Enzyme-Substrate Complex
Lock and Key Vs. Induced Fit Models
Optimal Enzyme Conditions
Activation Energy
Types of Enzymes
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
Specificity Constant

Concept #1: Theoretical Maximum Reaction Velocity (Vmax)

Practice: In a Michaelis-Menten kinetics plot (V0 vs. [S]), what is the reason that the curve reaches a plateau and V0 cannot increase any further upon adding more substrate?

Concept #2: Vmax can be Expressed with a Rate Law

Concept #3: Vmax is Affected by [E]T

Practice: Vmax for an enzyme-catalyzed reaction:

Practice: What kind of kinetics is observed initially in an enzymatic reaction under conditions where [S] is saturating?