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: Energy of Activation

Practice: Which of the following best describes the energy of activation for a reaction?

Concept #2: Reducing Entropy and Random Motion

Practice: Which of the following best describes catalysis by proximity?

Concept #3: Proper Orientation of Substrates 

Practice: Which of the following statements is false with respect to an enzyme’s ability to catalyze a reaction?

Concept #4: Distortion of Substrate 

Practice: Which of the following is not a way that enzymes increase rates of reactions?

Practice: Binding energy between an enzyme and a substrate contributes to catalysis in which way?

Practice: Enzymes are potent catalysts because they: