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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 ...
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
Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3.
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.
Enteropeptidase is a type II transmembrane serine protease (TTSP) localized to the brush border of the duodenal and jejunal mucosa and synthesized as a zymogen, proenteropeptidase, which requires activation by duodenase or trypsin. [9] TTSPs are synthesized as single chain zymogens with N-terminal propeptide sequences of different lengths.
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.