LIFE 210 Lecture Notes - Enzyme Kinetics, Allosteric Regulation, Enzyme Inhibitor
Document Summary
P; at v0 only k1 is significant, v0 = k1 [s] Compare rates or velocities (v0) as it varies with [s] E + s es ep e + p. Km michaelis constant [s] at vmax. Applied m&m kinetics in terms and conditions useful for enzyme comparison. If k2 << k1, km k 1 k1. = kd, measure of e and s affinity (m) Determining the effect of changing active site amino acids. The km for an enzyme catalyzed reaction consistently overestimates the es binding affinity. Two enzyme preparations have the same km, but the bacterially expressed enzyme has a 10- fold lower vmax. The most likely explanation for this is that 90% of the enzyme expressed in bacteria is inactive. If you were to design an enzyme for a cell, you would give it a km near the normal cellular substrate concentration to make the enzyme activity responsive to changes in cellular substrate concentrations.
