Nature Catalysis, Published online: 25 June 2026; doi:10.1038/s41929-026-01553-4 The chalcone synthase (CHS)–chalcone isomerase-like protein (CHIL) complex is well defined, however, regulatory mechanisms remain obscure for this complex, as for most metabolons. Now, evaluating transient dynamics of this metabolon reveals that CHS undergoes rapid reversible binding cycles with CHIL and that this transiently displaces the coenzyme A inhibitor from the binding tunnel through competitive occupation,