Serine Protease

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A Serine Protease is an endopeptidase that cleave peptide bonds in proteins.



References

2020

2009

  • (Wikipedia, 2009) ⇒ http://en.wikipedia.org/wiki/Bacterial_outer_membrane
    • Serine proteases or serine endopeptidases (newer name) are proteases (enzymes that cut peptide bonds in proteins) in which one of the amino acids at the active site is serine.
    • They are found in both single-cell and complex organisms, in both cells with nuclei (eukaryotes) and without nuclei (prokaryotes).
    • Serine proteases are grouped into clans that share structural similarities (homology) and are then further subgrouped into families with similar sequences.
    • The major clans found in humans include the chymotrypsin-like, the subtilisin-like, the alpha/beta hydrolase, and signal peptidase clans.
    • In evolutionary history, serine proteases were originally digestive enzymes. In mammals, they evolved by gene duplication to serve functions in blood clotting, the immune system, and inflammation.
    • Serine proteases are paired with serine protease inhibitors, which turn off their activity when they are no longer needed. [1]
  • Gene Ontology http://amigo.geneontology.org/cgi-bin/amigo/term-details.cgi?term=GO:0004867&session_id=5828amigo1240506945
    • Accession: GO:0004867
    • Ontology:molecular function
    • Synonyms
      • narrow: serpin activity
      • exact: serine protease inhibitor activity
      • exact: serine proteinase inhibitor activity
    • Definition
      • Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. [source: GOC:ai]