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(a) What are the values of Vmax and KM in the absence of inhibitor? In its
presence?

(b) What type of inhibition is it?

(c) What is the binding constant of this inhibitor?

(d) If [S] = 10 M and [I] = 2 mM, what fraction of the enzyme molecules have a
bound substrate? A bound inhibitor?

(e) If [S] = 30 M, what fraction of the enzyme molecules have a bound substrate in
the presence and in the absence of 2 mM inhibitor? Compare this ratio with the
ratio of the reaction velocities under the same conditions.

(a) In the absence of inhibitor, Vmax is 47.6 mol minute-1, and KM is 1.1 10-5 M.
In the presence of inhibitor, Vmax is the same, and the apparent KM is 3.1 10-5
M.

(b) Competitive.

(c) 1.1 10-3 M.

(d) fES is 0.243, and fEI is 0.488.

(e) fES is 0.73 in the absence of inhibitor and 0.49 in the presence of 2 10-3 M
inhibitor. The ratio of these values, 1.49, is the same as the ratio of the reaction
velocities under these conditions.