CHEM 271 Lecture Notes - Lecture 6: Serine Protease, Enzyme Catalysis, Aromatic Amino Acids

• School: Concordia University
• Department: Chemistry
• Course: CHEM 271
• Professor: Paul Joyce

Document Summary

Enzyme mechanisms (chapter 9) and regulation (chapter 10) Kinetic analysis lets us know about rates of reaction, but it does not tell us a lot about what is actually happening. Some specific examples: lysozyme catalyzes the cleavage of bacterial cell walls catalysis by approximation, general acid-base catalysis. Role of acid-base interactions can be seen in ph profiles. Shows how kinetics can provide some idea about mechanism!! Do you see this: proteases catalyse hydrolysis of peptide bonds, many different types (at least six different families defined by their catalytic mechanisms) as this process is important; understand proteases and design of protease inhibitors. Peptide bonds are resistant to hydrolysis because of their partial double bond character and relatively unreactive carbonyl group. So although this cleavage is energetically favourable (spontaneous) it is not instantaneous. Multiple families of enzymes have evolved to break these peptide bonds. They recognize and cleave next to specific amino acid residues.