The kinetics analyses of an enzyme are measured as a function of substrate concentration in the presence and in the absence of 2mM inhibitor (I).
[S] (µM): 3, 5, 10, 30, 90
Velocity (µmol/min) No Inhibitor: 10.4, 14.5, 22.5, 33.8, 40.5
Velocity (µmol/min) With Inhibitor: 4.1, 6.4, 11.3, 22.6, 33.8
(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 Ki of the inhibitor?
(d) Is [S] = 10µM and [I] = 2mM, what fraction of the enzyme molecules have a bound substrate? A bound inhibitor?