The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.
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The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibitionMany 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.
- For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?Explain 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.Why can’t an enzyme use an induced fit mechanism to achieve catalytic perfection?
- The covalent catalytic mechanism of an enzyme depends on a single active site Cys residue with a pKa of 8.0. A mutation in a nearby residue alters the microenvironment such that the pKa of the Cys residue increases to 10.2 Would the mutation cause the reaction rate to increase or decrease? Explain.Would 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.why is biocatalysis over inorganic catalysts in enzyme catalysis favored?
- Would you expect an “enzyme” designed to bind its target substrate as tightly as it binds the reaction transition state to show a rate enhancement over the uncatalyzed reaction? In other words, would such protein be a catalyst? Use a reaction energy diagram to explain why or why not.The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pKa is 8. A mutation in a nearby residue alters the microenvironment so that this pKa increases to 10. Would the mutation cause the reaction rate to increase or decrease? Justify your answer.In the absence of substrate, an allosteric enzyme that follows the concerted model has a T/R ratio of 300. Assume the ratio was inverted as a result of a mutation. What effect would this mutation have on the relationship between reaction rate and substrate concentration?