Which pancreatic protease cleaves peptide bonds after aromatic amino acids?

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Multiple Choice

Which pancreatic protease cleaves peptide bonds after aromatic amino acids?

Protease specificity for the amino acid side chain at the cleavage site determines which peptide bonds are cut. Chymotrypsin has a hydrophobic pocket that fits bulky aromatic side chains, so it cleaves peptide bonds on the carboxyl side of aromatic residues like phenylalanine, tyrosine, and tryptophan. That makes it the enzyme that cleaves after aromatic amino acids in pancreatic digestion. Elastase prefers small neutral residues, trypsin targets basic residues, and carboxypeptidase acts from the C-terminus as an exopeptidase rather than cleaving after a particular internal residue.

Protease specificity for the amino acid side chain at the cleavage site determines which peptide bonds are cut. Chymotrypsin has a hydrophobic pocket that fits bulky aromatic side chains, so it cleaves peptide bonds on the carboxyl side of aromatic residues like phenylalanine, tyrosine, and tryptophan. That makes it the enzyme that cleaves after aromatic amino acids in pancreatic digestion.

Elastase prefers small neutral residues, trypsin targets basic residues, and carboxypeptidase acts from the C-terminus as an exopeptidase rather than cleaving after a particular internal residue.

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