We finally explored the ability to use an enzyme as a stimulus. Alkaline phosphatase (ALP) was chosen as an enzymatic cleavage agent for its ability to catalytically hydrolyze ATP into adenosine and three equivalents of monophosphate groups in very mild conditions. We exploited this property and used ALP as a trigger to dynamically control ATP/AzoDiGua coassembly. Adding ALP to the preformed ATP/AzoDiGua aggregates ([ATP] = 1 mM, [AzoDiGua] = 1 mM) led to their complete disassembly in 10 min (Figure ). This disassembly was accompanied by a loss of turbidity of the ATP/AzoDiGua solution after adding the enzyme to the mixture (Figure ). When the same experiment was performed with a previously denaturated ALP (treatment at 90 °C), the suspension turbidity remained and no disassembly was observed (Figure ), confirming that ALP-triggered disassembly was due to ATP hydrolysis by the active enzyme. This enzyme-mediated disassembly was accompanied by a gradual decrease of suspension fluorescence down to a minimal level corresponding to that of free AzoDiGua after 10 min of reaction (Figure ), confirming the complete disassembly and release of free AzoDiGua. These results thus demonstrated how both aggregation-induced fluorescence of azobenzene and the characteristics of a self-assembled structure can be dynamically controlled through the action of an active enzyme having as a substrate one of two co-assembled partners.