Podcast
Questions and Answers
What is the term for the catalytically active form of an enzyme?
What is the term for the catalytically active form of an enzyme?
- Cofactor
- Apoenzyme
- Substrate
- Holoenzyme (correct)
Which factor does not affect enzyme activity?
Which factor does not affect enzyme activity?
- Enzyme concentration
- Substrate shape (correct)
- Temperature
- pH
What is the unit of activity for an enzyme?
What is the unit of activity for an enzyme?
- 1 mmol substrate converted in 1 minute
- 1 µmol substrate converted in 1 hour
- 1 µmol substrate converted in 1 minute (correct)
- 1 nmol substrate converted in 1 minute
What does the Km value indicate in enzyme kinetics?
What does the Km value indicate in enzyme kinetics?
What defines the optimum temperature for an enzyme?
What defines the optimum temperature for an enzyme?
What type of inhibitor permanently alters enzyme activity?
What type of inhibitor permanently alters enzyme activity?
Enzymes in humans typically show maximum activity at what temperature range?
Enzymes in humans typically show maximum activity at what temperature range?
Which statement is true regarding enzyme concentration?
Which statement is true regarding enzyme concentration?
What is the primary role of enzymes in biochemical reactions?
What is the primary role of enzymes in biochemical reactions?
Which type of enzyme is responsible for catalyzing oxidation-reduction reactions?
Which type of enzyme is responsible for catalyzing oxidation-reduction reactions?
Which statement accurately describes the efficiency of enzyme-catalyzed reactions?
Which statement accurately describes the efficiency of enzyme-catalyzed reactions?
What distinguishes enzymes in terms of specificity?
What distinguishes enzymes in terms of specificity?
What is the relationship between enzyme activity and the Michaelis constant (Km)?
What is the relationship between enzyme activity and the Michaelis constant (Km)?
Which of the following is NOT a classification of enzymes?
Which of the following is NOT a classification of enzymes?
Which of the following characteristics is true for all enzymes?
Which of the following characteristics is true for all enzymes?
What defines a catalyst in the context of enzymatic reactions?
What defines a catalyst in the context of enzymatic reactions?
Flashcards
Apoenzyme
Apoenzyme
The protein part of an enzyme.
Cofactor
Cofactor
The non-protein component of an enzyme that aids in catalytic activity.
Holoenzyme
Holoenzyme
The fully functional, catalytically active form of an enzyme, composed of both apoenzyme and cofactor.
Active site
Active site
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Enzyme Activity
Enzyme Activity
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Optimum temperature for an enzyme
Optimum temperature for an enzyme
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Optimum pH for an enzyme
Optimum pH for an enzyme
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Inhibitor
Inhibitor
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Enzymes
Enzymes
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Enzyme Composition
Enzyme Composition
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Enzyme Function
Enzyme Function
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Enzyme Specificity
Enzyme Specificity
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Activation Energy and Enzymes
Activation Energy and Enzymes
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Enzyme Classification
Enzyme Classification
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Michaelis-Menten Constant (Km)
Michaelis-Menten Constant (Km)
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Enzyme Inhibition
Enzyme Inhibition
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Study Notes
Enzyme Overview
- Enzymes are biological catalysts
- They increase the rate of biochemical reactions
- They are highly specific for their substrate and reaction type
- Enzymes are not consumed in the reaction
- Most are proteins, some are ribozymes (RNA)
- Lower activation energy by stabilizing the transition state
Learning Objectives for Enzymes
- Describe enzymes and their properties
- List enzyme classifications
- Describe factors affecting enzyme activity
- Explain the relationship between Km and enzyme activity
- Explain enzyme inhibition and different types of inhibition
Metabolic Reactions and Enzymes
- Enzymes facilitate metabolic reactions, including both anabolic (building up) and catabolic (breaking down) pathways
- Enzymes increase the rate of these reactions, which are fundamental to life processes
- Enzymes catalyze reactions by lowering activation energy
- This speeds up reaction rates
- Enzymes can modify molecules by binding temporarily for transport, degradation, or modifications within cells.
- With some special molecules
Glycolysis Overview
- Glycolysis is a metabolic process that breaks down glucose into pyruvate
- Enzymes are crucial to facilitate these reactions (e.g., hexokinase, phosphofructokinase, etc.)
- Each reaction step is catalyzed by specific enzymes
Enzyme Activity
- Enzyme activity is the rate at which an enzyme catalyzes a reaction
- Measured by the amount of substrate converted to product in a given time
- One unit of enzyme activity converts 1 μmol of substrate to product in one minute under optimal conditions
- Enzyme activity is influenced by several factors, including enzyme concentration, substrate concentration, temperature, pH, and inhibitors.
- Enzyme activity can be measured and optimized according to these factors
Factors Affecting Enzyme Activity
- Enzyme concentration: Higher concentration, faster reaction
- Substrate concentration: More substrate, speeds reaction up until saturation
- Temperature: Optimal temperature for max efficiency; high temp, denatures/slows reactions
- pH: Affects enzyme structure and function (optimal pH for every enzyme)
- Inhibitors: Substrates that reduce enzyme rate.
Enzyme Nomenclature
- Enzymes are classified in an organized way
- This is done according to their function (i.e. oxidoreductases, transferases, hydrolases, etc.)
- Each enzyme is given a unique EC number for precise identification
Enzyme Kinetics and Km
- Km reflects the enzyme's affinity for its substrate
- Low Km means higher affinity (higher substrate concentration required to reach half V-max)
- High Km means lower affinity (requires high substrate concentration to get half Vmax)
- Vmax is the maximum reaction rate of an enzyme
Enzyme Regulation
- Factors influencing enzyme activity
- Enzymes can be regulated by changing the amount (synthesis/degradation), enzyme modification (e.g., phosphorylation / dephosphorylation), or the compartments in a cell.
- These factors influence enzyme activity at different stages/steps
Isoenzymes
- Enzymes that share the same catalytic function but have different structures(sequences) and different regulatory properties
- Examples include lactate dehydrogenase and creatine kinase
- Can be used to distinguish between different tissues or cellular conditions
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