Exam 6: The Behavior of Proteins Enzymes

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Which of the following is implied by induced fit between the enzyme's active site and the substrate?

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The rate of a zero-order reaction depends on the _____.

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Which of the following is more likely to inhibit regulatory subunits of an allosteric enzyme?

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Nonenzymatic catalysts enhance the rate of a reaction by factors of _____.

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

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As catalysts, enzymes are

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Generally speaking, a competitive inhibitor and the substrate cannot both bind to the enzyme at the same time.

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Which of the following is not related to the others?

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When the substrate concentration is low, an enzyme reaction

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Which of the following is the most unique about an uncompetitive inhibitor?

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Which of the following is true about lactate dehydrogenase (LDH)?

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Identify a true statement about the enzyme creatine kinase (CK).

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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 K<sub>M</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 K<sub>M</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 KM of the enzyme?

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The KM of hexokinase for glucose = 0.15 mM and for fructose, KM = 1.5 mM. Which is the preferred substrate?

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Thermodynamically favorable reactions all release energy.

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When an enzyme-catalyzed reaction has two substrates and substrate A must bind before substrate B, the mechanism is called

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Which of the following is not true?

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Which of the following is true concerning a ping-pong mechanism?

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For competitive inhibition

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The sign of Gibb's Free Energy is positive ("+") when energy is released.

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