Which pancreatic protease cleaves peptide bonds after small, neutral amino acids?

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Multiple Choice

Which pancreatic protease cleaves peptide bonds after small, neutral amino acids?

Pancreatic proteases have distinct substrate preferences based on their active sites. Elastase has a narrow pocket that favors small, neutral side chains, so it cleaves peptide bonds after residues like alanine and glycine. This makes elastase the enzyme that targets these small, neutral amino acids. In contrast, trypsin cuts after positively charged residues (lysine, arginine), chymotrypsin after bulky hydrophobic residues (phenylalanine, tyrosine, tryptophan), and carboxypeptidases remove amino acids from the C-terminus rather than performing internal peptide bond cleavage.

Pancreatic proteases have distinct substrate preferences based on their active sites. Elastase has a narrow pocket that favors small, neutral side chains, so it cleaves peptide bonds after residues like alanine and glycine. This makes elastase the enzyme that targets these small, neutral amino acids. In contrast, trypsin cuts after positively charged residues (lysine, arginine), chymotrypsin after bulky hydrophobic residues (phenylalanine, tyrosine, tryptophan), and carboxypeptidases remove amino acids from the C-terminus rather than performing internal peptide bond cleavage.

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