In billion of years of evolution, Nature has evolved systems (or materials) to control chemical reactivity with unique specificity, efficiency and fidelity. Enzymes, capable of catalyzing reactions in their substrate-binding cavities, are a notable example. In these systems, the reactants are dynamically encapsulated in the enzymes binding site, where the reaction occurs, and the products are then expelled leaving the reaction site free for hosting another reaction. Such a machinery is controlled by a delicate modulation of host-guest interactions, which control key factors, such as, e.g., the residence time of the reactants/products (guest) in the reaction site of the enzymes (host), conformational changes in the guests favoring the reaction, etc., controlling de facto, the reactivity in the system. In the attempt to mimic natural catalytic systems, chemists have designed synthetic cavities capable of encapsulating reactants with high selectivity. In particular, supramolecular coordination cages have been designed, which can host catalytic reactions in their internal cavities. Reactivity, regio-selectivity and enantio-selectivity can be manipulated in such systems, e.g. by engineering the structural and electronic properties of the cage frameworks or by changing the guest structure. Noteworthy, mimicking what happens in some proteolytic enzymes, in a recent work it has been shown that the encapsulation of amide guests in a coordination cage may result in a considerable acceleration of amide hydrolysis.