Name the three essential active site residues of chymotrypsin and describe how each is involved in the catalytic mechanism.

The active site residues include Serine, Histidine and Aspartatic acid

Explanation:

The catalytic triad at the active site of Chymotrypsin includes Ser-105 (Serine), His-57 (Histidine) and Asp-102 (Aspartic acid).

His-57: Deprotonates and polarizes Ser-105 so that it is able to react with substrate.

Asp-102: The carboxyl group of Asp-102 hydrogen bonds with the R-group of the His-57 which facilitates the deprotonation of Ser-105.

Ser-105: The strong nucleophile of serine attacks the substrate leading to hydrolysis.

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