Here is a good example of transition state stabilization using a bacterial glycosidase . Another excellent example that clearly shows how transition state stabilization works is found in the structure of this transferase . Serine proteases Serine proteases are endoproteases that cleave internal peptide bonds in proteins. Transition state stabilization. Covalent catalysis, involving a catalytic triad of Asp, His and Ser in the active site.
All serine proteases follow the same mechanism.
Their specificity is determined by the nature of the specificity pocket. In the trypsin specificity pocket, the basic residue of the substrate interacts with an Asp at the bottom of the pocket. Divergent Evolution of Enzymes - Substrate specificity of pancreatic serine proteases. The serine proteases all have the same substrate, a polypeptide chain. Different enzymes cleave the chain adjacent to different amino acids.