1. Review enzyme nomenclature/classification with regards to systematic name and the different types of reactions that can be catalyzed.
2. Define the following terms with regard to enzymes: turnover number, international unit (IU), steady-state, flux, key-lock theory, induced-fit theory, cooperativity, feed-back regulation, feed- forward regulation, product inhibition.
3. Compare and contrast (using a reaction profile diagram), the characteristics of enzymatic and nonenzymatic reactions from the viewpoint of free energy, equilibrium and kinetics.
4. Discuss the structure and composition of enzymes, including the role of coenzymes, cofactors, prosthetic groups. In the process, also define the terms: zymogen/proenzyme, apoenzyme, holoenzyme, isozyme, active/catalytic site, regulatory/allosteric site.
6. Describe enzyme kinetics based on the Michaelis-Menton equation with particular regard to the relationship between Km and Vmax.
7. Estimate changes in v or v/Vmax when provided with changes in the Km or substrate concentration.
8. Differentiate between the following types of inhibitors: transition state, competitive, noncompetitive, reversible, irreversible and suicide. Provide an example of a transition state
inhibitor and a competitive inhibitor. Understand how different types of inhibitors affect Vmax and/or Km.
9. Interpret a Lineweaver-Burke plot to determine the type of inhibitor affecting a given reaction.
10. Understand how enzyme activity can be regulated by covalent modification, proteolytic activation, allosteric regulation and positive or negative cooperativity.
12. List examples of enzymes that are frequently measured in clinical assays and how changes in serum levels of specific enzymes are used for diagnosis.