CHEM 3050 Lecture Notes - Lecture 32: Elastase, Chymotrypsin, Trypsin

• School: York University
• Department: Chemistry
• Course: CHEM 3050
• Professor: Paula Wilson

Document Summary

How do enzymes with similar catalytic mechanisms recognize different substrates: may have similar tertiary structures and active site, chymotrypsin, trypsin, elastase: similar structures but different substrate specificities. How are they different: enzymes vary in specificity pocket, vary in amino acids in pockets, controls pocket dimensions, chymotrypsin: specificity pockets fits aromatic ring, trypsin: same pocket dimensions as. Chymotrypsin but different chain at the bottom: asp (-) binds with lys (+) or arg (+) (opposite charges attracts, elastase: specificity pockets fits bulkier groups but the pocket is much smaller, binds small nonpolar side chains. Inactive precursors: zymogens (capable of being generated into active enzymes and the benefit is that it doesn"t require much effort to active them). Autoactivation: ability to active themselves: benefit: no-time is delayed to synthesize (zymogens: fast ready to go) Activity is also controlled by protease inhibitors (remember the lock and key idea)