The Pursuit of a Hydroxylation Switch Uncovers a Key Residue for Various Product Outcomes in the ent-Kaurene Synthase from Bradyrhizobium japonicum

A single residue switch leading to hydroxylation has been identified in ent-kaurene synthases (KSs) from plant gibberellin hormone biosynthesis. Here, we identified a putative equivalent in the bacterial BjKS from the gibberellin producing Bradyrhizobium japonicum. Notably, this serves as a key residue that can be varied in concert with a surrounding network to redirect product outcome, with specificity of up to 94%, providing mechanistic insight into not only BjKS but (di)terpene synthases more generally.