Finding VMax of hexokinase

Noncompetitive inhibitor can bind to an enzyme with or without a substrate at different places at the same time. It changes the conformation of an enzyme as well as its active site, which makes the substrate unable to bind to the enzyme effectively so that the efficiency decreases. A noncompetitive inhibitor binds to the enzyme away from the active site, altering the shape of the enzyme so that even if the substrate can bind, the active site functions less effectively. Most of the time, the inhibitor is reversible. However, this inhibition decreases the turnover number, meaning the rate of reaction decreases. As the inhibitor binds to the enzyme and the enzyme-substrate complex, it reduces the concentration of enzyme available for proper catalysis. Fewer functional enzymes leads to fewer available active sites and thus a smaller Vmax. Unlike competitive inhibition, raising [ S ] (substrate concentration)is pointless with noncompetitive inhibition.

Based on the Michaelis-Menten Model, KM, the concentration of the substrate when the velocity is the half of the maximum velocity (or half of the substrates at maximum velocity), remains same, but the maximum velocity is decreased.

See attachment

The picture shows a double-reciprocal plot of V0 and [ S ]. The x-intercept is equal to -1/Km while the y-intercept is 1/Vmax. The slope of the line is Km/Vmax. Thus, the plot shows that there is no change in Km and Vmax is decreased. In relation to the original plot, the x intercept stays constant while the y intercept increases along with the slope.