Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134066639
Author: Bruice
Publisher: PEARSON
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Textbook Question
Chapter 22.11, Problem 21P
Draw the pH-activity profile for an enzyme that has one catalytic group at the active site:
- a. the catalytic group is a general-acid catalyst with a pKa = 5.6.
- b. the catalytic group is a general-base catalyst with a pKa = 7.2.
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Draw the pH–activity profile for an enzyme that has one catalytic group at the active site:
the catalytic group is a general-acid catalyst with a pKa = 5.6.
Draw the pH–activity profile for an enzyme that has one catalytic group at the active site:
a. the catalytic group is a general-acid catalyst with a pKa = 5.6.
b. the catalytic group is a general-base catalyst with a pKa = 7.2.
The following grap shows the relationship between enzyme activity and both pH and temperature for two enzymes (A and B).
Based on this graphical information
What is the optimum pH for enzyme A?
What is the optimum temperature for enzyme B?
Which enzyme has the greater activity at a pH of 4?
Which enzyme has the greater activity at a temperature of 37.8°C?
Chapter 22 Solutions
Organic Chemistry (8th Edition)
Ch. 22.2 - Compare each of the mechanisms listed here with...Ch. 22.2 - Prob. 3PCh. 22.2 - Prob. 4PCh. 22.3 - a. Draw the mechanism for the following reaction...Ch. 22.5 - Prob. 7PCh. 22.5 - Propose a mechanism for the Co2+ catalyzed...Ch. 22.6 - Prob. 9PCh. 22.7 - Prob. 10PCh. 22.7 - Prob. 12PCh. 22.7 - Prob. 13P
Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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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
- Based on the graphical information in Problem 21-41 about enzymes A and B a. What is the optimum pH for enzyme B? b. What is the optimum temperature for enzyme A? c. Which enzyme has the greater activity at a pH of 7.2? d. Which enzyme has the greater activity at a temperature of 37.2C?arrow_forwardThe human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum valuearrow_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
- Quesrion: Enzyme X exhibits maximum activity at pH = 10.5. X shows a fairly sharp decrease in its activity when the pH goes much lower than 9.5. One likely interpretation of this pH activity is that: a. A His residue on the enzyme is involved in the reaction b. a Glu residue on the enzyme is involved in the reaction c. a Tyr residue on the enzyme is involved in the reaction d. the enzyme uses NADH has a cofactor e. the enzyme uses coenzyme A has a cofactor Please explain why, thanks!arrow_forwardIf the active site of lysozyme contains Glu (pKa 5.9) and Asp (pKa 4.5), what is the ionization state (protonated or deprotonated) of each residue at pH 5.2 (the optimum pH of lysozyme). How can the ionization state of these residues explain the pH effect on enzymes' function?arrow_forward1.The fundamental difference between competitive and noncompetitive inhibition is A. the degree of cooperativity of the reaction B. the size of the active site of the enzyme C. the manner of binding of substrate to the enzyme D. the manner of binding of inhibitor to the enzyme 2. Which of the following statements is correct? A. Although enzyme cannot change the value of Delta G, but it can change the value of delta G0 . B. Enzyme can increase the rate of a reaction because it can turn the value of DG0‡ from positive to negative C. Both A and B D. Neither A nor Barrow_forward
- Chymotrypsin is secreted by the pancreas and passed into the intestine. The optimal pH for this enzyme is 7.8. If a patient’s pancreas cannot manufacture chymotrypsin, would it be possible to supply it orally? Justifyarrow_forward4. 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.arrow_forwardDoes Km value change with an increase of enzyme concentration? Explainarrow_forward
- Why does an enzyme lose activity when the pH is drastically changed from optimum pH?arrow_forward1. 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_forwardDefine the optimum pH for enzyme activity.arrow_forward
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