in electron transfer reactions?
Which of the following is a characteristic feature of allosteric regulation?
Which of the following is a characteristic feature of allosteric regulation?
What is the primary role of an enzyme in a chemical reaction?
What is the primary role of an enzyme in a chemical reaction?
What is the specific region on an enzyme that binds to the substrate molecule called?
What is the specific region on an enzyme that binds to the substrate molecule called?
What is the key characteristic that enzymes possess, allowing them to specifically bind and catalyze only one type of substrate?
What is the key characteristic that enzymes possess, allowing them to specifically bind and catalyze only one type of substrate?
What is the primary reason that enzymatic reactions occur much faster than non-enzymatic reactions under mild conditions?
What is the primary reason that enzymatic reactions occur much faster than non-enzymatic reactions under mild conditions?
Why do enzymes have such a significant impact on the rate of chemical reactions within living organisms?
Why do enzymes have such a significant impact on the rate of chemical reactions within living organisms?
Which of the following statements accurately describes the mechanism of enzyme action?
Which of the following statements accurately describes the mechanism of enzyme action?
How do variations in the active site of an enzyme affect its catalytic activity?
How do variations in the active site of an enzyme affect its catalytic activity?
Which of the following statements best describes the role of water-soluble vitamins in enzyme function?
Which of the following statements best describes the role of water-soluble vitamins in enzyme function?
What is the relationship between the rate of a reaction and the substrate concentration?
What is the relationship between the rate of a reaction and the substrate concentration?
What is the term for the maximum rate of a reaction when the enzyme is saturated with substrate?
What is the term for the maximum rate of a reaction when the enzyme is saturated with substrate?
What is the effect of increasing enzyme concentration on the reaction rate?
What is the effect of increasing enzyme concentration on the reaction rate?
Which of the following factors does NOT directly affect the rate of an enzymatic reaction?
Which of the following factors does NOT directly affect the rate of an enzymatic reaction?
What is the significance of a regulatory enzyme in a metabolic pathway?
What is the significance of a regulatory enzyme in a metabolic pathway?
What is the definition of a metabolic pathway?
What is the definition of a metabolic pathway?
How do regulatory enzymes affect the rate of a metabolic pathway?
How do regulatory enzymes affect the rate of a metabolic pathway?
What is the relationship between the Vmax and the Michaelis constant (Km) of an enzyme?
What is the relationship between the Vmax and the Michaelis constant (Km) of an enzyme?
Flashcards
Enzyme
Enzyme
A protein that catalyzes a specific chemical reaction.
Active Site
Active Site
The part of an enzyme that binds to the substrate and catalyzes the reaction.
Substrate Specificity
Substrate Specificity
Enzymes can bind only one specific substrate.
Reaction Rate
Reaction Rate
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Activation Energy
Activation Energy
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Enzyme-Substrate Complex
Enzyme-Substrate Complex
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Transition State
Transition State
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Enzyme Regulation
Enzyme Regulation
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Allosteric enzyme
Allosteric enzyme
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Allosteric site
Allosteric site
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Reversible covalent modification
Reversible covalent modification
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Apoenzyme
Apoenzyme
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Coenzymes
Coenzymes
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Enzymatic Kinetics
Enzymatic Kinetics
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V0
V0
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Substrate Concentration
Substrate Concentration
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Maximum Velocity (Vmax)
Maximum Velocity (Vmax)
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Optimal pH
Optimal pH
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Metabolic Pathway
Metabolic Pathway
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Regulatory Enzyme
Regulatory Enzyme
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External Factors
External Factors
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Study Notes
Enzymology
- Enzymology is the study of enzymes
- Enzymes are crucial for biological reactions
- Water-soluble vitamins act as coenzymes
- Enzyme activity is regulated
Structure of Enzymes
- Enzymes are proteins that catalyze specific chemical reactions
- Active site: the region of an enzyme that binds to a substrate
- Catalytic activity depends on the enzyme's conformation
- Amino acid residues within the active site bind and transform substrates
- Enzymes increase the speed of chemical reactions
Enzymes Properties
- High specificity: Enzymes bind only one specific substrate
- Enzymes always catalyze the exact same reaction
- Enzymes are efficient, proximity creates tension between substrate and catalytic residues
- Enzymatic reactions occur in specialized pockets called active sites
- Enzymes activity can be regulated by altering the active site
How do Enzymes Work?
- Enzymes lower the activation energy needed to start a chemical reaction
- Enzymes facilitate reactions by forming an enzyme-substrate complex
- Enzymes provide a more favorable environment for reaction to occur
- Enzyme activity is modulated to control reaction rate
Enzymatic Kinetics
- The study of reaction rates and how they change with external factors
- The reaction rate is dependent on product concentration and time
- Substrate concentration affects the rate of enzyme reaction
- Change in Enzyme concentration
- pH affects enzyme activity
- Temperature affects enzyme activity
Metabolic Pathway
- Metabolic pathways are sequences of enzymatic reactions
- Each pathway includes several enzymes
- Regulatory enzymes have a significant influence on the overall rate of the pathway
- Regulatory enzymes change in catalytic activity via allosteric or covalent modification
Regulators of Enzyme Activity
- Allosteric regulation: Enzymes are modulated by binding to a specific site other than the active site
- Allosteric inhibitors: Molecules that bind to the allosteric site to inhibit enzyme activity
- Allosteric activators: Molecules that bind to the allosteric site to increase enzyme activity
- Reversible covalent modification: Enzyme activity is altered by adding or removing phosphate groups
- Phosphorylation: The most common type of reversible covalent modification
Coenzymes
- Coenzymes are non-protein molecules that help enzymes function effectively.
- Coenzymes may be inorganic ions or organic/metalloorganic molecules
- Some coenzymes are vitamins (like vitamin B)
- Some coenzymes are derived from vitamins
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