Define the transition-state of reaction. The Michaelis-Menten equation gives a rate expression for a simple enzymatic reaction. State the assumptions in the derivation of the MM equation. Calculate the rate of reaction given the substrate concentration and other kinetic parameters. Compare two enzyme reactions with different K m and V max values by drawing their v vs. S plots.
Enzymes often catalyze reactions with two substrates and two products.
Define three types of common mechanisms for two substrate - two product reactions. Enzymes are inhibited by competitive and non-competitive types of inhibitors. K m and V max vary with each of these inhibitor types. Predict whether inhibitor effects are overcome by changes in substrate concentration. Predict the changes in v vs. S plots and Lineweaver-Burk plots in the absence and presence of various types of inhibitors.