These organic substrates have a [more/less/equivalent] negative free energy of hydrolysis than ATP. In glycolysis, 4 total ATP are produced in this way from a single molecule of glucose in [1/2/4] different enzymatic reactions/steps in the [investment/payoff] phase.
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Substrate level phosphorylation is the spontaneous transfer of phosphate from an organic substrate to ADP. These organic substrates have a [more/less/equivalent] negative free energy of hydrolysis than ATP. In glycolysis, 4 total ATP are produced in this way from a single molecule of glucose in [1/2/4] different enzymatic reactions/steps in the [investment/payoff] phase.
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- In glycolysis, the KM value of hexoquinase is 0.04 mM. At physiological conditions, the cellular concentration of glucose is between 4 mM to 15 mM. According with this information, which of the following statements is true (Choose all that are correct) The enzyme has a low affinity for its substrate The enzme is working at its maximum velocity The phosphorilation of glucose is very slow The small value of KM assures that glycolysis will continue even when the concentration of glucose drops below 4 mM. The hexoquinase is saturated with glucoseThe enzyme phosphofructokinase (PFK) catalyzes the reaction fuctose 6 phosphate and ATP, functions as a tetramer and is regulated by several mechanisms, including allosteric regulation. Based on your knowledge of the homotropic regulation of PFK, draw a curve of the rate of Fructose 1, 6-bisphosphate produced vs. [ATP].Which of the following sequences represents the correct general sequence of oxidative fatty acid catabolism? (1) NAD+ dependent oxidation(2) FAD-dependent oxidation(3) thiolysis(4) hydration Please explain...thanks
- 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?Under aerobic conditions when glucose is limiting, with high ratios of NADH/NAD+ and ATP/ADP, as carbon-2 radiolabeled pyruvate is utilized for its carbon skeleton, which molecules would you expect to see significant radiolabeling in the liver? Select all that apply. **Please note some molecules contain more details, including not only molecule name, but location of the label. Pick the options that are accurate for the above situation. Glucose C-2 only Label is halved over many TCA cycles Oxaloacetate Glucose C-1 and C-6 Glucose C-2 and C-5 CO2 from TCA cycle shows some radiolabel Lactate C-2 for export Malate Pyruvate C-1Taking into consideration glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle, how many substrate level phosphorylation events occur from a single molecule of glucose? 6 substrate level phosphorylation events 4 substrate level phosphorylation events 3 substrate level phosphorylation events 2 substrate level phosphorylation events None of the above answers are correct
- In the living cell, free energy made from one reaction can be used to drive another in an energetically unfavorable direction, provided the two reactions have a common intermediate (this is termed the principle of common intermediates). Example: In glycolysis, glucose is converted into pyruvate; in gluconeogenesis, pyruvate is converted into glucose. However, the actual ΔG for the formation of pyruvate from glucose is about -84 kJ/mol under typical cellular conditions. Most of the decrease in free energy in glycolysis takes place in three essentially irreversible steps catalyzed by, hexokinase, pyruvate kinase and phosphofructokinase. Use one of the 3 opposing reactions (in glycolysis and gluconeogenesis) to demonstrate the PRINCIPLE OF COMMON INTERMEDIATESMost metabolic pathways are relatively long and appear to be very complex. For example, there are 10 individual chemical reactions in glycolysis, converting glucose to pyruvate. Suggest a reason for the complexity.For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DG
- The formation of glutamine from glutamate and ammonium ions requires 14.2 kJ mol-1 of energy input. It is driven by the hydrolysis of ATP to ADP mediated by the enzyme glutamine synthetase. {a) Given that the change in Gibbs energy for the hydrolysis of ATP corresponds to ΔG = -31 kJ mol-1, under the conditions prevailing in a typical cell , can the hydrolysis drive the formation of glutamine? (b) What amount {in moles) of ATP must be hydrolysed to form 1 mol glutamine? (c) Suppose that the radius of a typical cell is 10 μm and that inside it 106 ATP molecules are hydrolysed each second. What is the power density of the cell in watts per cubic metre (1W = 1 Js- 1)? (d) A computer battery delivers about 15 Wand has a volume of 100 cm3 Which has the greater power density, the biological cell or the battery?The regulation of 1-phosphofructokinase occurs primarily by allosteric effectors, including ATP and ADP. Given that phosphofructokinase activity is necessary for glycolysis to proceed, predict what effect ATP would have. How about ADP?phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucitol-1,6-diphosphate. (a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of substrate concentration to show a sigmoidal or hyperbolic curve? (b) How would each of the regulators above affect the dynamics of the T state to R state equilibrium of phosphofructokinase? Briefly explain your reasoning. (c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP, AMP, and 2,5-anhydro-D-glucitol-1,6-diphosphate? Briefly explain your answers.