AP BIOLOGY

Detailed explanation-1: -On passing into the intestine, where proteolytic enzymes are required to digest dietary proteins, chymotrypsinogen is attacked by trypsin. This breaks the peptide bond between arginine-15 and isoleucine-16, producing -chymotrypsin.

Detailed explanation-2: -Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.

Detailed explanation-3: -The role of enzymes Once a protein source reaches your stomach, hydrochloric acid and enzymes called proteases break it down into smaller chains of amino acids. Amino acids are joined together by peptides, which are broken by proteases.

Detailed explanation-4: -It uses an active serine residue to perform hydrolysis on the C-terminus of the aromatic amino acids of other proteins. Chymotrypsin is a protease enzyme that cleaves on the C-terminal phenylalanine (F), tryptophan (W), and tyrosine (Y) on peptide chains.

Detailed explanation-5: -Chymotrypsin is an enzyme that is used in the small intestine to break down proteins into individual amino acids.