1. Analyze an enzyme catalyzed reac8on using the Michaelis-Menten equa8on
and calculate relevant parameters (KM , kcat, etc.).
2. Recognize the similari8es between a binding isotherm and a plot of the ini8al
velocity (ν 0) vs. [S] for an enzyme catalyzed reac8on.
3. Iden8fy the rate-determining step in a reac8on scheme.
4. Define what a “perfect” enzyme would be.
5. Demonstrate how the different rate constants in an enzyma8c scheme relate to enzyme efficiency and ul8mately substrate specificity.
