Plot the Gibbs free energy of a catalyzed exothermic reaction over the reaction

coordinate. Label the energies of the products and reactants. Plot superposed what

the uncatalyzed reaction might look like. Show the transition state Gibbs free energy

(∆G‡

) for the uncatalyzed reaction and for the catalyzed reaction (∆G‡

cat). Show also

the changes in Gibbs free energy ∆G and ∆Gcat for the reaction.

Write the chemical equation for enzyme catalysis. Indicate the forward (kf) and

reverse (kr) rate constants for binding and and also the rate constant for catalysis

(kcat).

For the reaction R 

 P, write the differential equation for the reaction velocity,

v, in terms of the concentration of the product, [P].

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Write the Michaelis-Menten equation for enzyme catalysis and define the terms

of the equation.

 What is the rate of an enzyme catalyzed reaction when the concentration of the

substrate is equal to the Michaelis constant, Km.

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Under what conditions does the maximum rate of catalysis for a given enzyme

occur?

The maximum rate of catalysis for a given enzyme occurs when the enzyme is

fully saturated by substrate.

What is the significance of the ratio kcat

Km?