Question text Edrophonium inhibits the enzyme, acetylcholinesterase. Which of the following changes in Vmax and Km of acetylcholinesterase are MOST LIKELY to occur in the presence of edrophonium? Multiple choice 1 Question 8increase in Km, decrease in Vmaxdecrease in Km, no change to Vmax increase in Km, no change to Vmaxdecrease in Km, decrease in Vmax Edrophonium binds to acetylcholinesterase leading to: Multiple choice 2 Question 8rapid hydrolysis of acetylcholine.ionic bond formation at the anionic site.covalent modification of the catalytic site.slow cleavage of the serine-OH site. Which one of the following could be relieved by edrophonium? Multiple choice 3 Question 8bradycardiadiarrhoeabronchoconstrictiondroopy eyelids多项填空题
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Question text SECTION A: ENZYMATIC REACTIONS This section contains a total of 7 marks. You should allow 7-10 mins to answer the questions in this section. Jeroen is an honours student working in the La Trobe Institute for Molecular Sciences. He is testing the efficacy of a new compound "X" that he hopes inhibits the activity of the enzyme he is interested in, Lockdownase. He conducts a Michaelis-Menten assay where his enzyme, Lockdownase, is incubated in the presence of increasing concentrations of substrate, with a constant concentration of inhibitor X. He obtains the following Lineweaver-Burk plot: Using the data above, answer the following questions (1 mark each): Q1. A. Calculate the Km for the enzyme alone (give your answer to 3 decimal places). Answer 1 Question 1[input] Q2. Calculate the Kmfor the enzyme + inhibitor (give your answer to 3 decimal places). Answer 2 Question 1[input] Q3. Calculate the Vmax for the enzyme alone (give your answer to 3 decimal places).Answer 3 Question 1[input] Q4. Calculate the Vmax for the enzyme + inhibitor (give your answer to 3 decimal places).Answer 4 Question 1[input] Q5. What is the type of inhibitor used in this experiment? Answer 5 Question 1[select: , Competitive, Irreversible, Uncompetitive, Covalent] Q6. What would you alter in the reaction mixture to increase the activity of enzyme back to normal levels (i.e. to before compound X was added) even in the presence of the inhibitor? Answer 6 Question 1[input] Q7. Which of the following conditions are important to keep constant when measuring enzyme activity? Select all that apply.pHvolumetemperatureoxygen levels Ensure that you have entered and checked all your answers before pressing "Next page" as you will not be able to return to this page and these questions.
Which of the following statements about V0, Vmax, [S] and Km values is not true?
The Vmax of an enzyme is:
Is the following statement true or false?'There is an inverse relationship between the Km and an enzyme’s affinity for its substrate'.
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