• The intercept on the 1/v axis of a Lineweaver–Burk plot.

• The substrate concentration at v = ½V_max.

• Equal to ½V_max.

• The equilibrium constant for the dissociation of ES to E + P.

• Not changed by the presence of a noncompetitive inhibitor.

No

It is both beneficial and detrimental at the same time

Yes

It does not make any difference

• Inhibiting the rate of reverse reactions.

• Altering the change in free energy of the reaction.

• Changing the equilibrium constant of the reaction.

• Decreasing the energy of activation.

• Selectively enhancing the rate of the forward reaction.

• An enzyme that catalyzes A + B → C + D accelerates the reaction velocity of A + B → C + D, but does not accelerate the reaction velocity of C + D → A + B.

• Enzymes can change the reaction velocity without directly interacting with substrates.

• Enzymes mainly consist of proteins. Coenzymes are small compounds that support the structure of the enzyme, but are not involved in the reaction.

• Enzymes decrease the activation energy of reactions, but do not affect the free-energy change, ΔG.

• Since enzymes catalyze chemical reactions in much the same manner as inorganic catalysts, the higher the reaction temperature, the higher the reaction velocity becomes.

• Dissociation of subunit into oligomeric enzymes.

• Phosphorylation by protein kinases.

• Allosteric regulation by substrates.

• Proteolytic conversion of digestive enzymes.

• Inhibition by competitive inhibitors.