2. Go to Enzyme Nomenclature Database (http://www.expasy.ch/enzyme/) Identify an enzyme of interest (for example carbonic anhydrase, fumerase, DNA ligase etc.). List a common name of the enzyme, the classification number, the substrate and product(s), Type of Reaction (group classification; for example, oxidoreductase, hydrolase, transferase, lyase, isomerase, ligase), Systematic name, Cofactors/prosthetic groups

1. Know that most enzymes are PROTEINS (a few are RNA).
2. Know the terms: active site, substrate, cofactor, coenzyme, transition state, free energy of reaction (D G) vs. free energy of activation (D G^‡),haloenzyme, apoenzyme, stereospecificity, geometric specificity.
3. Know the role of cofactors and coenzymes in enzyme catalyzed reactions and that cofactors and coenzymes come from vitamins and trace minerals.
4. Be able to draw a transition state diagram for a uncatalyzed and enzyme catalyzed reaction.
5. Know that enzymes increase the rate of reaction by lowering D G^‡. Spontaneity of reaction depends on D G.
6. Know the six classes of enzymes (oxidoreductase, hydrolase, transferase, lyase, isomerase, ligase).
7. Serine proteases are a class of proteases that share a common mechanism involving a highly active serine residue. Many zymogens are cleaved by serine proteases to yield active enzymes. These include trypsinogen, prelastase and thrombin.
8. Drugs (sarin) and endogenous protease inhibitors (BPTI) are transition state analogues. Understanding catalytic mechanisms aid in design of enzyme inhibitors.