Instability of the negative charge on the substrate carbonyl oxygen leads to collapse of the tetrahedral intermediate; re-formation of a double bond with carbon displaces the bond between carbon and the amino group of the peptide linkage, breaking the peptide bond. The amino leaving ,Hisc„ group is protonated by

His57, facilitating its displacement.



MECHANISM FIGURE 6-21 Hydrolytic cleavage of a peptide bond by chymotrypsin. The reaction has two phases. In the acylation phase (steps d to ©), formation of a covalent acyl-enzyme intermediate is coupled to cleavage of the peptide bond. In the deacylation phase (steps @ to ©), deacylation regenerates the free enzyme; this is essentially the reverse of the acylation phase, with water mirroring, in reverse, the role of the amine component of the substrate. ^ Chymo-trypsin Mechanism

Short-lived intermediate


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