referred to feedback inhibition as “Goldilocks regulation”.  Describe how feedback inhibition keeps a pathway running at just the right level?

Which statement is true about noncompetitive inhibition? a. Binding of the inhibitor occurs to the active site of the enzyme b. Inhibition is irreversible  c. Increasing the amount of substrate does not reverse the inhibition  d. We talked about it in context of aspirin inhibiting blood clotting

Give typing answer with explanation and conclusion If an enzyme was extracted from a mammal versus a freshwater trout from a mountain stream, what differences in functional rage and optimal temperature would you expect?

Give typing answer with explanation and conclusion

Explain why using higher concentration of substrate does not produce a significant change in the rate of a chemical reaction after a certain point.

Explain why using higher concentrations of substrate does not produce a significant change in the rate of a chemical reaction after a certain point.

A single polypeptide chain houses the transferase and debranching enzyme. Cite a potential advantage of this arrangement.

Bonus: You use a drug to inactivate all of the kinases inside of an animal cell that is actively undergoing mitosis Part 1: What category of receptor would be directly affected? (one word answer) Part 2: Would this drug directly disrupt the enzymatic activity of a phosphatase? Briefly explain why. Part 3: Would this drug impact a phosphorylation cascade? Briefly explain why.

You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place.  Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place.  Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.

Which phrase characterizes a uncompetitive inhibitor? OA. binds either enzyme or enzyme-substrate complex when present, Km of an enzyme will appear to decrease OB. when present, Km of an enzyme will either increase or decrease when present, Km of an enzyme will appear to increase OD.