The following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?

The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate facilitate the catalysis of chemical reactions. Which of the following properties of enzyme-substrate interaction best explains enzymatic catalysis according to the induced-fit model? A B с D Environmental conditions can alter the affinity between a substrate and an enzyme by changing the conformation of the enzyme. Conformation changes in both the enzyme and the substrate due to their chemical in- teractions lower the activation energy of the catalyzed reactions. The interactions between an enzyme and a substrate depend on both structural and chemical compatibility and are therefore highly specific. Enzymes remain chemically unaltered between cycles of enzymatic catalysis while sub- strates are transformed into products.

Can you explain the answe?

How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators