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- Study Figure 19.18 and decide which of the following statements is false. Pyruvate dehydrogenase is inhibited by· NIADH. Pyruvate dehydrogenase is inhibited by AΤΡ. Citrate synthase is inhibited by NADH. Succinyl-CoA activates citrate synthase. Acetyl-CoA activates pyruvate carboxylase.Glucose is converted to pyruvate in glycolysis, yielding a netsynthesis of 2 ATP. In certain cells pyruvate can be reconverted to glucose during gluconeogenesis. How many ATPsare required to convert pyruvate back to glucose?During gluconeogenesis, the three irreversible steps of glycolysis have to be bypassed. The first step is the conversion of pyruvate to phosphoenolpyruvate. Which of the following statement is false regarding the reaction step? Select one: a. Conversion of oxaloacetate from pyruvate occurs in mitochondria and shuttled into the cytosol. b. Formation of phosphoenolpyruvate requires both ATP and GTP as an energy source. c. Acetyl CoA is an activator of enzyme pyruvate carboxylase. d. This reaction involves two-step process catalyzed by pyruvate carboxylase and phosphoenolpyruvate carboxykinase
- 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 INTERMEDIATESIn 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 glucoseOne consequence of ethanol addiction is fatty liver disease, an illness in which liver cells accumulate large amounts of triacylglycerols, the esters derived from glycerol and fatty acids. Ethanol is oxidized in the cytoplasm of liver cells by alcohol dehydrogenase and aldehyde dehydrogenase to yield acetate and 2 NADH. Acetate is then transported into the mitochondrion, where it is converted to acetyl-CoA and metabolized in the citric acid cycle. When alcohol is consumed in excessive quantities, the resulting high levels of NADH cause metabolic abnormalities, one of which is high levels of fatty acid synthesis. Fatty acid synthesis, also a cytoplasmic process, uses acetyl-CoA as a substrate and NADPH as a reducing agent. Speculate about how a high level of cytoplasmic NADH provides a source of NADPH for fatty acid synthesis.
- If glucokinase has a higher Km for glucose than does hexokinase, but can only bind to D-glucose, while hexokinase can bind to several hexose sugars (like D-glucose, D-mannose, and D-fructose), then: glucokinase has both a higher affinity and a higher specificity for D-glucose than does hexokinase glucokinase has both a lower affinity and a lower specificity for D-glucose than does hexokinase glucokinase has a higher affinity but a lower specificity for D-glucose than does hexokinase glucokinase has a lower affinity but a higher specificity for D-glucose than does hexokinase all of the aboveUnder 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-1In the last step of glycolysis, phosphoenolpyruvate (PEP) is converted to pyruvate and during this reaction ATP is synthesized. Based on the fact that ATP is synthesized, which of the following enzymes would most likely catalyze this reaction? a. enolase b. pyruvate kinase c. aldolase d. pyruvate isomerase e. pyruvate dehydrogenase
- One of the consequences of ethanol addiction is fattyliver disease, an illness in which liver cells accumulatetriacylglycerols, the esters derived from glycerol and fattyacids. Ethanol is oxidized in the cytoplasm of liver cells byalcohol dehydrogenase and aldehyde dehydrogenase to yieldacetate and 2 NADH. Acetate is then transported into themitochondrion, where it is converted to acetyl-CoA andmetabolized by the citric acid cycle. When alcohol is consumed in excessive quantities, the resulting high levels ofNADH cause metabolic abnormalities, one of which is highlevels of fatty acid synthesis. Fatty acid synthesis, also acytoplasmic process, uses acetyl-CoA as a substrate andNADPH as a reducing agent. Determine how a high level ofcytoplasmic NADH provides a source of NADPH for fattyacid synthesis.The completion of one cycle of the citric acid cycle oxidizing one acetyl CoA results in net... Group of answer choices 2 ATP produced consumption of 1 molecule of citrate consumption of 1 molecule of oxaloacetate production of 2 CO2 Which of the following is not a component of the citric acid cycle? Group of answer choices Oxaloacetate Succinyl CoA Malate Pyruvate Which of the following enzymes catalyzes an anaplerotic reaction? Group of answer choices citrate synthase pyruvate dehydrogenase complex malate dehydrogenase pyruvate carboxylasephosphofructokinase 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.
