Serine Protease
(Redirected from serine protease)
Jump to navigation
Jump to search
A Serine Protease is an endopeptidase that cleave peptide bonds in proteins.
- Context:
- It can involve a Hydroxy Group of the Serine Residue.
- It can play an important role in Digestion, Blood Clotting, and the Complement System.
- …
- Example(s):
- Halobacterium mediterranei http://www.uniprot.org/uniprot/P28308
- PMID 1637313:“A homogeneous serine proteinase secreted by the extreme halophilic bacterium Halobacterium mediterranei 1538 was isolated by affinity chromatography on bacitracin-Sepharose with a yield of 48% (260-fold purification)”
- See: Eukaryotes), prokaryotes, Subtilisin, Camostat, Enzyme, Peptide Bond, Serine, Nucleophilic, Amino Acid.
References
2020
- (Wikipedia, 2020) ⇒ https://en.wikipedia.org/wiki/serine_protease Retrieved:2020-3-25.
- Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.[1]
They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.[2]
- Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.[1]
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]