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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.
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.
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
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.
Enteropeptidase was discovered by Ivan Pavlov, who was awarded the 1904 Nobel Prize in Physiology or Medicine for his studies of gastrointestinal physiology.It is the first known enzyme to activate other enzymes, and it remains a remarkable example of how serine proteases have been crafted to regulate metabolic pathways. [6]
Transmembrane protease, serine 11D is an enzyme that in humans is encoded by the TMPRSS11D gene. [ 5 ] [ 6 ] [ 7 ] This gene encodes a trypsin -like serine protease released from the submucosal serous glands onto mucous membrane.
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.