Under standard conditions, is the oxidation of free FADH2 by ubiquinonesufficiently exergonic to drive the synthesis of ATP?
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Under standard conditions, is the oxidation of free FADH2 by ubiquinone
sufficiently exergonic to drive the synthesis of ATP?
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- What is the effect of the mutation on succinate-coupled ATP synthesis?What is the biochemical rationale for ATP serving as a positive regulator of ATCase?a gain-of-expression of MCT1 transporters in pancreatic b-cells wreaks havoc on the cell’s function. To consider this point further, determine the number of ATP that result from complete catabolism of a) 5 lactate and b) 5 b-hydroxybutyrate in aerobic conditions in humans. Assume TCA intermediates are NOT limiting. Use the exact number of c-subunits and the details of the electron transport chain in humans to determine the number of ATP from NADH and FADH2 (not 2.5ATP per NADH and 1.5ATP per FADH2
- Consider the typical beta oxidation of linoleic acid (C18:2 ^Δ9, 12): How many ATP are generated in complete oxidation of linoleic acid? How many NADH are generated in complete oxidation of linoleic acid? How many FADH2 are generated in complete oxidation of linoleic acid?Describe the reactions catalyzed by nucleoside phosphorylase, adenosinedeaminase, and xanthine oxidase.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.
- The enzyme dihydrofolate reductase (DHFR) normally resides in the cytosol, andDHFR can be imported into mitochondria by appending a mitochondrial signalsequence. However, when this modified DHFR is incubated with methotrexate, whichis a substrate analog that binds tightly to the active site, the modified DHFR is nolonger imported.a) Propose an explanation for why methotrexate prevents import of DHFR intomitochondria.b) Suppose that DHFR were modified instead by appending a nuclear localizationsignal. Would you expect methotrexate to prevent transport of this modified DHFRinto the nucleus? Why or why not?The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*a) Based on the mechanism shown in Figure 2A, what type of enzyme is transpeptidase? : Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Transpeptidases have two substrates. From Figure 2A, what type of mechanism do they most likely adopt in processing the two substrates? sequential or ping-pong c) β-lactams inactivate transpeptidases by forming a covalent bond with the serine residue in the active site. Based on this description and Figure 2B caption, what type of inhibitor are β-lactams? _________________________________________ d) Based on the mechanism for lactamase shown in Figure 3, what type of enzyme is lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase e) Based on your answer in d, what other reactant, in addition to the antibiotic substrate, needs to be in the active site of lactamase for the hydrolysis reaction to proceed? ____________________
- What is the stoichiometry of the synthesis of (a) ribose 5-phosphate from glucose 6-phosphate without the concomitant generation of NADPH? (b) NADPH from glucose 6- phosphate without the concomitant formation of pentose sugars?Some bacteria contain three different forms of aspartokinase, each with its own mode of regulation. Based on the roles of aspartoki- nase, as discussed in the text, propose a regulatory scheme applicable to each form of aspartokinase.Explain the Phosphorylation of glycogen phosphorylase by phosphorylase kinase mechanism. What is happening in each step? what are activating nucleophiles and stabilizing intermediates?