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[edit]
- ^ "endopeptidase". Merriam-Webster. Archived from the original on 21 December 2016. Retrieved 18 January 2017.
- Endopeptidases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
See also[edit]
Well, that’s interesting to know that Psilotum nudum are known as whisk ferns. Psilotum nudum is the commoner species of the two. While the P. flaccidum is a rare species and is found in the tropical islands. Both the species are usually epiphytic in habit and grow upon tree ferns. These species may also be terrestrial and grow in humus or in the crevices of the rocks.
View the detailed Guide of Psilotum nudum: Detailed Study Of Psilotum Nudum (Whisk Fern), Classification, Anatomy, Reproduction