The direction of a chemical reaction is determined by two factors: 1) the thermodynamics of the reaction, and 2) the availability of products and reactants.
In the pyruvate carboxylase reaction, the enzyme works only in the pyruvate-to-oxaloacetate direction because the thermodynamics of the reaction greatly favors that direction. You'll note that the reaction is coupled to the hydrolysis of ATP, which provides the large decrease in free energy (ΔG << 0). Running the reaction in the oxaloacetate-to-pyruvate direction involves the very thermodynamically unfavorable process of synthesizing ATP from ADP and PO43-.
Reaction represented by the reversible arrows indicate reactions where the change in free energy of the reactions is close to zero (ΔG ~ 0). In these cases, the relative concentrations of products and reactants will determine the direction of the reaction. For example, if 1,3-bisphosphoglycerate accumulates, phosphoglycerate kinase will facilitate its conversion into 3-phosphoglycerate. Alternatively, if the 1,3-bisphosphoglycerate gets depleted, the enzyme will work to restore the equilibrium between the two species by converting 3-phosphoglycerate into 1,3-bisphosphoglycerate.
In essence, enzymes speed up the progress of a reaction towards an equilibrium state. If the equilibrium greatly favors products over reactants, the enzyme will appear to catalyze only the forward reaction. Even though it is fully capable of catalyzing the reverse reaction, it will very do so because of the thermodynamic unfavorability of the reverse reaction. If the equilibrium constant is such that products and reactants co-exist in equilibrium, the enzyme will catalyze whichever direction brings the concentration of products and reactants to their equilibrium values.