Podcast
Questions and Answers
What happens to the rate of enzyme action when enzyme concentration increases?
What happens to the rate of enzyme action when enzyme concentration increases?
- It decreases when substrate is in low concentration.
- It is proportional to enzyme concentration under constant conditions. (correct)
- It remains constant regardless of substrate concentration.
- It always reaches Vmax immediately.
What is the significance of Vmax in enzyme kinetics?
What is the significance of Vmax in enzyme kinetics?
- It indicates the maximum concentration of substrate.
- It means that all enzyme sites are vacant.
- It is the substrate concentration at which all enzymes are inactive.
- It represents the maximum rate of reaction achievable. (correct)
Which enzyme has a high affinity for its substrate based on its Km value?
Which enzyme has a high affinity for its substrate based on its Km value?
- Neither has a significant affinity.
- Glucokinase
- Both have the same affinity.
- Hexokinase (correct)
What does a higher Km value indicate about an enzyme?
What does a higher Km value indicate about an enzyme?
Which factor does NOT affect the rate of enzyme action?
Which factor does NOT affect the rate of enzyme action?
What happens to the reaction rate if substrate concentration increases beyond Vmax?
What happens to the reaction rate if substrate concentration increases beyond Vmax?
Which enzyme is characterized by functioning effectively at high substrate concentrations?
Which enzyme is characterized by functioning effectively at high substrate concentrations?
What role do coenzymes play in enzyme activity?
What role do coenzymes play in enzyme activity?
What happens to the rate of enzyme reaction as temperature increases until it reaches the optimum temperature?
What happens to the rate of enzyme reaction as temperature increases until it reaches the optimum temperature?
What is the optimum temperature range for enzyme activity as mentioned?
What is the optimum temperature range for enzyme activity as mentioned?
What effect does the concentration of coenzymes have on the rate of reaction?
What effect does the concentration of coenzymes have on the rate of reaction?
What is the optimum pH range for pepsin activity?
What is the optimum pH range for pepsin activity?
What is one of the reasons that a change in pH affects the rate of enzyme action?
What is one of the reasons that a change in pH affects the rate of enzyme action?
What type of enzyme inhibitor decreases enzyme activity by competing with the substrate for the active site?
What type of enzyme inhibitor decreases enzyme activity by competing with the substrate for the active site?
Which ion activates the enzyme salivary amylase, facilitating carbohydrate digestion?
Which ion activates the enzyme salivary amylase, facilitating carbohydrate digestion?
What consequence does prolonged reaction time have on enzyme activity?
What consequence does prolonged reaction time have on enzyme activity?
What characterizes an enzyme with a low Km value?
What characterizes an enzyme with a low Km value?
Which factor does NOT influence the enzyme reaction rate according to enzyme kinetics?
Which factor does NOT influence the enzyme reaction rate according to enzyme kinetics?
At what point does adding more substrate concentration have no effect on the enzyme reaction rate?
At what point does adding more substrate concentration have no effect on the enzyme reaction rate?
Which enzyme is likely to function effectively at low glucose concentrations?
Which enzyme is likely to function effectively at low glucose concentrations?
What is the relationship between substrate concentration and reaction rate up to Vmax?
What is the relationship between substrate concentration and reaction rate up to Vmax?
Which statement about the effect of temperature on enzyme activity is true?
Which statement about the effect of temperature on enzyme activity is true?
What defines the Michaelis constant (Km) in enzyme kinetics?
What defines the Michaelis constant (Km) in enzyme kinetics?
What effect do inhibitors have on enzyme activity?
What effect do inhibitors have on enzyme activity?
How does temperature affect enzyme activity beyond the optimum range?
How does temperature affect enzyme activity beyond the optimum range?
What is the primary reason a change in pH impacts enzyme activity?
What is the primary reason a change in pH impacts enzyme activity?
What defines the effect of time on enzyme activity?
What defines the effect of time on enzyme activity?
Which ion is known to activate thrombokinase enzyme?
