What effect does a negative effector have on the graph of reac- tion rate (V) vs. [substrate] for an allosteric effector?
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- CYP2E1 has a much higher Km for ethanol than ADH (11 mM versus 0.05 mM,respectively). When greater portions of ethanol are ingested (0.08% or 17 mM), which part of the statement would be true?Under what conditions can we assume that KM indicates the binding affinity between substrate and enzyme?If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
- What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compareIf you were to remove the ER retrieval signal (KDEL) from protein disulfide isomerase (PDI), which is normally a soluble resident of the ER lumen, where would you expect the modified PDI to be located? Why?
- Below is a plot of Vo vs. [S] for a specific allosteric enzyme under different conditions. Which of the following best describes the graph? 4 (S] O Adding a positive modulator to #2 would result in curve 3. Curve 1 represents maximum inhibition. Line 4 is valid exclusively for curves 1 and 2. Adding a positive modulator to #1 would result in curve 2. O Curve 3 represents the effect of a negative modulator added to curve 2.Which arrestin is required for activation of phosphorylation of MDM2 during chronic Iso stimulation? use the following Figures 1and 2 respectively to explain pleaseIf the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible?
- If intracellular [ATP] = 5 mM, [ADP] = 0.5 mM, and [Pi] = 1.0 mM, calculate the concentration of AMP at pH 7 and 25°C under the condition that the adenylate kinase reaction is at equilibrium.O Att Intestinal epithelial cells pump glucose into the cell against its concentration gradient using the Nat-glucose symporter. Recall that the Nat concentration is significantly higher outside the cell than inside the cell. The symporter couples the "downhill" transport of two Nat ions into the cell to the "uphill" transport of glucose into the cell. If the Nat concentration outside the cell ([Na lout) is 161 mM and that inside the cell ([Na* Jm) is 17.0 mM, and the cell potential is -50.0 mV (inside negative), calculate the maximum energy available for pumping a mole of glucose into the cell. Assume the temperature is 37 °C. What is the maximum ratio of (glucose] to [glucoselout 10.62 kJ AG gluc mol that could theoretically be produced if the energy Incorrect coupling were 100% efficient? O 1.13 8.24 3800 2.6 x 10 IncorrectAn enzyme that follows the MWC (concerted) model for allostery has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation were to reverse that ratio (T/R = 1/300 = 3.3 x 10–3 in the absence of any substrate). How would this mutation affect the relation between the rate of the reaction and substrate concentration, i.e., what would a Vo vs. [S] plot look like, and why?