Is chymotrypsin responsible for hydrolysis of peptide bonds?
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One such enzyme, chymotrypsin, cleaves peptide bonds selectively on the carboxylterminal side of the large hydrophobic amino acids such as tryptophan, tyrosine, phenylalanine, and methionine (Figure 9.1). Chymotrypsin is a good example of the use of covalent modification as a catalytic strategy.
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Is chymotrypsin responsible for hydrolysis of peptide bonds?
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◇ Chymotrypsin occurs in an inactive form called
chymotrypsinogen which is activated by Trypsin,
◇ Chymotrypsin hydrolyses peptide bonds associated with specific amino acid.
◇It is a pancreatic enzyme and is proteolytie in nature. It plays a role in digestion of food in the duodenum.
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