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🥼organic chemistry review

Chymotrypsin

Written by the Fiveable Content Team • Last updated September 2025
Written by the Fiveable Content Team • Last updated September 2025

Definition

Chymotrypsin is a digestive enzyme produced in the pancreas that plays a crucial role in the Edman degradation process for peptide sequencing. It is a serine protease that cleaves peptide bonds on the carboxyl side of aromatic amino acids, such as tyrosine, tryptophan, and phenylalanine.

5 Must Know Facts For Your Next Test

  1. Chymotrypsin is produced in the pancreas and is released into the small intestine, where it helps digest proteins in the diet.
  2. The specificity of chymotrypsin for cleaving peptide bonds on the carboxyl side of aromatic amino acids is crucial for the Edman degradation process.
  3. Chymotrypsin is classified as a serine protease, meaning it uses a serine residue in its active site to catalyze the hydrolysis of peptide bonds.
  4. The Edman degradation technique relies on the selective cleavage of the N-terminal amino acid by chymotrypsin, allowing for the stepwise identification of the amino acid sequence.
  5. The ability of chymotrypsin to cleave peptide bonds at specific sites makes it an essential tool in the field of protein sequencing and structural analysis.

Review Questions

  • Explain the role of chymotrypsin in the Edman degradation process for peptide sequencing.
    • Chymotrypsin is a crucial enzyme in the Edman degradation process, which is used to determine the amino acid sequence of a peptide or protein. Chymotrypsin is a serine protease that selectively cleaves peptide bonds on the carboxyl side of aromatic amino acids, such as tyrosine, tryptophan, and phenylalanine. This specific cleavage pattern allows for the stepwise removal and identification of the N-terminal amino acid, which is the fundamental principle of the Edman degradation technique. By repeatedly applying this process, the complete amino acid sequence of the peptide can be determined.
  • Describe the structural and functional properties of chymotrypsin that make it well-suited for its role in peptide sequencing.
    • Chymotrypsin is classified as a serine protease, meaning it uses a serine residue in its active site to catalyze the hydrolysis of peptide bonds. This specific catalytic mechanism, along with the enzyme's selectivity for cleaving peptide bonds on the carboxyl side of aromatic amino acids, makes chymotrypsin an ideal tool for the Edman degradation process. The ability to selectively cleave peptide bonds at specific sites allows for the stepwise removal and identification of the N-terminal amino acid, which is the foundation of the Edman degradation technique. Additionally, the structural features of chymotrypsin, such as its active site configuration and substrate-binding properties, contribute to its effectiveness in peptide sequencing applications.
  • Evaluate the significance of chymotrypsin in the broader context of protein structure analysis and biotechnological applications.
    • Chymotrypsin's role in the Edman degradation process for peptide sequencing is just one aspect of its broader significance in the field of protein structure analysis and biotechnology. As a serine protease, chymotrypsin's ability to selectively cleave peptide bonds has numerous applications beyond just peptide sequencing. For example, chymotrypsin is widely used in the characterization and structural elucidation of proteins, as the specific cleavage patterns it generates can provide valuable information about a protein's primary structure and potential functional domains. Furthermore, chymotrypsin has found utility in various biotechnological applications, such as in the production of peptide-based drugs, the development of protein-based biosensors, and the purification of recombinant proteins. The versatility and specificity of chymotrypsin make it an indispensable tool in the arsenal of modern biochemistry and biotechnology.