91Ó°ÊÓ

The preferential binding of the transition state (tetrahedral intermediate) over the enzyme-substrate complex/ the acyl-enzyme intermediate is responsible for much of the catalytic efficiency of serine proteases

A catalytic mechanism is based on chemical and structural data formulated and given in chymotrypsin, which is applied to all serine proteases and other hydrolytic enzymes. Much of chymotrypsin’s catalytic power derives from its preferential binding of the transition state; therefore,a catalytic mechanism that contributes the most to rate acceleration is transition state binding catalysis.

For example,mutating any or all of the residues in chymotrypsin’s catalytic triad yields enzymes that still enhance proteolysis by approximately by -fold over the uncatalyzed reaction.