Endopeptidase or endoproteinase are proteolytic peptidases that break peptide obligations of nonterminal amino acids (for example inside the particle), as opposed to exopeptidases, which break peptide bonds from end-bits of terminal amino acids. For this explanation, endopeptidases can't separate peptides into monomers, while exopeptidases can separate proteins into monomers. A specific instance of endopeptidase is the oligopeptidase, whose substrates are oligopeptides rather than proteins.

 

They are generally quite certain for certain amino acids. Instances of endopeptidases include:

 

Trypsin - cuts after Arg or Lys, except if followed by Pro. Strict. Works best at pH 8.

 

Chymotrypsin - cuts after Phe, Trp, or Tyr, except if followed by Pro. Cuts all the more gradually after His, Met or Leu. Works best at pH 8.

 

Elastase - cuts after Ala, Gly, Ser, or Val, except if followed by Pro.

 

Thermolysin - cuts before Ile, Met, Phe, Trp, Tyr, or Val, except if went before by Pro. In some cases cuts after Ala, Asp, His or Thr. Warmth stable.

 

Pepsin - cuts before Leu, Phe, Trp or Tyr, except if went before by Pro. Additionally others, very vague; works best at pH 2.

 

Glutamyl endopeptidase - cuts after Glu. Works best at pH 8.

 

Neprilysin

Last Updated on: Jul 05, 2024