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

Practice: What is the initial velocity of a reaction when the concentration of substrate is set equal to the Km?

Concept #2: Km Can Be Expressed with Rate Constants

Practice: Select the best description of the K m.

Concept #3: Km Measures an Enzyme’s Affinity for its Substrate

Practice: According to the chart below, which one of the following enzymes has the strongest affinity for its substrate?

Concept #4: [E]T Does Not Affect the Km

Practice: Indicate which region of the Enzyme Kinetics plot below best corresponds to each statement.

A) Initial reaction velocity is limited mainly by the [S] present: ______

B) Initial reaction velocity limited mainly by the [E] present: ______

C) The active site of an enzyme is most likely free/unoccupied: ______

D) The active site of an enzyme is most likely occupied by substrate: ______

E) This region includes the points corresponding to Km & ½Vmax: ______

Practice: Use the data in the following chart to determine the Km of the enzyme.