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Endopeptidase

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.[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 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

References

  1. ^ "endopeptidase". Merriam-Webster. from the original on 18 January 2017. Retrieved 18 January 2017.

See also


endopeptidase, endoproteinase, proteolytic, peptidases, that, break, peptide, bonds, nonterminal, amino, acids, within, molecule, contrast, exopeptidases, which, break, peptide, bonds, from, pieces, terminal, amino, acids, this, reason, endopeptidases, cannot,. 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 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 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 NeprilysinReferences Edit endopeptidase Merriam Webster Archived from the original on 18 January 2017 Retrieved 18 January 2017 Endopeptidases at the US National Library of Medicine Medical Subject Headings MeSH See also EditExopeptidase The Proteolysis Map Portal Biology This enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Endopeptidase amp oldid 1111512091, wikipedia, wiki, book, books, library,

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