draw 3 allosteric enzyme curves for glycogen synthesis in the presence of high AMP, high NADH, and no regulators on 1 graph.
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- draw allosteric enzyme curves comparing beta oxidation and fatty acid synthesis in the presence of high AMP and high acetyl CoA, and no regulatorsThe mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer the following questions related to chymotrypsin: 1. List the 3 amino acids in the catalytic triad of chymotrypsin. 2. List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
- Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limitingMake tables of reactions of the Glycolysis and Gluconeogenesis with enzyme names and DGo’ values. I provided a template for the table below. With this information, determine the overall free energy of each pathway. Discuss the differences in these values and suggest a reason for this difference. Please answer very soon will give rating surelyImagine you make a mutation to an enzyme and determine that you have strongly stabilized the ES complex. the stability of the EX‡ is unchanged. Draw the expected reaction free energy coordinate for the original enzyme (solid line) and the mutated enzyme (dashed line). Do you expect this mutation to have an effect on the rate of product formation? If so, what is the effect?
- The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.The free energy change of each step of glycolysis is given in the table below. ∆G°’ is the free energy under standard conditions (25°C, 1M each reactant, pH 7), while ∆G is the free energy change at presumed physiological conditions. Why must no step have a positive ∆G under physiological conditions?Enzyme X and enzyme Y catalyze the same reaction and exhibit the νo versus [S] curves shown below. Which enzyme is more effi cient at low [S]? Which is more effi cient at high [S]?
- 1 = 2, for sufficiently large values of 1. The energetic equivalent of two molecules of ATP is used to activate an amino acid, yet only one molecule of ATP is used. ExplainIn enzyme catalysed reactions, the energy level of the enzyme/substrate (or ES) complex is higher (or raised) compared to the uncatalyzed reaction. List 4 factors that contribute to this raised energy level and explain how each of these factors contribute to the higher energy level of the ES complexa. 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.