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Chymotrypsin: Nucleophilic catalysis:: Carboxypeptidase A: __________

Correct Answer: Electrophilic catalysis
Chymotrypsin mediated peptide bond is an example of nucleophilic catalysis. In the same way, carboxypeptidase A is and an example of electrophilic catalysis. In most of the enzymatic reaction protons are involved. General and specific acid-base catalysis are types of acid-base catalysis.

Analysis of a hexapeptide using enzymatic cleavage reveals the following result:
• Amino acid composition of the peptide is: 2R, A, V, S, Y
• Trypsin digestion yields two fragments and the compositions are: (R, A, V) and (R, S, Y)
• Chymotrypsin digestion yields two fragments and the compositions are: (A, R, V, Y) and (R, S)
• Digestion with carboxypeptidase A yields no cleavage product.
Given: Trypsin cleaves at carboxyl side of R. Chymotrypsin cleaves at carboxyl side of Y. Carboxypeptidase A cleaves at amino side of the C-terminal amino acid (except R and K) of the peptide.
The correct amino acid sequence of the peptide is:

Which of these is the cofactor for carboxypeptidase?

What is the role of carboxypeptidase B and trypsin-like peptidases in glucagon formation?

The metal present at the active site of the protein carboxypeptidase A is

Bromelain: Brewing industry:: Chymotrypsin: __________

Trypsin is used to activate __________ to form chymotrypsin.

By what factor chymotrypsin enhances the rate of peptide bond hydrolysis?

The active site of chymotrypsin consists of a catalytic triad of which of the following amino acid residues?

Which of the following statements are true about the reactions at the active center of chymotrypsin?

The polypeptide chains in chymotrypsin are linked by ___________