Endopeptidase orendoproteinase areproteolyticpeptidases that breakpeptide bonds of nonterminalamino acids (i.e. within the molecule), in contrast toexopeptidases, which break peptide bonds from end-pieces of terminal amino acids.[1] For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is theoligopeptidase, 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 - cutsbefore Ile, Met, Phe, Trp, Tyr, or Val, unlesspreceded by Pro. Sometimes cuts after Ala, Asp, His or Thr. Heat stable.
Pepsin - cutsbefore Leu, Phe, Trp or Tyr, unlesspreceded by Pro. Also others, quite nonspecific; works best at pH 2.
