Enzyme catalysis

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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.

Aims[edit]

By the end of this lesson, you should

  1. be familiar with the Michaelis-Menten model
  2. understand the steady state kinetic parameters
  3. understand the types of enzyme inhibition
  4. understand the four strategies used by enzymes in catalysis
  5. understand the molecular basis for proximity effects and intramolecular catalysis
  6. know examples of amino acid residues which could participate in acid/base and covalent catalysis

Theory[edit]

Kinetic model[edit]

Strategies for catalysis[edit]

Important functions