What is the relationship between a transitionstate analog and the induced-fit model of enzyme kinetics?
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Q: Why is the overall coupled reaction exergonic?
A: The coupled reaction like a redox reaction which is coupled or combined.
Q: Can the Rate of an Enzyme-Catalyzed Reaction Be Defined ina Mathematical Way?
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Q: Graphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed…
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Q: What Role Does Transition-State Stabilization Play inEnzyme Catalysis?
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Q: What is the difference between the lock-and-key model of enzyme action and the induced-fit model?
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Q: Why do most enzyme reactions slow down at extremely high temperatures?
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Q: Do all enzymes display kinetics that obey the Michaelis– Menten equation? Which ones do not?
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Q: Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to…
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Q: Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme…
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Q: What are the two types of enzyme inhibitors? Give anexample of each.
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Q: How do an activator and an inhibitor have differenteffects on an allosterically regulated enzyme?
A: ALLOSTERIC REGULATION:- The site beside the active site certain enzymes possess site for attachment…
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Q: Calculate the specific activity and kcat for this enzyme
A: Enzymes are catalyst that speed up the biochemical reaction by lowering the activation energy of the…
Q: Why can’t enzyme kinetics prove that a particular enzyme mechanism is correct?
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Q: at is the difference between enzyme limited and a substrate limited reaction?
A: Enzymes are substances that are mainly protein which acts as biocatalysts in living organisms and…
What is the relationship between a transitionstate analog and the induced-fit model of enzyme kinetics?
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- What is the difference between the lock-and-key model of enzyme action and the induced-fit model?Do all enzymes display kinetics that obey the Michaelis– Menten equation? Which ones do not?In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of enzyme action?
- Several factors contribute to enzyme catalysis. What arethey? Briefly explain the effect of each.If you want to determine the KM for lactate, what protocol do you set up? Discuss the significance of the following kinetic parameters that are used to characterize enzyme activity: KM, Vmax, kcat, and kcat / KM.What are the three most common mechanisms for enzymecatalyzed reactions that have two substrates?
- 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 Role Does Transition-State Stabilization Play inEnzyme Catalysis?In enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.
- Graphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed reaction proportional to the amount of E.S complex?How to identify the Vmax and the Michaelis constant (Km) in an enzyme kinetics graph?Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)