BIOC 2580 Study Guide - Midterm Guide: Linear Map, Celecoxib, Stoichiometry

• School: University of Guelph
• Department: Biochemistry
• Course: BIOC 2580
• Professor: Enoka Wijekoon

Document Summary

Hydrolysis of peptide bonds by chymotrypsin chain upstream of the target amino acid: chymotrypsin binds weakly to peptide, the targetted amino acid (phe, tyr or, how does chymotrypsin catalyze. Trp) fits into the binding pocket, so substrate binds more tightly. H2o acts as a nucleophile, lone pair donates to electron deficient c upper o to take back a bond. Neutral o is not a good nucleophile. C maintains 8 valence electrons by allowing. This leads to the oxyanion transition state. It tends to hold onto its own electrons. Note that c is now sp3 tetrahedral. Oxyanion o returns the bond to c. Carboxylate c must give up a bond to maintain. Transition state may break down with n as. If n takes back the excess electrons, the peptide bond breaks leaving group. 40 reactions per second for chymotrypsin; 1 reaction in 10 years for h2o.