Given the active site diagram below, indicate the mechanism(s) of catalysis.

In a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?

Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs and equations in illustrating the different modes of action of enzyme inhibitors.

Can you explain the following based on its mode of enzyme kinetics:  1) Synthesis/degradation of enzymes 2) Allosteric regulation  3) Covalent modification

"Enzymes that undergo cooperative allosteric transitions invariably consist of symmetric assemblies of multiple subunits" is true or false.

Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes

What is the defining characteristic for an enzyme catalyzing a sequential reaction? A doubledisplacement reaction?

Why can’t an enzyme use an induced fit mechanism to achieve catalytic perfection?

Catalysis involves overcoming the activation energy barrier of a reaction. What are three ways by which enzymes can do this?

Allosteric activators block the active site, so the enzyme cannot bind True Or False