Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Textbook Question
Chapter 18, Problem 25P
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
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Match the letter structures to the given description.
Parts of the mechanism for lysozyme are shown below. The catalytic lysozyme residue side chains can be identified as
being above and below the polysaccharide chain shown at point A. Complete the missing structures (points B and E)
and curly arrows (points A, B, C, D and E) in the mechanism, as well as from the knowledge you have gained, label the
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A
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D
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B
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Within the body, CoQ 10 can be found in an oxidized or reduced form (also known as ubiquinone and ubiquinol). Describe how these structures differ and the biochemical role of coenzyme Q10.
Chapter 18 Solutions
Biochemistry
Ch. 18 - Characterizing Glycolysis List the reactions of...Ch. 18 - Radiotracer Labeling of Pyruvate from Glucose...Ch. 18 - Effects of Changing Metabolite Concentrations on...Ch. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - The Reactions and Meehanisms of the Leloir Pathway...Ch. 18 - The Effect of lodoacetic Acid on the...Ch. 18 - Prob. 8PCh. 18 - Comparing Glycolysis Entry Points for Sucrose...Ch. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Energetic of Fructose-1 ,6-bis P Hydrolysis...Ch. 18 - Prob. 15PCh. 18 - Energetics of the Hexokinase Reaction The...Ch. 18 - Prob. 17PCh. 18 - Distinguishing the Mechanisms of Class I and Class...Ch. 18 - Prob. 19PCh. 18 - Understanding the Mechanism of Hemolytic Anemia...Ch. 18 - Prob. 21PCh. 18 - Based on your residing of this chapter, what would...Ch. 18 - Examine the ActiveModel for alcohol dehydrogenase...Ch. 18 - Based on your knowledge of the structure of NAD+...Ch. 18 - Using the ActiveModel for phosphofructokinase...
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forwardBriefly describe the induced-fit conformational change when hexokinase binds its substrate.arrow_forward. The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized form, whereas the nearby Asp52 must be ionized (see the figure below). The pK values for the side-chain carboxyl groups on the two amino acids in solution are virtually identical. a) How can one carboxyl group be charged and the other uncharged in the active site of lysozyme? b) The pH optimum for lysozyme is about 5. Why do you suppose that the activity decreases above and below this optimum? Glu3s NAG Asp52 0-H Glu35 -C Asp52 tri-NAG NAGarrow_forward
- Consider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.arrow_forwardExplain why the option is correct and others are notarrow_forwardUsing the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.arrow_forward
- Assuming that G6P is labeled at its C1 position, determine where the label will appear in the formed ribulose-5-phosphate from the oxidative stage.arrow_forwardDescribe a common feature at the active site of serine proteases and acetyl cholinesterasearrow_forwardThis question should be answered with two or three sentences using relevant biochemical vocabulary.arrow_forward
- Referring to figure 5 and 8 which substrate molecule serves as the phosphate donor during substrate-level phosphorylation in step 10 of glycosis and the succinyl CoA-succinate step of the Krebs Cycle?arrow_forwardBriefly discuss the synthesis of selenocysteine amino acid.arrow_forwardActivated carriers participate in carbohydrate, peptidoglycan, lipid, and LPS synthesis. Briefly describe these carriers and their roles. Are there any features common to all the carriers? Explain your answerarrow_forward
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