Sections
Enzymes
Enzyme-Substrate Complex
Lock and Key Vs. Induced Fit Models
Optimal Enzyme Conditions
Activation Energy
Types of Enzymes
Cofactor
Catalysis
Electrostatic and Metal Ion Catalysis
Covalent Catalysis
Reaction Rate
Enzyme Kinetics
Rate Constants and Rate Law
Reaction Orders
Rate Constant Units
Initial Velocity
Vmax Enzyme
Km Enzyme
Steady-State Conditions
Michaelis-Menten Assumptions
Michaelis-Menten Equation
Lineweaver-Burk Plot
Michaelis-Menten vs. Lineweaver-Burk Plots
Shifting Lineweaver-Burk Plots
Calculating Vmax
Calculating Km
Kcat
Specificity Constant

Concept #1: Steady State Conditions

Concept #2: Pre-Steady-State

Concept #3: Steady-State Conditions

Practice: True or false: A reaction system at steady-state must also be at equilibrium.

Concept #4: Km and Michaelis-Menten-Equation are Derived under Steady-State

Practice: The steady state assumption, as applied to enzyme kinetics, implies:

Practice: Draw the curves that show the appropriate relationships between the variables in each of the plots below for a simple enzyme-catalyzed reaction that follows Michaelis-Menten kinetics.