Introduction to General, Organic and Biochemistry
11th Edition
ISBN: 9781285869759
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
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Textbook Question
Chapter 23, Problem 23.32P
2 The enzyme trypsin is synthesized by the body in the form of a long polypeptide chain containing 235 amino acids (trypsinogen), from which a piece must be cut before the trypsin can be active. Why does the body not synthesize trypsin directly?
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The vast majority of serine protease inhibitors are competitive inhibitors. Which of the following statements is true?
The Vmax of a reaction decreases in the presence of a competitive inhibitor.
Km increases with a competitive inhibitor.
A competitive inhibitor can bind to a site adjacent to the active site.
Competitive inhibition cannot be overcome by the addition of large amounts of substrate.
4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin.
a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189.
b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity?
c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
Draw the amino acids and peptide fragments formed when the decapeptide A–P–F–L–K–W–S–G–R–G is treated with each reagent or enzyme: (a) chymotrypsin; 8 pt helvetica roman (b) trypsin; (c) carboxypeptidase; (d) C6H5N = C = S.
Chapter 23 Solutions
Introduction to General, Organic and Biochemistry
Ch. 23 - What is the difference between a catalyst and an...Ch. 23 - What are ribozymes made of?Ch. 23 - Would a lipase hydrolyze two triglycerides, one...Ch. 23 - Compare the activation energy in uncatalyzed...Ch. 23 - Prob. 23.5PCh. 23 - Prob. 23.6PCh. 23 - Prob. 23.7PCh. 23 - Monoamine oxidases are important enzymes in brain...Ch. 23 - Prob. 23.9PCh. 23 - 0 What kind of reaction does each of the following...
Ch. 23 - Prob. 23.11PCh. 23 - Prob. 23.12PCh. 23 - 3 What is the difference between reversible and...Ch. 23 - Prob. 23.14PCh. 23 - 5 At a very low concentration of a certain...Ch. 23 - 6 If we wish to double the rate of an...Ch. 23 - 7 A bacterial enzyme has the following...Ch. 23 - 8 The optimal temperature for the action of...Ch. 23 - 9 The activity of pepsin was measured at various...Ch. 23 - Prob. 23.20PCh. 23 - Prob. 23.21PCh. 23 - Prob. 23.22PCh. 23 - Prob. 23.23PCh. 23 - 4 What kind of chemical reaction occurs most...Ch. 23 - 5 Which of the following is a correct statement...Ch. 23 - Prob. 23.26PCh. 23 - 7 Enzymes are long protein chains, usually...Ch. 23 - Prob. 23.28PCh. 23 - Prob. 23.29PCh. 23 - 0 Can the product of a reaction that is part of a...Ch. 23 - 1 What is the difference between a zymogen and a...Ch. 23 - 2 The enzyme trypsin is synthesized by the body in...Ch. 23 - Prob. 23.33PCh. 23 - Prob. 23.34PCh. 23 - Prob. 23.35PCh. 23 - Prob. 23.36PCh. 23 - Prob. 23.37PCh. 23 - Prob. 23.38PCh. 23 - 9 The enzyme phosphofructokinase (PFK) (Chapter...Ch. 23 - Prob. 23.40PCh. 23 - 1 After a heart attack, the levels of certain...Ch. 23 - Prob. 23.42PCh. 23 - Prob. 23.43PCh. 23 - Prob. 23.44PCh. 23 - 5 Chemists who have been exposed for years to or...Ch. 23 - 6 Which enzyme preparation is given to patients...Ch. 23 - 7 Chymotrypsm is secreted by the pancreas and...Ch. 23 - 8 Explain why transition-state analogs are potent...Ch. 23 - Prob. 23.49PCh. 23 - 0 Explain the relationship between...Ch. 23 - 1 (Chemical Connections 23A) Acetylcholine causes...Ch. 23 - Prob. 23.52PCh. 23 - Prob. 23.53PCh. 23 - Prob. 23.54PCh. 23 - Prob. 23.55PCh. 23 - 6 (Chemical Connections 23C) What role does Mn2+...Ch. 23 - 7 (Chemical Connections 23C) Which amino acids of...Ch. 23 - 8 (Chemical Connections 23D) What is the strategy...Ch. 23 - 9 (Chemical Connections 23D) Why did scientists...Ch. 23 - Prob. 23.60PCh. 23 - Prob. 23.61PCh. 23 - Prob. 23.62PCh. 23 - 3 (Chemical Connections 23E) What is the...Ch. 23 - Prob. 23.64PCh. 23 - Prob. 23.65PCh. 23 - Prob. 23.66PCh. 23 - Prob. 23.67PCh. 23 - Prob. 23.68PCh. 23 - Prob. 23.69PCh. 23 - Prob. 23.70PCh. 23 - 1 Food can be preserved by inactivation of enzymes...Ch. 23 - Prob. 23.72PCh. 23 - 3 Would you expect to find active digestive...Ch. 23 - Prob. 23.74PCh. 23 - Prob. 23.75PCh. 23 - Prob. 23.76PCh. 23 - 7 An enzyme has the following pH dependence: At...Ch. 23 - Prob. 23.78PCh. 23 - Prob. 23.79PCh. 23 - 0 Nerve gases operate by forming covalent bonds at...Ch. 23 - 1 What would be the appropriate name for an enzyme...Ch. 23 - Prob. 23.82PCh. 23 - 3 A liver enzyme is made of four subunits: 2A and...Ch. 23 - Prob. 23.84PCh. 23 - Prob. 23.85PCh. 23 - Prob. 23.86PCh. 23 - Prob. 23.87PCh. 23 - Prob. 23.88PCh. 23 - Prob. 23.89PCh. 23 - Prob. 23.90PCh. 23 - Prob. 23.91P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Why is amino acid activation called the second genetic code?arrow_forwardIn the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproductarrow_forwardWhen a foreign substance is injected in a rabbit, how long does it take to find antibodies against the foreign substance in the rabbit serum?arrow_forward
- Arginine and lysine side chains fit into trypsin’s binding pocket . One of these side chains forms a direct hydrogen bond with serine and an indirect hydrogen bond (mediated through a water molecule) with aspartate. The other side chain forms direct hydrogen bonds with both serine and aspartate. Which is which?arrow_forward[12:13 PM, 6/19/2020] Ella: Which statements about isoenzymes are TRUE?1) they are different, biologically active forms of the same enzyme2) they are the inactive forms of a biologically active enzyme3) they catalyze different reactions4) they catalyze the same reactions5) they have different tissue localizationa) 1+2+4b) 2+4+5c) 1+3+5d) 1+4+5e) 2+3+5arrow_forwardArginine and lysine side chains fit into trypsin’s binding pocket (Figure 22.5). One of these side chains forms a direct hydrogen bond with serine and an indirect hydrogen bond (mediated through a water molecule) with aspartate. The other side chain forms direct hydrogen bonds with both serine and aspartate. Which is which?arrow_forward
- 1. How will each of the following changes in condition alter the rate of the enzyme-catalyzed reaction? a. Decreasing the temperature from 37C to 10 C? b. Increasing the pH of the solution from 7 to 11? c. Heating the enzyme from 37C to 100C? d. Doubling the substrate concentration?arrow_forwardChymotrypsin is secreted by the pancres and passed into the intestine. The optimal pH for this enzyme is 7.8. If a patients pancreas cannot manufacture chymotrypsin, would it be possible to supply it orally? What happens to chymotrypsin's activity during passage through the gastrointestinal tract?arrow_forward
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