Question

Please carry out a table-based comparison between the catalytic mechanisms of chymotrypsin and lysozyme.

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Answer 1

chymotrypsin and lysozyme.
Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid C-terminal to the scissile amide bond is a large hydrophobic amino acid like tyrosine, tryptophan, and phenylalanine.
chymotrypsin is a proteolytic enzyme, especially belonging to the serine protease. This acts in the digestive systems of many organisms. The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine.
Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile.

Lysozyme is also known as muramidase or N-acetylmuramide glycanhydrolase. It is an antimicrobial enzyme produced by animals.
Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.
This hydrolysis causes lysis of the bacteria.