What determines the specificity of chymotrypsin?
The Active Site Environment A specific pocket adjacent to the active site triad determines the specificity of the protease (chymotrypsin cleaves adjacent to large aromatic side chains, trypsin adjacent to lys or arg residues). These are amino acids 189, 216 and 226 which line a pocket adjacent to the active site triad.
What is the significance of chymotrypsin?
Chymotrypsin is an enzyme that is used in the small intestine to break down proteins into individual amino acids. It specifically targets the aromatic amino acids, tyrosine, phenylalanine, and tryptophan. Chymotrypsin has also seen some use in medicine, particularly in assisting cataract surgery.
Which amino acid undergoes acylation and deacylation in the active site of chymotrypsin?
Since only serine-195 was modified by diisopropylphosphofluoridate, it indicates that Serine-195 plays the crucial role in the mechanism as a nucleophile. It is covalently linked to Serine-195. Covalent catalysis of chymotrypsin basically goes through acylation and deacylation.
Which type of the specificity is exhibited by enzymes?
Enzymes are specific to particular reactions. There are 4 types of specificity – absolute, group, linkage, and stereochemical. Not all enzymes work on all substrates.
Which of the following is function of enzyme chymotrypsin?
Chymotrypsin (Chy or α-Chy) is a digestive enzyme containing an active serine residue, which helps to digest proteins in our food.
Why does the enzyme reaction for chymotrypsin proceed in two phases?
Why does the enzyme reaction for chymotrypsin proceed in two phases? The initial phase releases the first product and involves and acylenzyme intermediate. This step is faster than te second part, in which water comes into the active site and breaks the acyl-enzyme bond.
What three amino acids are found in the catalytic triad of chymotrypsin?
Chymotrypsin contains a collection of three amino acids called the catalytic triad. This triad consists of serine-195, histidine-57 and aspartate-102. These amino acids work together to carry out the catalytic function of breaking peptide bonds.
How does chymotrypsin catalyze the hydrolysis of peptides?
The probable catalytic mechanism for chymotrypsin has been worked out during the past half-century of intensive investigation. This enzyme cleaves peptide bonds within peptides and proteins, acting preferentially at sites where the carboxyl-donating amino acid residue has a hydrophobic side-chain.
What is the mechanism of action of chymotrypsin?
Chymotrypsin is a member of a family of enzymes that cleave peptide bonds through the action of an active site serine (the serine proteases). This family includes the pancreatic enzymes chymotrypsin, trypsin, and elastase as well as a variety of other proteases (e.g., cocoonase, thrombin, acrosomal protease, etc.).
What is the pH of chymotrypsin?
The mammalian chymotrypsin has a pH optimum around 8, with two catalytic important pK a s of 6.8 and 9.5, corresponding to the active-site histidine and N-terminal leucine, respectively. In contrast, the M. sexta chymotrypsin has pH optimum 10.5–11, and a single kinetically significant pK a at pH 9.2.
When did chymotrypsin become a proteinase?
As early as the late 1930s, Bergmann & Fruton  realized that chymotrypsin (and trypsin), which were thus far considered as ‘proteinases’ specifically splitting large proteins, were actually able to cleave ‘internal’ peptide bonds of short peptides also.
What is the molecular mass of chymotrypsin in insects?
Insect chymotrypsins usually have molecular masses of 20–30 kDa and pH optima of 8–11, and they differ from their vertebrate counterparts in their instability at acidic pH, inhibition pattern with SBTI (Terra and Ferreira, 1994) and, finally, in reacting with N -α-tosyl- l -phenylalanine chloromethyl ketone (TPCK) (see below).