1. Know the mechanism for serine proteases and think about potential amino acid changes to the active site catalytic triad. a. What might still be functional? b. What might slow the kinetics? c. What will cause the enzyme to be inactive? 2. Know the various Michaelis-Menten plots for inhibited and non- inhibited enzymes. a. Why does binding of an inhibitor cause the kinetic effect seen? b. What is the effect of various concentration changes? c. What makes a good inhibitor? 3. Get comfortable with how experimental evidence can support Cor not support) a particular proposed mechanism. 4. Know the ways enzymes are regulated and the effects of various changes (i.e. allosteric effectors, PTMs, isozymes, etc.) 5. For drug-design, be able to evaluate a potential drug based on the mechanism of the enzyme for its effectiveness.