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What is the catalytic triad of chymotrypsin, a type of serine protease?

a. the amino acids serine, histidine, and glutamate
b. the enzyme−cofactor−intermediate complex
c. the enzyme−cofactor−substrate complex
d. the amino acids cysteine, histidine, and aspartate
e. the amino acids serine, histidine, and aspartate

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Answer:

e. the amino acids serine, histidine, and aspartate

Step-by-step explanation:

Chymotrypsin is a digestive proteolytic enzyme secreted in the duodenum by the pancreas. It is a member of the serine proteases with active sites containing serine, histidine, and aspartate which it uses to cleave through hydrolysis (addition of a molecule of water) the c-terminus of aromatic amino acid tryptophan, tyrosine, and phenylalanine on peptide chains. Its hydrophobic pockets makes it suitable for aromatic amino acids.

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