If the enzyme-catalyzed reaction E + S ES E + P is proceeding at or near the V_m

Question

If the enzyme-catalyzed reaction E + S ES E + P is proceeding at or near the V_max of E. what can be deduced about the relative concentrations of S and ES? Please choose from one of the following options. A. [S] is vanishingly low. [ES] is vanishingly low B. S is abundant. [ES] is at its highest point C. S is abundant, [ES] is vanishingly low D. [S] is vanishingly low. [ES] is at its highest point In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect? A. It moves the entire curve to right B. It moves the entire curve to left C. It changes the x-intercept D. It has no effect on the slope What is Kin? A. The concentration of substrate at which v = [S]. B. The amount of substrate consumed per unit time. C. The point on the graph at which half the substrate has been consumed. D. The substrate concentration at which v = 1/2 V_max. What relative values of Km and Kcat would describe an enzyme with a high catalytic efficiency? A. low Km and high Kcat B. high Km and high Kcat C. high Km and low Kcat D. low Kin and low Kcat Molecule 'X' is an enzyme inhibitor that reversibly binds to an enzyme at a site that is distinct from its active Molecule 'X' must NOT be what type of inhibitor? A. Competitive inhibitor B. Noncompetitive inhibitor C. Uncompetitive inhibitor D. Mixed inhibitor

Explanation / Answer

1)C

2)B&C

3)D

4)A

The KM value characterizes the affinity between the substrate and the enzyme. At known KM and Vmax, Vo can be calculated for each value of substrate concentration. A low KM value reflects high affinity.

5)A

In mixed inhibition, the inhibitor binds to an allosteric site, i.e. a site different from the active site where the substratebinds

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