This lesson will explain the transition state theory of enzyme catalysis, the Michaelis-Menten model for enzyme kinetics, and the kinetic parameters Km, kcat, and kcat/Km. Scenarios for simple enzyme inhibition will be illustrated. Enzymes employ several strategies for catalysis: proximity effects (illustrated by intramolecular catalysis); acid/base catalysis; covalent catalysis; strain/distortion.
By the end of this lesson, you should
- be familiar with the Michaelis-Menten model
- understand the steady state kinetic parameters
- understand the types of enzyme inhibition
- understand the four strategies used by enzymes in catalysis
- understand the molecular basis for proximity effects and intramolecular catalysis
- know examples of amino acid residues which could participate in acid/base and covalent catalysis