Chymotrypsin

Definition

Chymotrypsin is a digestive enzyme produced in the pancreas and activated in the small intestine. It breaks down proteins into smaller peptides by cleaving peptide bonds.

5 Must Know Facts For Your Next Test

1. Chymotrypsin is secreted as an inactive precursor called chymotrypsinogen.
2. The activation of chymotrypsinogen into chymotrypsin occurs in the small intestine.
3. Chymotrypsin specifically targets peptide bonds adjacent to aromatic amino acids like phenylalanine, tyrosine, and tryptophan.
4. It works optimally at a slightly alkaline pH found in the small intestine.
5. Chymotrypsin plays a crucial role in protein digestion, complementing other proteases such as trypsin.

Review Questions

• What form is chymotrypsin secreted in from the pancreas?
• Where does the activation of chymotrypsinogen occur?
• Which type of amino acids does chymotrypsin specifically target when breaking peptide bonds?

Related terms

Trypsin: A pancreatic enzyme that activates chymotrypsinogen and also breaks down proteins into peptides.

Peptidase: An enzyme that catalyzes the hydrolysis of peptides into amino acids.

Pancreas: A glandular organ that produces enzymes like chymotrypsin for digestion and hormones for blood sugar regulation.