Question

Chymotrypsin, trypsin, and elastase are digestive enzymes called serine proteases. The serine proteases differ in substrate specificity: Chymotrypsin cleaves peptide bonds after aromatic or bulky hydrophobic side chains; trypsin requires basic amino acid residues; and elastase cleaves bonds following small uncharged side chains. A chart of amino acids can be found here. The specificity pockets (substrate-binding sites) of each of the senne proteases are drawn below. (a) Determine which specificity pocket is a part of each enzyme. Move each specificity pocket, below, to the proper bin. Note: If you answer part (a) incorrectly, a single red X will appear indicating that one or more of the answers are sorted incorrectly, Chymotrypsin Trypsin Elastase Which of the following amino acids have side chains that fit into the specificity pocket of elastase? a) Select all the amino acids that fit. b) You will need to check more than one amino acid. c) tyrosine arginine aspartate alanine glycine lysine

Answer 1

Answer:

1. Trypsin like Proteases; cleaves peptide bond following a positively charged amino acids(Lysine or Argenine)
2. Chymotrypsin like proteases; The S1 pockets of chemotrypsin like enzyme is more hydrophobic than in trypsin like proteases
3. Elastase like protease; have a much smaller S1 cleft than either trypsin or chymotrypsin like proteases.

Amino acids that have side chains that fits into the specificity pocket of elastase include; alanine, glycine and valine.