Question

The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor B has an apparent Km of 3.80 μM and an apparent Vmax of 2.00 μM/sec.

Inhibitor B is a(n):

competitive inhibitor.

uncompetitive inhibitor.

mixed inhibitor

allosteric activator.

irreversible inhibitor.

Inhibitor A must be a(n) ________________ inhibitor because ______________.

uncompetitive; the apparent V_max decreases in the presence of Inhibitor A

uncompetitive; the apparent K_m decreases in the presence of Inhibitor A

uncompetitive; both the apparent K_m and the apparent V_max decrease to the same extent in the presence of Inhibitor A

mixed; both the apparent K_m and the apparent V_max decrease, but to different extents, in the presence of Inhibitor A

competitive; the apparent K_m increases but the apparent V_max is unchanged in the presense of Inhibitor A

Answer 1

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