Which of the following would help elucidate the role of Ser195 in chymotrypsin? modification with TPCK modification with p-nitrophenyl ester modification with DIPF modification with both p-nitrophenyl ester and TPCK
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Step 1: Ser195 is the active site residue in chymotrypsin. Show more…
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TPCK inactivates chymotrypsin but not trypsin because: a. It looks like the substrate for chymotrypsin (but not trypsin) and thus can bind in its active site and modify His-57. b. Trypsin does not have a His residue present in the active site to react with TPCK. c. TPCK is a transition state analog for chymotrypsin but not trypsin.
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TPCK and TLCK are irreversible inhibitors of serine proteases. One of these inhibits trypsin and the other inhibits chymotrypsin. Which inhibits which? Explain:
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You have isolated a new protease that cleaves peptide bonds following Asp and Glu. Based on its inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by: (A) the presence of a positively charged residue in the S1 binding pocket. (B) the replacement of serine-195 with a positively charged residue. (C) the presence of a negatively charged residue in the S1 binding pocket.
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