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Enzyme Kinetics
Jul 23, 2024
Enzyme Kinetics Lecture
Introduction
Kinetics:
Study of reaction rates or speeds.
Enzyme Kinetics:
Understanding the rate of reactions involving enzymes.
Focus is on several key concepts/terms:
Michaelis-Menten Equation
Graphical representations (Michaelis-Menten plot, Lineweaver-Burk plot)
Types of inhibition (competitive, non-competitive, uncompetitive, suicide inhibition)
Michaelis-Menten Equation
Reaction and Derivation
Essential reaction: Enzyme (E) + Substrate (S) → Enzyme-Substrate Complex (ES) → Product (P) + Enzyme (E)
Rates:
K1: Formation of ES
K-1: Dissociation into E + S
K2: Dissociation into E + P
K-2: Negligibly small, considered unidirectional reaction
Steady State Assumption
Formation rate of ES = Dissociation rate of ES
Graphical representation:
Enzyme + Substrate concentration decreases over time
Enzyme + Product concentration increases over time
Point where ES concentration remains constant
Mathematical Derivation
Set equal rates: K1 [E][S] = K-1 [ES] + K2 [ES]
Total enzyme concentration: E_total = [ES] + [E]
Solve for [E]: [E] = E_total - [ES]
Substitute in the steady state equation.
Simplify using Michaelis constant (Km = (K-1 + K2) / K1)
Derive final Michaelis-Menten Equation: V_0 = (V_max [S]) / (Km + [S])
Key Assumptions
Km (Michaelis constant):
Substrate concentration at half V_max
V_max:
Maximum velocity when enzyme is saturated with substrate
Application of Km
Relationship to enzyme-substrate affinity:
Low Km → High substrate affinity
High Km → Low substrate affinity
Practical examples:
Hexokinase (muscles): Low Km, high affinity
Glucokinase (liver): High Km, low affinity
Summary and Important Concepts
Derivation Steps
: From basic reaction to Michaelis-Menten equation
Steady-state assumption:
Key to understanding reaction rates
Km as an indicator:
Affinity of enzyme for substrate
Next Steps
Future lectures will cover types of enzyme inhibition and graphical methods like Lineweaver-Burk plot.
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