Endopeptidase

An Endopeptidase is a proteolytic peptidase that breaks peptide bonds of amino acids within the Biomolecule.

• AKA: Endoproteinase.
  • …
• Example(s)
  • An Oligopeptidase.
  • A Trypsin.
  • A Chymotrypsin.
  • An Elastase.
  • A Thermolysin.
  • A Pepsin.
  • A Glutamyl Endopeptidase.
  • A Neprilysin.
  • …
• Counter-Example(s)
  • An Exopeptidase.
• See: Neprilysin, Proteolysis, Peptidase, Peptide Bonds, Amino Acid, Exopeptidase, Oligopeptidase, Trypsin, Chymotrypsin, Elastase, Thermolysin, Pepsin.

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References

2017

• (Wikipedia, 2017) ⇒ https://en.wikipedia.org/wiki/Endopeptidase Retrieved:2017-7-9.
  • Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins.

    They are usually very specific for certain amino acids. Examples of endopeptidases include:

    • Trypsin - cuts after Arg or Lys, unless followed by Pro. Very strict. Works best at pH 8.
    • Chymotrypsin - cuts after Phe, Trp, or Tyr, unless followed by Pro. Cuts more slowly after His, Met or Leu. Works best at pH 8.
    • Elastase - cuts after Ala, Gly, Ser, or Val, unless followed by Pro.
    • Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, unless preceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. Heat stable.
    • Pepsin - cuts before Leu, Phe, Trp or Tyr, unless preceded by Pro. Also others, quite nonspecific; works best at pH 2.
    • Glutamyl endopeptidase - cuts after Glu. Works best at pH 8.
    • Neprilysin

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