- wide is a toxic chemical that hinders the production of ATP by inhibiting the enzyme cytochrome Using the graph to explain whether cyanide's inhibition of cytochrome oxidase is competitive or non competitive inhibition. Provide evidence to support your answer. ing the graph below, draw an additional curve on the graph here you would expect the other type of bition to lie and label the lines competitive and non competitive inhibitor. tion -Without Cyanide - With Cyanide Substrate Concentration →
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- You are testing the effects of different molecules on respiration using isolated liver cells that are growing on glucose. For each of the compounds listed below, indicate whether the compound will increase or decrease respiration (measured by monitoring oxygen consumption), and provide reasoning for your answer in two sentences at most. Consider only the early time after the compound begins to exert its effects. a. An inhibitor of the FoF1 ATPase b. A proton channel that enables protons to cross the inner mitochondrial membrane by facilitated diffusion c. An inhibitor of NADH dehydrogenase (complex I of the electron transport chain)this question is about 16 carbon fatty acid A) what are the end procuts of the eight cycles of beta oxidation of a 16 carbon fatty acid? B) assuming 2.5 ATP molecules are produced from one NADH, how many molecules of ATP are produced from the NADH produced during beta oxidation of a 16-carbon fatty acidAll enzymes have an optimal temperature at which they work as well as an optimal pH for their activity. Does this mean that enzymes only work at those specific temperatures and pH optima? Briefly explain your answer and note the evidence provided in this unit that supports your answer.
- The important amino acid residues in the active site of enzyme X were found to be aspartic acid and lysine. In an experiment, the pH of the buffer solution in which enzyme X was dissolved was changed from pH 7 to pH 5. What would be the expected effect of this change on the enzyme’s catalytic activity? A. decrease B. increase C. unchanged D. cannot be determinedQuestion 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…a. Cellular respiration is an energy releasing enzymatically controlled catabolic process which evolves a stepwise oxidative breakdown of organic substances inside living cells. Describe the steps involved in cellular respiration when oxygen is and is not available. In your answer, state the inputs and outputs of yeast cell respiration with and without oxygen. In the yeast respiration experiment, we saw that yeast were able to use sucrose (table sugar) for respiration, but not sucralose (the active ingredient in Splenda). b. b. Explain what these results indicate about how the specific structure of an enzyme affects its function. In your answer, make sure to include the term “active site.” c. c. Explain how you think the results may have differed if the fermentation tubes had been placed in a refrigerator (~4 degrees Celsius) over the duration of the experiment, instead of an incubator set to 40 degrees Celsius, and why. In the photosynthesis experiment with spinach,…
- 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*In living cells, one mole of glucose undergoes a complete oxidation.(a). How many moles of ATP equivalents can be produced when one mole ofglucose is completely oxidized?(b). Indicate at which reaction steps are the ATP equivalents produced,directly or indirectly.Skeletal muscle can store energy in the form of phosphocreatine, which is able to regenerate ATP. In relation to this, answer all of the following: (Show all your work for each part) a) Use your knowledge of bioenergentics to show why this statement is true. b) What is K¢eq for the overall reaction? c) Drawbiochemicalstructuresfortheoverallreaction. d) If the steady-state concentrations of phosphocreatine and creatine in a myocyte (muscle cell) are 1 uM and 129 uM, respectively, what will be the ratio of [ATP]/[ADP], assuming the creatine kinase reaction is at equilibrium?
- Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share the same value for Vmax. Using this information, can you derive conclusions how the km values for enzymes A and B compare to each other?Explain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. All coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement. b. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? c. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer d. Why is penicillin toxic to bacteria but not to higher organisms? e. What is the metabolic basis for the observation that many adults cannot ingest large quantities of milk without developing gastric difficulties?The oxidation of glucose to CO2 and water is a major source of energy in aerobic organisms. It is a reaction favored mainly by a large negative enthalpy change. C6H12O6(s) + 6O2(g) →6CO2(g) + 6H2O(l) ∆H° = -2816 kJ/mol ∆S ° = +181 J/mol . K (a) At 37 °C, what is the value for ∆G°? (b) In the overall reaction of aerobic metabolism of glucose, 32 moles of ATP are produced from ADP for every mole of glucose oxidized. Calculate the standard state free energy change for the overall reaction when glucose oxidation is coupled to the formation of ATP at 37 °C. (c) What is the efficiency of the process in terms of the percentage of the available free energy change captured in ATP?