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12 Nov 2019
1·Chemical mechanism of chymotrypsin. a) What are the substrates and the products of chymotrypsin? Why do you think artificial substrates with brightly colored C-terminal or N-terminal labels are commonly used to study this enzyme? b) What is meant by saying that catalysis by chymotrypsin shows an "early burst phase" and what is the significance of that observation for the mechanism by which chymotrypsin cleaves a protein substrate. c) What are the main roles of the aspartic acid and the histidine in the catalytic triad in chymotrypsin's active site? d) Chymotrypsin is a digestive enzyme produced by the pancreas. Why is chymotrypsin not active inside the pancreas? In other words, what happens in the digestive tract to activate this protease? e) Chymotrypsin uses an activated Ser to cut its substrate proteins. Name some of the other activated groups used by proteases to cut proteins
1·Chemical mechanism of chymotrypsin. a) What are the substrates and the products of chymotrypsin? Why do you think artificial substrates with brightly colored C-terminal or N-terminal labels are commonly used to study this enzyme? b) What is meant by saying that catalysis by chymotrypsin shows an "early burst phase" and what is the significance of that observation for the mechanism by which chymotrypsin cleaves a protein substrate. c) What are the main roles of the aspartic acid and the histidine in the catalytic triad in chymotrypsin's active site? d) Chymotrypsin is a digestive enzyme produced by the pancreas. Why is chymotrypsin not active inside the pancreas? In other words, what happens in the digestive tract to activate this protease? e) Chymotrypsin uses an activated Ser to cut its substrate proteins. Name some of the other activated groups used by proteases to cut proteins
Reid WolffLv2
25 Oct 2019