Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots:       (a) Is high or low KM preferable for an enzyme reaction? Give reason. (b) Draw the Lineweaver-Burk plot and on the same plot, draw a graph to indicate competitive inhibition. (c) Draw another Lineweaver-Burk plot and on the same plot, draw a graph to indicate non-competitive inhibition.

Q: Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of…

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Q: Using lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?

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Q: What is meant by the catalytic triad? Where is this triad located on the enzyme?

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Q: When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to…

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Q: Graph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction…

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Q: What is the optimal temperature for the enzyme shown above?

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Q: Consider an enzyme that uses general acid-base catalysis such that the reverse protonated form (call…

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Q: (Vmax.f [S] - (Vmax,b [P] KM,b [P] vo [S] 1+ KM.f KM.b ||

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Q: Do all enzymes display kinetics that obey the Michaelis– Menten equation? Which ones do not?

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Q: The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/u) versus the…

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Q: Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.

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Q: 1/V, min/umol 5.50 5.00 4.50 4.00 3.50 answer. 3.00 2.50 2.00 0.00 y = 0.9474x + 2.6649 0.50 1.00…

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Q: Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten…

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