Question

1)     About Chymotrypsin:

a.      What 3 amino acids are part of the catalytic triad?

b.      What does the catalytic triad do in the enzyme mechanism?

c.      What is the function of the hydrophobic pocket?

d.      What is the function of the oxyanion hole?

Answer 1

Chymotrypsin is a serine proteases which functions as a digestive enzyme.

a)  Histidine 57, aspartic acid 102, and serine 195 residue forms the catalytic triadin the active site.

b) The catalytic triad facilitates the cleavage of peptide bonds by a hydrolysis reaction.

c) The hydrophobic pocket allows uncharged amino acids like phenylalanine and tryptophan to fit in chymotrypsin and to fot the adjacent peptide bond at the active site for cleavage.

d) The oxyanion hole is a pocket in the active site of an enzyme. It's function is to stabilize the transition state negative charge on a deprotonated oxygen or alkoxide.