Calculate the rate enhancement that could be accomplished by an enzymeforming one low-barrier hydrogen bond with its transition state at 25°C.
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Calculate the rate enhancement that could be accomplished by an enzyme
forming one low-barrier hydrogen bond with its transition state at 25°C.
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- An uncatalyzed reaction has keq=50. in the presence of an appropriate enzyme.the forward rate of the reaction increased by 20-fold.what is the equilibrium constant in the presence of the enzyme?Calculate the factor by which the enzyme will decrease the rate of the reaction with the following information. ES complex releases 30kj/mol of binding free energy that lowers the activaiton energy barrier needed for the transition state.Student conducting research observe the rate of an enzyme-catalyzed reaction under various conditions with a fixed amount of enzyme in each sample. When will increasing the substrate concentration likely result in the greatest increase in the reaction rate?
- Students conducting research observe the rate of an enzyme-catalyzed reaction under various conditions with a fixed amount of enzyme in each sample. When will increasing the substrate concentration likely result in the greatest increase in the reaction rate?name and explain the model that most likely accounts for cooperativity in enzymeNADH Also indicate why this is the most likely model.At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
- At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIIExplain and differentiate the lock-and-key and induced fit models for binding of a substrate to an enzyme. If only a few of the amino acid residues of an enzyme are involved in its catalytic activity, then why does the enzyme need such a large number of amino acids?
- Calculate the numerical relationship between KM and [S] when a reaction enzymatically catalyzed reaches 80% of Vmax.2c which is altered by a catalyst such as an enzyme, the net free energy change of the reaction or the activation energy of the reaction?calculate the turnover number for an enzyme, assuming Vmax is 0.5M.sec-1 and the concentration of the enzyme used is 0.002M . why is it usefull to know this?