Which pancreatic protease cleaves peptide bonds after basic amino acids?

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Multiple Choice

Which pancreatic protease cleaves peptide bonds after basic amino acids?

Protease specificity is defined by the enzyme’s substrate-binding pocket and how it recognizes certain side chains to position the peptide bond for cleavage. Trypsin has a negatively charged pocket that binds positively charged side chains, specifically the amino acids lysine and arginine. This makes it cut the peptide bond on the carboxyl side of these basic residues, which is exactly what the question describes. Chymotrypsin, in contrast, prefers bulky aromatic side chains; elastase targets small neutral residues; and carboxypeptidase works from the C-terminus, removing amino acids rather than making internal cuts. So the pancreatic protease that cleaves after basic amino acids is trypsin.

Protease specificity is defined by the enzyme’s substrate-binding pocket and how it recognizes certain side chains to position the peptide bond for cleavage. Trypsin has a negatively charged pocket that binds positively charged side chains, specifically the amino acids lysine and arginine. This makes it cut the peptide bond on the carboxyl side of these basic residues, which is exactly what the question describes. Chymotrypsin, in contrast, prefers bulky aromatic side chains; elastase targets small neutral residues; and carboxypeptidase works from the C-terminus, removing amino acids rather than making internal cuts. So the pancreatic protease that cleaves after basic amino acids is trypsin.

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