Concept explainers
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - IV Carbonic anhydrase catalyzes the hydration of
a. What is Vmax for this enzyme?
b. Assuming 5 pmol/mL (
c. What is the catalytic efficiency of this enzyme?
d. Does carbonic anhydrase approach "catalytic perfection"?
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Biochemistry
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Plot the Titration Curve for Bicine and Calculate How to Prepare a pH 7.5 Bicine Buffer Solution Bicine (N, N—bis (2-hydroxyethyl) glycine) is another commonly used buffer in biochemistry labs. The structure of Bicine in its fully protonated form is shown here: Draw the titration curve for Bicine. assuming the pA'a for its free COOH group is 2.3 and the pAa for its tertiary amino group is 8.3. Draw the structure of the fully deprotonated form (completely dissociated form) of bicine. You have available a U.l Msolution of Bicine at its isoelectric point (pH|)T 0.1 M solutions of HCI and NaOH. and ample distilled water. Describe the preparation of 1 L of 0.U4 M Bicine buffer. pH 7.5. What is the concentration of the fully protonated form of Bicine in your final buffer solution?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating [H] and pKd from the pH of a Solution of Weak Acid The pH of a 0.02 M solution of an acid was measured at 4.6. What is the [H+] in this solution? Calculate the acid dissociation constant Ka and pKa for this acid.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculate the pH in a Muscle Cell from the HPO42-/H2PO4Ratio If the internal pH of a muscle cell is 6.8, what is the [HPO42-]/ [H2PO4-] ratio in this cell?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - III The citric acid cycle enzyme fumarase catalyzes the conversion of fumarate to form malate. Fumarate+H2OmalateThe turnover number, kcat, for fumarase is 800/sec. The Km of fumarase for its substrate fumarate is 5M. a. In an experiment using 2 nanomole/mL of fumarase, what is Vmax? b. The cellular concentration of fumarate is 47.5 M. What is v when [fumarate] = 47.5 M? c. What is the catalytic efficiency of fumarase? d. Does fumarase approach catalytic perfection?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.arrow_forwardAnswers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Consult the following reference (Samanta U. and Bahnson. B. J., 2008. Crystal structure of human plasma platelet-activating factor acetylhydrolase. Journal of Biological Chemistry 283:31617-3U624). consider the active-site structure of this enzyme in the Light of material in this chapter, and write a detailed mechanism for the PAF acetylhydrolase.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - VI The enzyme catalase catalyzes the decomposition of hydrogen peroxide: 2H2O22H2O+O2The turnover number (kcat) for catalase is 40,000,000 sec-1. The Km of catalase for its substrate H2O2 is 0.11 M. a. In an experiment using 3 nanomole/L of catalase, what is Vmax? b. What is v when [H2O2] = 0.75 M? c. What is the catalytic efficiency of catalase? d. Does catalase approach catalytic perfection?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Using Graphical Methods to Derive the Kinetic Constants for an Ordered, Single-Displacement Reaction The general rate equation for an ordered, single-displacement reaction where A is the leading substrate is v=Vmax[ A ][ B ](KsAKmB+KmA[ B ]+KmB[ A ]+[ A ][ B ])Write the Lineweaver-Burk (double-reciprocal) equivalent of this equation and from it calculate algebraic expressions for the following: a. The slope b. The y-intercepts c. The horizontal and vertical coordinates of the point of intersection when 1/v is plotted versus 1/[B] at various fixed concentrations of Aarrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rale Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxy-acetone phosphate. Glyceraldehyde3PdihydroxyacetonePThe Km of this enzyme tor its substrate glyceraldehyde-3-phosphate is 1.8 10-5 M. When [glyceraldehydes-3-phosphate] = 30 M, the rate of the reaction, v, was 82.5 mol mL-1 sec-1. a. What is Vmax for this enzyme? b. Assuming 3 nanomoles per mL of enzyme was used in this experiment ([Etotal]) = 3 nanomol/mL), what is kcat for this enzyme? c. What is the catalytic efficiency (kcat/Km) for triose phosphate isomerase? d. Does the value of kcat/Km reveal whether triose phosphate isomerase approaches catalytic perfection? e. What determines the ultimate speed limit of an enzyme-catalyzed reaction? That is, what is it that imposes the physical limit on kinetic perfection?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating Keq from G°’ Write the equilibrium constant, Keq, for the hydrolysis of creatine phosphate and calculated value for Keq at 25°C from the value of G' in Table 3.2.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating pH from [H+] Calculate the pH of the following. 5 10-4 M HCl 7 10-5 M NaOH 2M HCl 7 10-2 M KOH 04 m HCl 6 10-9 M HClarrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating [H+] from pH Calculate the following from the pH values given in Table 2.3. [H+] in vinegar [H+] in saliva [H+] in household ammonia [OH-] in milk of magnesia [OH-] in beer [H+] inside a liver cellarrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning