Azobenzene is a widely recognized tool for achieving artificial spatiotemporal control of enzyme activity through the use of light. Photocontrol reversibility is typically based on photostationary states with varying E and Z isomer compositions attained through irradiation at specific wavelengths. Here, we report an alternative mechanism for azobenzene based enzyme regulation, discovered through simultaneous irradiation with two wavelengths. Using two engineered variants of imidazole glycerol phosphate synthase, in which azobenzene was incorporated as an unnatural amino acid to enable reversible control under monochromatic irradiation, we uncovered unique behavior under dichromatic irradiation. Notably, a distinct spectroscopic signal from the azobenzene moiety emerged during simultaneous irradiation at 365:420 nm, inducing the establishment of a second photostationary state, and vanished upon return to the dark. Intriguingly, dichromatic irradiation triggered a reproducible 2-fold increase in catalytic activity and an instantaneous return to baseline activity in the dark for one variant. We could exclude sample heating as cause of this effect, as the other variant and the wild-type enzyme maintained their baseline activity under the same conditions. Remarkably, we could directly correlate this alternative photocontrol with the formation of the second photostationary state. Finally, we demonstrate that photocontrol with dichromatic irradiation appears to be successful in positions with conformational importance for catalysis. These findings reveal an unexplored avenue for azobenzene photoswitching, offering an alternative approach to photocontrol with potential applications in the sequential regulation of multiple enzymes, especially when combined with monochromatic irradiation strategies.