Review Concept 8.4 Enzymes. Match the term and its description. Each term can only be used once. These are nonprotein enzyme helpers. ( Choose ) These inhibitors bind to the active site of an enzyme, | Choose) competing with the substrate to decrease reaction
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- QUESTION 6 Which of the following statements are true about enzyme inhibitors? QUESTION 6 Which of the following statements are true about enzyme inhibitors? A. Competitive inhibitors cause the slope of the Lineweaver-Burk line to change but not the y-intercept. B. Noncompetitive inhibitors are a type of mixed inhibitors. C. Uncompetitive inhibitors result in an alpha equal to 1 and an alpha' not equal to 1. D. Noncompetitive inhibitors result in lines with increasing [I] to share the same x-intercept. all of the above E. All of the above are true.Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3
- Answer TRUE or FALSE.a. According to the lock-and-key model of enzyme action, the active site of an enzyme is not flexible in shape.b. In an enzyme-catalyzed reaction, the compound that does not undergo a chemical change is called the substrate.c. The nonprotein portion of a conjugated enzyme is not the enzyme’s active sited. Simple enzymes are composed only of protein; conjugated enzymes have nonprotein cofactors.QUESTION 1 a. John has just taken his Lunch meal, after which he is going to takes his Daily soccer practice match in the next 30 min, how will glycolysis operate/work in such conditions or be applicable b. How will oxidative phosphorylation work in sickly John who usually practice daily in soccer? Make possible scenarios c. Enzymes are critical in the metabolism of most most organic compounds, actually 30% of reactions are catalysed by them. How would the inactive enzymes (Sickness) in electron Transport Chain compromise the fat breakdown in the body.Question 1: Part a: Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)
- Briefly describe why the Michaelis-Menten equilibrium-assumption cannotbe applicable to all enzyme-catalyzed reactionsSome enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)Question 1: Cytochrome c oxidase actually conserves energy not just by pumping protons from the matrix to cytosol but also by consuming protons from the matrix in production of water. If consumption of a matrix proton has a similar effect on the gradient as pumping a proton (not strictly true but a fair place to start), what would the efficiency of energy conservation be?
- Question:- The enzyme aromatase is found in the cytoplasm of some cells and converts testosterone to estrogen. You decide to test aromatase from a particular cell, and oops, your lab partner admits he drastically increased the pH in all the test tubes. Which of the following is a likely result? a. The enzyme will be denatured and the substrate will not bind to the active site. b. The enzyme will convert testosterone to estrogen at a faster rate. c. The mistake will have no effect on the experiment, because enzymes are not sensitive to pH. d. The free energy will be lowered and the reaction will not proceed spontaneously.Question 6 Give a diagrammatic representation of fatty acid synthase complex and discuss the regulation of fatty acid synthesis.Can you please help me answer the following question in three paragraphs and in your own words. 1. How do you determine the effects of substrate concentration on enzyme activity? (Do not write a procedure just give as many details as possible. Please make sure this is at least in three paragraphs and in your own words).