Many early attempts at enzyme engineering tried to design so-called catalytic antibodies. This strategy was used to create an antibody whose antigen was a transition state analogue of the reaction to be catalyzed. Why was this a sound strategy for engineering a biocatalyst?
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7) Many early attempts at enzyme engineering tried to design so-called catalytic antibodies. This strategy was used to create an antibody whose antigen was a transition state analogue of the reaction to be catalyzed. Why was this a sound strategy for engineering a biocatalyst?
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- why is biocatalysis over inorganic catalysts in enzyme catalysis favored?A TAMU undergraduate biochemistry student is tasked with characterizing a new enzyme. After devising an assay, the student does some initial experiments. When initiating the reaction by adding the enzyme to a solution of substrates (but no products) she finds that at the earliest times the change in the [A] is non-linear and increasing and then becomes linear for awhile and then decreases eventually to zero. Explain what is unusual and what various aspects of the time course mostly likely means.Why can’t an enzyme use an induced fit mechanism to achieve catalytic perfection?
- Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.What features distinguish enzymes that undergo allosteric control from those that obey Michaelis-Menten equations? Give 2 differencesWould you expect an “enzyme” designed to bind to its target substrate astightly as it binds the reaction transition state to show a rate enhancementover the uncatalyzed reaction? In other words, would such a protein actuallybe a catalyst? Explain why or why not.
- Many isolated enzymes, if incubated at 37°C, will be denatured. However, if the enzymes are incubated at 37°C in the presence of substrate, the enzymes are catalytically active. Explain this apparent paradox.Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.You have been researching two additional methyltransferase enzymes that catalyze the same reaction. At a concentration of 10 nMoles enzyme, Enzyme A has a Km of 60 mmol, while Enzyme B has a Km of 2 mmol for the reaction conditions. You have two solutions (A and B) with equal amounts of Enzyme A in tube A and Enzyme B in tube B respectively. They both have the same Vmax of 500 mmol/second. Which enzyme would have a higher reaction velocity with the substrate concentration of 30 mmol? Why? Give approximate reaction velocity values for each enzyme (mmol/s) Would this result change if the substrate was 1000 and 1,000,000 mmol? Explain why, and give approximate reaction velocity concentrations. An irreversible inhibitor has been added to the reaction mixes A and B. It binds with 100% affinity for Enzyme A, but does not bind to Enzyme B. If 5 nMoles of inhibitor is added to the reaction, what would happen to the apparent Km and Vmax of Enzyme A and B?
- Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and referenceExplain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.How can you recognize an enzyme that does not display Michaelis–Menten kinetics?