Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 18, Problem 25P
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
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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)
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A
OH
R
OH
O-R
H₂C-
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NHAC
E
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D
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B
R
C
H
RO
H3C-
°
H₂C-
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R
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R
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.
Briefly describe the induced-fit conformational change when hexokinase binds its substrate.
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_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_forwarduizzes/67365/take Based on the image below, select the correct statements. Note: There may be more than 1 correct response. I Ribose 5-phosphate ribose phosphate pyrophosphokinase (PRPP synthetase) glutamine-PRPP amidotransferase adenylosuccinate synthetase AMP > 5-Phosphoribosylamine I adenylosuccinate PRPP lyase 9 steps Adenylosuccinate AMP IMP <-- ADP - AMP <-- GMP <-- IMP IMP dehydrogenase <- GMP - XMP ADP ATP GMP يمد XMP-glutamine amidotransferase Increased levels of ADP inhibit the production of PRPP. Increased levels of GMP inhibit the production of XMP. O Increased ADP activates PRPP synthase to increase PRPP levels. Increased IMP activates glutamine-PRPP amidotransferase to further increase IMP levels. 8 OBCarrow_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_forwardLysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many) products. List, in order, the reactants that bind and the products that are released during a lysozyme-catalyzed reaction cycle -- be succinct but be specific. 1. First reactant = 2. First product = 3. Second reactant = 4. Second product %3Darrow_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_forwardthe following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.arrow_forwardConsider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). II. What is the net ATP yield for the complete oxidation of all the fatty acid residues of the simple TAG? (Note: glycerol backbone is not included)arrow_forward
- Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. What is the number of ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residuearrow_forwardWe talked about the types (mechanisms) of catalysis, including acid-base catalysis, covalent bond formation, metal ion stabilization, and nucleophile attacks of reactants/intermediates following substrate binding. Using the SN2 mechanism for Peptidoglycan cleavage by Lysozyme, indicate the type of catalysis that each of these groups are taking part in. Provide your answers in the thread. Note: this is not part of the assignments for Friday. i. Glu35 ii. Asp52 iii. H2Oarrow_forwardSketch curves for reaction velocity versus [fructose-6-phosphate] for the phosphorylated and nonphosphorylated forms of PFK-2 in liver.arrow_forward
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