whoa whoa. The DAT will not go over enzyme kinetics in detail, such as michaelis-menten equation etc. Just know that it does not alter the equilibrium constant, you just get there faster and the point where it reaches Vmax is where the enzyme is fully saturated. Know types of inhibition and allosteric regulation. Allosteric binds at site away from active site. Pretty simple.
One example problem from the top of my head would be: use of an enzyme catalyst, will give more products (no), give more reactants (no), will get utilized in the reaction (no), will reach equilibrium (Keq) faster (yes)