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Peptidases definitions

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  • Peptidase
    Enzyme that hydrolyzes specific peptide bonds, often with unique amino acid preferences and inhibition by proline.
  • Trypsin
    Digestive enzyme that cleaves peptide bonds on the carboxyl side of lysine and arginine, but not when proline is involved.
  • Chymotrypsin
    Enzyme preferring aromatic amino acids for cleavage, also slowly acts on leucine and methionine, always on the carboxyl side.
  • Aromatic Amino Acid
    Residue with a ring structure, such as phenylalanine, tyrosine, or tryptophan, recognized by chymotrypsin and pepsin.
  • Lysine
    Amino acid with an extended R group, targeted by trypsin for cleavage on its carboxyl side unless proline is present.
  • Arginine
    Residue with a three-carbon chain and a triangular nitrogen group, recognized by trypsin and thrombin for cleavage.
  • Proline
    Amino acid whose involvement in peptide bonds inhibits cleavage by most peptidases due to its unique ring structure.
  • Leucine
    Hydrophobic residue slowly cleaved by chymotrypsin and recognized by pepsin, but not by elastase if proline is present.
  • Methionine
    Residue with a sulfur atom, cleaved slowly by chymotrypsin, but not recognized by pepsin or elastase.
  • Elastase
    Peptidase that cleaves peptide bonds after small neutral R group residues, excluding methionine and proline.
  • Thrombin
    Enzyme that specifically cleaves peptide bonds after arginine residues on the carboxyl side.
  • Pepsin
    Enzyme that cleaves peptide bonds on the N-terminal side of aromatic residues and leucine, but not methionine.
  • Carboxypeptidase A
    Peptidase that removes C-terminal residues, except arginine, lysine, and proline, by cleaving the N-terminal bond.
  • C-terminal
    End of a polypeptide chain with a free carboxyl group, often the site of peptidase cleavage.
  • N-terminal
    End of a polypeptide chain with a free amino group, recognized by pepsin for cleavage.