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[1] [2] Absence of enteropeptidase results in intestinal digestion impairment. [3] Enteropeptidase is a serine protease (EC 3.4.21.9) consisting of a disulfide-linked heavy-chain of 82-140 kDa that anchors enterokinase in the intestinal brush border membrane and a light-chain of 35–62 kDa that contains the catalytic subunit. [4]
Trypsinogen (/ ˌ t r ɪ p ˈ s ɪ n ə dʒ ə n,-ˌ dʒ ɛ n / [1] [2]) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen. It is cleaved to its active form, trypsin, by enteropeptidase, which is found in the ...
When the tetrahedral intermediate of step 1 and step 3 are generated, the negative oxygen ion, having accepted the electrons from the carbonyl double bond, fits perfectly into the oxyanion hole. In effect, serine proteases preferentially bind the transition state and the overall structure is favored, lowering the activation energy of the reaction.
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.
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. [1]
Some examples of exopeptidases include: [1] Carboxypeptidase A - cleaves C-terminal Phe, Tyr, Trp, or Leu; Carboxypeptidase B - cleaves C-terminal Lys or Arg; Aminopeptidase - cleaves any N-terminal amino acid; Prolinase - cleaves N-terminal Pro from dipeptides [2] Prolidase - cleaves C-terminal Pro from dipeptides [3]
S. aureus glutamyl endopeptidase GluV8 [1] The first discovered enzyme of this family, and the most well characterized, was isolated from the Staphylococcus aureus strain V8, and hence better known as "V8 protease". Other common references to this protease are staphylococcal serine protease, and SspA from its corresponding gene. [1] [2] [3]
The family is usually broken into two parts, one being the ClpA/B family with two ATPase domains, and the other being ClpX and friends with only one such domain. [7] ClpA through E is put into the first group along with Hsp78/104, and ClpX and HSIU is put into the second group.