Choose reaction #6 or #10 in glycolysis and write out the complete reaction. Then, answer the following questions about this reaction. Explain your reasoning for each answer. a. Is it coupled? b. Is it catalyzed by a transferase or an oxidoreductase or neither? c. Is Q > or < or ≈ to K?
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Chemistry
Choose reaction #6 or #10 in glycolysis and write out the complete reaction. Then, answer the following questions about this reaction. Explain your reasoning for each answer.
a. Is it coupled?
b. Is it catalyzed by a transferase or an oxidoreductase or neither?
c. Is Q > or < or ≈ to K?
Step by step
Solved in 2 steps
- 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?Is Reaction #3 favorable under mammalian cellular conditions when the concentration of dGTP is 0.2 M, dCMP is 20 mM, dGMP-dCMP is 7 mM, and PPi is 10 mM? Use △G to support your answer. Show your work and clearly label your final answer.Effects of Changing Metabolite Concentrations on Glycolysis In an erythrocyte undergoing glycolysis what would be the effect of a sudden increase in the concentration of a. AΤP? b. AMP? c. fructose-1.6-bisphosphate? d. fructose-2, 6-bisphosphate? e. citrate? f. glucose-6-phospthate?
- Chemistry List the reversible and irreversible steps in glycolysis. For each of them, provide an approximate value of (nonstandard) free energy change. Explain why glycolysis is a favorable process overallEnzyme A catalyzes the reaction below. Which enzyme in the glycolysis lectures you learned so far catalyzes a similar reaction as enzyme A? Based on the reaction mechanism you learned, draw out the arrow-pushing reaction mechanism including crucial intermediates for the reaction below catalyzed by enzyme A.If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
- PART IV. HOW FAST DOES IT GO?Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. A. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor. B. If GAPDH is inhibited, what specific type of inhibition is observed?a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzymeChemistry 1. Explain why gluconeogenesis is NOT just a reversal of glycolysis.2. Briefly but comprehensively discuss the purpose of the hexose monphosphate shunt, and explain the relationship to this pathway and the aetiology of gout. please include pictures if you can. Thank you!
- You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!a. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.DCCD (diocyclohexylcarbodiimide) inhibits oxidative phosphorylation when the substrate is mitochondrial NADH. DCCD is a drug that binds to ATP synthase and blocks proton transport through the ion channel. a) Explain what the consequences of DCCD on cellular energy production are. b) Suggest at least one other cellular effect of DCCD and explain this effect.