Enzymes & Enzyme Kinetics
A 25-module path through enzymes & enzyme kinetics, in study order from foundations to the frontier.
Modules
- Enzymes as Biological Catalysts
- Free-Energy Diagrams and the Transition State
- Enzyme Specificity and the Active Site
- Lock-and-Key vs Induced Fit
- Transition-State Stabilization
- Catalysis by Enzymes: Binding Energy
- Catalytic Mechanisms Overview
- Acid-Base and Covalent Catalysis
- Metal-Ion and Proximity Catalysis
- Cofactors, Coenzymes, and Metal Ions
- Common Coenzymes and Their Chemistry
- The Michaelis-Menten Model
- Deriving the Michaelis-Menten Equation
- The Meaning of Km and Vmax
- kcat, Catalytic Efficiency, and kcat/Km
- Lineweaver-Burk and Linearized Plots
- Enzyme Inhibition Overview
- Competitive Inhibition
- Uncompetitive Inhibition
- Noncompetitive and Mixed Inhibition
- Diagnosing Inhibition from Kinetic Plots
- Allosteric Enzymes and Sigmoidal Kinetics
- Regulation of Enzyme Activity: Covalent Modification and Zymogens
- The Serine Protease Mechanism
- The Lysozyme Mechanism