Ch. 6 - Enzymes and Enzyme KineticsWorksheetSee all chapters
All Chapters
Ch. 1 - Introduction to Biochemistry
Ch. 2 - Water
Ch. 3 - Amino Acids
Ch. 4 - Protein Structure
Ch. 5 - Protein Techniques
Ch. 6 - Enzymes and Enzyme Kinetics
Clutch Review 1: Enzymes: Binding, Kinetics & Inhibition
Clutch Review 2: Nucleic Acids, Lipids, & Membranes
Clutch Review 3: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway
Clutch Review 4: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism
Clutch Review 5: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation
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
Learn
Next SectionKcat

Concept #1: Calculating Km with Algebra  

Concept #2: Calculating Km with Reaction Rates 

Example #1: The following rate constants were measured for a simple enzyme-catalyzed reaction. Determine the Km.

Practice: To determine the Km from a Lineweaver-Burk plot you would:

Practice: The Vmax for an enzyme is 9 mg/min. Calculate the Km if the [S] = 5 mM when the V0 = 3 mg/min.

Practice: Calculate the Km of an enzyme using Michaelis-Menten kinetics if the forward rate constant for ES formation is 4.3 x 106 M-1s-1, the reverse rate constant for ES dissociation into E + S is 2.4 x 102 s-1, and the forward rate constant for ES dissociation into E + P is 1.2 x 10 3 s-1.

Previous SectionCalculating Vmax
Next SectionKcat