Which ion is known to activate thrombokinase enzyme?
What is the impact of a competitive inhibitor on enzyme function?
What is the impact of a competitive inhibitor on enzyme function?
What is the optimal pH for pancreatic lipase activity?
What is the optimal pH for pancreatic lipase activity?
What happens to the rate of reaction as enzyme concentration increases?
What happens to the rate of reaction as enzyme concentration increases?
How does the presence of non-competitive inhibitors affect enzyme function?
How does the presence of non-competitive inhibitors affect enzyme function?
Flashcards
Enzyme concentration
Enzyme concentration
The amount of enzyme present affects the reaction rate, directly proportional to the enzyme concentration, provided substrate and conditions are constant.
Substrate concentration
Substrate concentration
Increasing substrate concentration speeds up the reaction up to a point where the reaction rate hits its maximum (Vmax).
Vmax
Vmax
The maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate.
Michaelis constant (Km)
Michaelis constant (Km)
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Low Km enzyme
Low Km enzyme
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High Km enzyme
High Km enzyme
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Coenzyme/ion activators/ inhibitors
Coenzyme/ion activators/ inhibitors
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Enzyme
Enzyme
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Enzyme's optimum temperature
Enzyme's optimum temperature
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Enzyme denaturation
Enzyme denaturation
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Enzyme's effect of temperature
Enzyme's effect of temperature
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Optimum pH for enzyme activity
Optimum pH for enzyme activity
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Enzyme denaturation by pH changes
Enzyme denaturation by pH changes
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Enzyme inhibitors
Enzyme inhibitors
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Competitive inhibitor
Competitive inhibitor
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Non-competitive inhibitor
Non-competitive inhibitor
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What factors influence enzyme activity?
What factors influence enzyme activity?
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What happens when enzyme concentration increases?
What happens when enzyme concentration increases?
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What is saturation with substrate?
What is saturation with substrate?
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What is the Michaelis constant (Km)?
What is the Michaelis constant (Km)?
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High Km vs. Low Km
High Km vs. Low Km
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Coenzyme effect
Coenzyme effect
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Optimum temperature & pH
Optimum temperature & pH
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Enzyme's Ideal Temperature
Enzyme's Ideal Temperature
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Enzyme & Temperature
Enzyme & Temperature
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Optimum pH
Optimum pH
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PH & Enzyme Function
PH & Enzyme Function
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Study Notes
Enzyme Action Factors
- Enzyme concentration is directly proportional to reaction rate, if substrate is present.
- Substrate concentration increases reaction rate to a maximum (Vmax). Further substrate increase doesn't affect the rate.
- Coenzymes' concentration increase reaction rate.
- Metal ion activators increase reaction rate.
- Time affects reaction rate by decreasing substrate concentration and accumulating products.
Temperature
- Reaction rate increases with temperature to a maximum, then decreases due to denaturation.
- Optimum temperature for enzymes is ~37-40°C.
- Reactions decrease in rate above 60-65°C.
- Temperature affects reaction rate by increasing kinetic energy of the substrate or collision frequency.
pH
- Each enzyme has an optimal pH, at which maximal activity occurs.
- Pepsin (acidic environment, pH 1.5-2)
- Pancreatic lipase (alkaline environment, pH 7.5-8)
- Salivary amylase (slightly acidic environment, pH 6.8)
- pH change affects enzyme or substrate ionization, and significant changes lead to denaturation.
Michaelis Constant (Km)
- Substrate concentration yielding half of the maximum velocity (Vmax).
- Low Km signifies high affinity to the substrate.
- High Km signifies low affinity to the substrate.
- Hexokinase (low Km/high affinity for substrate)
- Glucokinase (high Km/low affinity for substrate)
Enzyme Inhibitors
- Inhibitors decrease or stop enzyme activity.
- Competitive inhibitors compete with the substrate for the active site.
- Non-competitive inhibitors bind to the enzyme at a site other than the active site, changing the enzyme's shape.
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