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Below is a figure of the chymotrypsin active site. Trypsin is a serine protease with an identical mechanism to chymotrypsin, but cleaves peptides next to positively-charged amino acids instead of after hydrophobic amino acids. Which of the following statements would you expect to be FALSE? Asp -- Active site Oxyanion hole HO-(Seps Chymotrypsin (free enzyme) Hydrophobic pocket

Below is a figure of the chymotrypsin active site. Trypsin is a serine protease with an identical mechanism to chymotrypsin, but cleaves peptides next to positively-charged amino acids instead of after hydrophobic amino acids. Which of the following statements would you expect to be FALSE? Asp -- Active site Oxyanion hole HO-(Seps Chymotrypsin (free enzyme) Hydrophobic pocket

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Below is a figure of the chymotrypsin active site. Trypsin is a serine protease with an identical mechanism to chymotrypsin, but cleaves peptides next to positively-charged amino acids instead of after hydrophobic amino acids. Which of the following statements would you expect to be FALSE? Asp --- Active site Oxyanion hole" HO-(Ser Chymotrypsin (free enzyme) Hydrophobic pocket O a. Asp 102 will bind the substrate in Trypsin. O b. Serine 195 will be conserved in Trypsin. Oc. His 57 will be conserved in Trypsin. Od. The oxyanion hole will be present in Trypsin. Oe. The substrate-binding site will include an Asp or Glu in Trypsin.
Transcribed Image Text:Below is a figure of the chymotrypsin active site. Trypsin is a serine protease with an identical mechanism to chymotrypsin, but cleaves peptides next to positively-charged amino acids instead of after hydrophobic amino acids. Which of the following statements would you expect to be FALSE? Asp --- Active site Oxyanion hole" HO-(Ser Chymotrypsin (free enzyme) Hydrophobic pocket O a. Asp 102 will bind the substrate in Trypsin. O b. Serine 195 will be conserved in Trypsin. Oc. His 57 will be conserved in Trypsin. Od. The oxyanion hole will be present in Trypsin. Oe. The substrate-binding site will include an Asp or Glu in Trypsin.
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