Podcast
Questions and Answers
Enzymes are ______ which reduce the needed activation energy.
Enzymes are ______ which reduce the needed activation energy.
catalysts
A graph of product concentration vs. time follows three phases, including an early increase, a ______ increase, and a leveling off.
A graph of product concentration vs. time follows three phases, including an early increase, a ______ increase, and a leveling off.
linear
The classic model of enzyme action is known as the ______ model.
The classic model of enzyme action is known as the ______ model.
Michaelis-Menten
Enzyme velocity often follows the - equation.
Enzyme velocity often follows the - equation.
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The variable $K_M$ represents the ______ constant in enzyme kinetics.
The variable $K_M$ represents the ______ constant in enzyme kinetics.
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$E + S
ightleftharpoons ______
ightarrow E + P$ describes the steps in enzyme action.
$E + S ightleftharpoons ______ ightarrow E + P$ describes the steps in enzyme action.
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Special techniques are needed to study early kinetics, as this transient phase usually lasts less than a ______.
Special techniques are needed to study early kinetics, as this transient phase usually lasts less than a ______.
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When substrate is depleted, the concentration of product reaches a ______.
When substrate is depleted, the concentration of product reaches a ______.
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The rate of ES formation equals the rate of ES ______.
The rate of ES formation equals the rate of ES ______.
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Assuming the concentration of ES is steady, the equation can be rewritten as k_1[S]([E_{total}] - [ES]) = k_{-1}[ES] + k_2[ES], where [E_{total}] equals ES plus ______.
Assuming the concentration of ES is steady, the equation can be rewritten as k_1[S]([E_{total}] - [ES]) = k_{-1}[ES] + k_2[ES], where [E_{total}] equals ES plus ______.
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The velocity of the enzyme reaction is represented as Velocity = k_2[ES] = k_2\frac{[E_{total}][S]}{[S] + ______}.
The velocity of the enzyme reaction is represented as Velocity = k_2[ES] = k_2\frac{[E_{total}][S]}{[S] + ______}.
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The maximum velocity, V_{max}, occurs at maximal concentrations of ______.
The maximum velocity, V_{max}, occurs at maximal concentrations of ______.
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K_M is defined as (k_{-1} + k_2)/k_______.
K_M is defined as (k_{-1} + k_2)/k_______.
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The Briggs-Haldane model is more useful because it considers a ______ of all five rate constants.
The Briggs-Haldane model is more useful because it considers a ______ of all five rate constants.
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Standard analyses of enzyme kinetics assume that the concentration of enzyme remains ______ during the time intervals used.
Standard analyses of enzyme kinetics assume that the concentration of enzyme remains ______ during the time intervals used.
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Data must be collected during the ______ part of the graph where the reaction is linear with time.
Data must be collected during the ______ part of the graph where the reaction is linear with time.
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Study Notes
Enzyme Kinetics
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Enzymes are biological catalysts, accelerating reactions by lowering activation energy
-
Product accumulation follows a three-phase pattern
- Initial rapid increase in product concentration
- Linear increase in product concentration
- Leveling off as substrate is depleted
-
Enzyme velocity is the rate of product formation. Measured as product formed per unit time
-
Enzyme velocity is dependent on substrate concentration
-
Michaelis-Menten equation describes relationship between enzyme velocity and substrate concentration:
V₀ = (Vmax[S]) / (Km + [S])Where: - V₀ = initial velocity of the reaction - Vmax = maximum velocity of the reaction - [S] = substrate concentration - Km = Michaelis constant
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Vmax is the maximum velocity of the enzyme-catalyzed reaction, reached when the enzyme is saturated with substrate. It has units of product formed per time
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Km is the substrate concentration at which the reaction velocity is half of Vmax; it reflects the enzyme's affinity for the substrate. Units are concentration
-
Km is not a binding constant, also includes reaction rate
Types of Inhibition
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Competitive Inhibition:
- Inhibitor resembles substrate and binds to active site, preventing substrate binding.
- Km increases; Vmax unchanged
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Uncompetitive Inhibition:
- Inhibitor binds only to the enzyme-substrate complex, preventing product release.
- Km decreases; Vmax decreases
-
Noncompetitive (Mixed) Inhibition:
- Inhibitor binds to the enzyme at a site other than the active site, changing the enzyme's conformation.
- Km unchanged; Vmax decreases
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Description
This quiz covers the fundamental concepts of enzyme kinetics, including the role of enzymes as biological catalysts and the phases of product accumulation. It also delves into the Michaelis-Menten equation and the important parameters such as Vmax and Km. Test your understanding of how these factors influence enzyme activity and reaction rates.
