Antimycins feature a nine-membered dilactone core and a bioactivity-essential 3-formaminosalic acid. Herein, we demonstrate that the formation of 3-aminosalicylate is catalyzed by AntHIJKL, a multicomponent diiron monooxygenase complex, via an unusual carrier protein-dependent oxidative rearrangement. AntH and AntJ constitute the minimal catalytic unit to convert anthraniloyl thioester into 3-aminosalicyl thioester on the carrier protein AntG, while AntI, AntK, and AntL function as auxiliary redox partners. This study expands the functional scope of multicomponent diiron monooxygenases.
Zhao et al. (Mon,) studied this question.