What type of inhibition is occurring when the end product stops the action of the first enzyme in the video on feedback inhibition found below: https://www.youtube.com/watch?v=qHb7iieM2Ro  Select one: a. competitive b. non-competitive c. Both competitive and non-competitive inhibition are illustrated in this video/figure

Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs and equations in illustrating the different modes of action of enzyme inhibitors.

In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm

A newly developed drug is suspected to act by inhibiting its enzymatic target. To test this, the rates of reaction in the presence and absence of the new drug were determined. The results of these experiments have been plotted as a double reciprocal plot shown in figure 1 below.    Using this figure, calculate the values of Vmax and Km for the enzyme in the presence and absence of the drug. 2. Based on the figure and your answer, what type of inhibition is the new drug displaying?   3. Briefly explain how this type of inhibition exerts its action on an enzyme. Figure 1: Double reciprocal plot of reaction rate against substrate concentration in the presence and absence of a new drug.

Knowing that for a bacterial colony to be able to grow it must produce product "3" AND "4", use the information in the image to describe which enzyme(s) are that are Non-Functional in Colony C? Please note error in enzyme description at bottom of image. X converts 1 into 2; Y converts 1 into 3; and z converts 2 into 4.

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.

Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes

Can you please help me answer this question:

Which type of potato do you think would be the best source of obtaining tyrosinase; a normal white potato or a sweet potato? Consider all the factors that might go into this decision (total amount of the enzyme, the enzyme activity and its specific activity). Give a brief description of your reasoning.