The following data were obtained in a study of an enzyme known to follow Michael

Question

The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: The K_m for this enzyme is approximately: A) 1 mM. B) 1000 mM. C) 2 mM. D) 4 mM. E) 6 mM. To calculate the turnover number of an enzyme, you need to know: A) the enzyme concentration. B) the velocity of the catalyzed reaction at [S] >>K_m. C) the velocity of the catalyzed reaction at low [S] D) the K_m for the substrate. E) both A and B. The concept of "induced fit" refers to the fact that: A) enzyme specificity is induced by enzyme-substrate binding. B) enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. C) enzyme-substrate binding induces movement along the reaction coordinate to the transition state. D) substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. E) when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate. A small molecule that decreases the activity of an enzyme by binding to a site other than the catalytic site is termed a(n): A) allosteric inhibitor B) alternative inhibitor. C) competitive inhibitor. D) stereospecific agent. E) transition-state analog. Fill in the blanks using the word bank given. Each question carries one point. 1) When the rate of reaction is completely independent of the concentration of the reactants, it is called a 2) The _____ model of enzyme-substrate binding has been proven to be incorrect and the newer _____ model is more correct.

Explanation / Answer

Answer 8: E) both A and B. (Explained as below)

Vmax = Kcat x Enzyme concentration

So, Kcat = Vmax / Enzyme concentration = turnover number

Answer 9: D) Substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. (Explained as below)

The concept of induced fit forces the enzyme to change its shape.

Answer 10: C) allosteric inhibitor. (Explained as below)

Allosteric inhibition of non-competitive type is capable of binding to site other than the catalytic site.

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