Halogenases offer valuable opportunities in synthetic chemistry and biocatalysis. Here, we identify two novel flavin-dependent phenolic multisite halogenases, FasVamrb99 and IdmB26, from distinct biosynthetic pathways that exhibit divergent polyhalogenation of naphthacemycin B2. Substrate screening revealed that both enzymes display robust polyhalogenation activity, enabling halogenation not only at ortho positions adjacent to nonphenolic hydroxyl groups but also across a range of drug molecules. These features highlight their versatility and potential as biocatalysts for synthetic applications.
Peng et al. (Fri,) studied this question.