Exam 6: The Behavior of Proteins Enzymes

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What effect is seen on a Lineweaver-Burk graph when a competitive inhibitor is added?

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The initial rate of an enzymatic reaction is usually determined in order to assure that

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If an inhibitor changes the slope of the Lineweaver-Burk graph, but not the x-intercept, it is this type of inhibition:

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The order of a reaction can be determined from the balanced equation for the reaction.

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Exhibit 6A This is a reaction going on in your muscle cells right this very minute: Exhibit 6A This is a reaction going on in your muscle cells right this very minute:   The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics:   Typical cellular concentrations: triose phosphate isomerase = 0.1 nM Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM Refer to Exhibit 6A. What is the V<sub>max</sub> of the enzyme? The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics: Exhibit 6A This is a reaction going on in your muscle cells right this very minute:   The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics:   Typical cellular concentrations: triose phosphate isomerase = 0.1 nM Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM Refer to Exhibit 6A. What is the V<sub>max</sub> of the enzyme? Typical cellular concentrations: triose phosphate isomerase = 0.1 nM Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM Refer to Exhibit 6A. What is the Vmax of the enzyme?

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In the reaction catalyzed by aspartate transcarbamoylase, a graph in which the rate is plotted against the concentration of substrate

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A rate constant is

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Pure noncompetitive inhibition is a limiting case of

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What effect is seen on a Lineweaver-Burk graph when a non-competitive inhibitor is added?

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If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec\millimole) and the slope = 75.3 L\sec, KM equals:

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The Michaelis constant is

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Given the rate law, rate = k[A][B], the overall reaction order is

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If an inhibitor changes the slope of the Lineweaver-Burk graph, but not the y-intercept, it is this type of inhibition:

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What effect does a catalyst have on the Δ G ° of a reaction?

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First order kinetics means

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The steady state of an enzyme reaction is the following:

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What effect is seen on a Lineweaver-Burk graph when a mixed-type inhibitor is added?

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When an enzyme is saturated with substrates,

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Competitive inhibitors have this effect:

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The substrate-enzyme (E-S) complex

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