Draw cartoon representations showing each of the following 3 types of inhibition: competitive, noncompetitive, and irreversible. Then look up Allopurinol, a medicine used to treat gout, and explain what type of inhibition it causes. Please attach actual drawings.
Q: -Inhibitor +Inhibitor [S] (mM) V&ν βσπ:(μmol/sec) ν0&νβσπ: &νβσπ: (μmol/sec) 0.0001 33 17 0.0005 71…
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Q: State and describe the three different types of inhibitors. short answer please.
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Q: Why does the apparent KM decrease in the presence ofan uncompetitive inhibitor?
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Q: Draw and label the Lineweaver–Burk, Plots for each type of inhibitor.
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- Batrachotoxin identify the species which releases the toxin (if it is man-made then this will be all that is required for this part) identify the step disrupted in the neuromuscular junction pathway Provide any consequences of this disruption. Does the toxin have any applications in biomedicine as a painkiller, disease treatment or analgesic? Please provide sources in APA formatProteases are one of the main drug targets. Choose the False statement regarding proteases. A. Proteases are enzymes that cleave peptide bonds. B. Water is a reactant in the reaction catalyzed by proteases. C. Proteases, like all enzymes show substrate specificity, meaning they cleave only substate that fit the bonding product. D. Proteases rely on the proton transfer from NADH to the substrate. E. Protease mechanism involves only acid-base catalysis.graph the data from the table after taking recipocals of [S], V without inhibitor and V with inhibitor. It should be Lineweaver - Burke. use graph paper or excel. however upload graph and answers as 1 document as jpeg, pdf, or word. there should be 2 lines on 1 graph and both lines should cross the Y axis and hit the X axis (negative X axis). label both axes, determine Km and Vmax (show work) in the presence and absence of inhibitor State type of inhibition and if inhibitor resembles the substrate or not. can more substrate relieve the inhibition? [S] (UM) 3 10 30 5 90 Velocity (umol minute-¹) No inhibitor 10.4 14.5 22.5 33.8 40.5 Inhibitor 4.1 6.4 11.3 22.6 33.8
- Answer the following using the picture attached: A. How does pepsin differ from chymotrypsin in terms of its active site residues and mechanism? B. How do these changes permit pepsin to operate at such a low pH?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?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.
- In a Lineweaver-Burk plot of an enzyme inhibited with a competitive inhibitor, how does the plot change with increasing inhibitor concentration? a) the slope decreases and the y-intercept stays the same b) the slope increases and the y-intercept stays the same c) the slope decreases and the y-intercept increases d) the slope increases and the y-intercept descreases e) none of the aboveCan you please help me answer this question: