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Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. 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 ...
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.
They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like in the trypsin serine proteases. The structure of proteins in this family shows that they have an alpha/beta fold containing a 7-stranded parallel beta sheet. The subtilisin family is the second largest serine protease family characterised to date.
Acrosin is a typical serine proteinase with trypsin-like specificity. [3]Acrosin catalytic mechanism. The reaction proceeds according to the usual serine protease mechanism. . First, His-57 deprotonates Ser-195, allowing it to serve as a nucleophi
Proteolytic removal of the domain activates the enzyme. It is structurally unrelated to the chymotrypsin-clan of serine proteases, but uses the same type of catalytic triad in the active site. This makes it a classic example of convergent evolution.
Matriptases (EC 3.4.21.109) are an enzyme family. [1] [2] This enzyme cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis.
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