Hi, I would like help with the following question regarding enzymes.
Chymotrypsin is a serine protease enzyme capable of cleaving peptide bonds at the C-terminal of amino acid residues containing aromatic non-polar side-chains (i.e. tryptophan, phenylalanine, tyrosine etc) Chymotrypsin H R2 Peptide Carboxyl component Amino component The enzyme mechanism for hydrolysis involves both non-covalent and covalent catalysis within the enzyme active site. Please describe the nature of these interactions illustrated in the catalytic triad below: Asp 102 His 57 Ser 195 peptide 1 N-peptide 2 0