Which pancreatic protease cleaves after aromatic residues?

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Multiple Choice

Which pancreatic protease cleaves after aromatic residues?

Chymotrypsin is tested here for its strong preference to cut peptide bonds after bulky aromatic side chains. Its active site features a hydrophobic S1 pocket that snugly accommodates phenylalanine, tyrosine, and tryptophan, lining up the bond for cleavage by the catalytic triad. This specificity explains why chymotrypsin cleaves after those aromatic residues. In contrast, trypsin targets basic residues (lysine and arginine) because its pocket is negatively charged, elastase prefers small neutral residues, and carboxypeptidase is an exopeptidase that removes amino acids from the C-terminus rather than performing internal cleavages.

Chymotrypsin is tested here for its strong preference to cut peptide bonds after bulky aromatic side chains. Its active site features a hydrophobic S1 pocket that snugly accommodates phenylalanine, tyrosine, and tryptophan, lining up the bond for cleavage by the catalytic triad. This specificity explains why chymotrypsin cleaves after those aromatic residues. In contrast, trypsin targets basic residues (lysine and arginine) because its pocket is negatively charged, elastase prefers small neutral residues, and carboxypeptidase is an exopeptidase that removes amino acids from the C-terminus rather than performing internal cleavages.

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