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In vivo, chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favorable, occurs extremely slowly in the absence of a catalyst. The main substrates of chymotrypsin are peptide bonds in ...
Recall that trypsin is also responsible for cleaving lysine peptide bonds, and thus, once a small amount of trypsin is generated, it participates in cleavage of its own zymogen, generating even more trypsin. The process of trypsin activation can thus be called autocatalytic. Chymotrypsinogen: chymotrypsin
The active form is called π-chymotrypsin and is used to create α-chymotrypsin. Trypsin cleaves the peptide bond in chymotrypsinogen between arginine-15 and isoleucine-16. This creates two peptides within the π-chymotrypsin molecule, held together by a disulfide bond. One π-chymotrypsin acts on another by breaking a leucine and serine ...
Chymotrypsin preferentially cleaves C-terminally of large aromatic residues such as phenylalanine (left). The peptide backbone is colored dark red, the sidechains are shown in bright red. In the first step, the catalytic triade enhances the nucleophilicity of Ser 195 which attacks the carbon atom of the peptide bond, leading to formation of a ...
Chymotrypsin C (EC 3.4.21.2) is an enzyme. [1] [2] [3] This enzyme catalyses the following chemical reaction: Preferential cleavage: Leu-, Tyr-, Phe-, Met-, Trp-, Gln-, Asn! This enzyme is formed from pig chymotrypsinogen C and from cattle subunit II of procarboxypeptidase A.
In the 1950s, a serine residue was identified as the catalytic nucleophile of trypsin and chymotrypsin (first purified in the 1930s) [6] by diisopropyl fluorophosphate modification. [7] The structure of chymotrypsin was solved by X-ray crystallography in the 1960s, showing the orientation of the catalytic triad in the active site. [8]
The 3C-like protease (3CL pro) or main protease (M pro), formally known as C30 endopeptidase or 3-chymotrypsin-like protease, [2] is the main protease found in coronaviruses. It cleaves the coronavirus polyprotein at eleven conserved sites. It is a cysteine protease and a member of the PA clan of proteases.
Examples include cleavage of the Asp-Pro bond in a subset of von Willebrand factor type D (VWD) domains [14] [15] and Neisseria meningitidis FrpC self-processing domain, [16] cleavage of the Asn-Pro bond in Salmonella FlhB protein, [17] Yersinia YscU protein, [18] as well as cleavage of the Gly-Ser bond in a subset of sea urchin sperm protein ...