Two experiments were conducted with an enzyme following Michaelis Menten kinetics at substrate concentrations of 0.5 g/l and 1 g/l. If the enzymatic reaction velocity increases approximately 2-fold at the higher substrate concentration, the K m for the enzyme would be around:
Answers
Thus, for the graph in Figure 8.11, V0 is determined for each substrate concentration by measuring the rate of product formation at early times before P accumulates (see Figure 8.12). An enzyme E combines with substrate S to form an ES complex, with a rate constant k1. The ES complex has two possible fates.Km is the Michaelis-Menten constant which shows the concentration of the substrate when the reaction velocity is equal to one half of the maximal velocity for the reaction. It can also be thought of as a measure of how well a substrate complexes with a given enzyme, otherwise known as its binding affinity.The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction, Vmax. ... An enzyme with a high Km has a low affinity for its substrate, and requires a greater concentration of substrate to achieve Vmax."