Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 6, Problem 19E
Summary Introduction
To draw: The pyroglutamate residue.
Concept introduction: Protein is made up of one or more amino acids linked together to form a chain. The building blocks of the protein are called amino acids. The eight essential amino acids are phenylalanine, isoleucine, leucine, methionine, histidine, lysine, tryptophan, threonine, and valine. The linear sequence of amino acid residues that are interlinked by a covalent bond is called peptide bond.
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The preferred substrate is T because the enzyme half-saturates at 7.00 mM for T, but requires 28.0 mM for U, and 112 mM for S.
b
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The rate constant k 2 with substrate S is 9.60×107 sec-1, with substrate T, k 2 = 6.00×104 sec-1, and with substrate U, k 2 = 2.40×106 sec-1.
Calculate the catalytic efficiency with S, T, and U.
Catalytic efficiency with S =
Catalytic efficiency with T =
Catalytic efficiency with U =
Does enzyme A use substrate S, substrate T, or substrate U with greater catalytic efficiency?
Fumerase catalyzes the conversion of fumerate to malate.
fumerate + H2O ⇋ malate
The turnover number, kcat, for fumerase is 8.00×102 sec-1. The Km of this enzyme for fumerate is 5.00×10-3 μmol mL-1.
a
In an experiment using 2.00×10-3 μmol·mL-1, what is Vmax?
Suppose you wanted to make a buffer of exactly pH 7.00 using KH2PO4 and Na2HPO4. If the final solution was 0.18 M in KH2PO4, you would need 0.25 M Na2HPO4. Now assume you wish to make a buffer at the same pH, using the same substances, but want the total phosphate molarity ([HPO42−]+[H2PO−4]) to equal 0.20 M. What concentration of the Na2HPO4 would be required?
Chapter 6 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 6 - Prob. 1ECh. 6 - Prob. 2ECh. 6 - 3. Why would you be unlikely to see an ? helix...Ch. 6 - 4. Calculate the length in angstroms of a...Ch. 6 - Prob. 5ECh. 6 - 6. Collagen IV, which occurs in basement...Ch. 6 - 7. Describe the primary, secondary, tertiary, and...Ch. 6 - 8. Explain why gelatin, which is mostly collagen,...Ch. 6 - Prob. 9ECh. 6 - 10. Is it possible for a native protein to be...
Ch. 6 - Prob. 11ECh. 6 - 12. (a) Is Trp or Gln more likely to be on a...Ch. 6 - 13. Classify the following proteins as ?, ?, or...Ch. 6 - 14. Classify the following proteins as ?, ?, or...Ch. 6 - 15. You are performing site-directed mutagenesis...Ch. 6 - 16. Laboratory techniques for randomly linking...Ch. 6 - Prob. 17ECh. 6 - 18. The genetically engineered proteins that...Ch. 6 - Prob. 19ECh. 6 - 20. Experiments in mice suggest that...Ch. 6 - 21. Helices can be described by the notation nm,...Ch. 6 - Prob. 22CQCh. 6 - 23. Which of the following polypeptides is most...Ch. 6 - 24. Which of the peptides in Problem 23 is least...Ch. 6 - Prob. 25CQCh. 6 - 26. What types of rotational symmetry are possible...Ch. 6 - Prob. 27CQCh. 6 - 28. Proteins in solution are often denatured if...Ch. 6 - 29. Given enough time, will all denatured proteins...Ch. 6 - Prob. 30CQCh. 6 - 31. Under physiological conditions, polylysine...Ch. 6 - 32. Would intrinsically disordered polypeptide...Ch. 6 - Prob. 33CQCh. 6 - Prob. 34CQCh. 6 - Prob. 35CQCh. 6 - 36. Not all heat shock proteins are chaperones;...Ch. 6 - 37. Protein denaturation can be triggered by a...Ch. 6 - 38. Explain why ? sheets are less likely to form...Ch. 6 - 39. The GroEL/ES cycle diagrammed in Fig. 6-45...Ch. 6 - Prob. 1MTE
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