A) Discuss how proteolytic cleavage is used to achieve tight control of the activity of digestive enzymes.

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Chapter1: Biochemistry: An Evolving Science
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6. More enzyme activity....
A) Discuss how proteolytic cleavage is used to achieve tight control of the activity of digestive enzymes.
B) If proteolytic cleavage leads to irreversible activation of digestive enzymes, how is the activity of digestive
enzymes reduced when no longer needed? There were two ways presented this semester.
C) We looked at three serine protease enzymes: elastase, chymotrypsin, and trypsin. All three enzymes cut
peptide bonds using a similar catalytic mechanism. Explain why these are called serine proteases.
D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a
structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
Transcribed Image Text:6. More enzyme activity.... A) Discuss how proteolytic cleavage is used to achieve tight control of the activity of digestive enzymes. B) If proteolytic cleavage leads to irreversible activation of digestive enzymes, how is the activity of digestive enzymes reduced when no longer needed? There were two ways presented this semester. C) We looked at three serine protease enzymes: elastase, chymotrypsin, and trypsin. All three enzymes cut peptide bonds using a similar catalytic mechanism. Explain why these are called serine proteases. D) What are the different substrate specificities of elastase, trypsin, and chymotrypsin? And, why, from a structural standpoint, do elastase, trypsin, and chymotrypsin have different substrate specificities?
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