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Salvia miltiorrhiza  Bunge is highly valued in traditional Chinese medicine for its roots and rhizomes. Its bioactive diterpenoid tanshinones have been reported to have many pharmaceutical activities, including antibacterial, anti-inflammatory, and anticancer properties. Previous studies found four different diterpenoid biosynthetic pathways from the universal diterpenoid precursor ( E , E , E )-geranylgeranyl diphosphate (GGPP) in  S. miltiorrhiza . Here, we describe the functional characterization of  ent -copalyl diphosphate synthase (SmCPS  ent  ), kaurene synthase (SmKS) and kaurene oxidase (SmKO) in the gibberellin (GA) biosynthetic pathway. SmCPS  ent   catalyzes the cyclization of GGPP to  ent -copalyl diphosphate ( ent -CPP), which is converted to  ent -kaurene by SmKS. Then, SmKO catalyzes the three-step oxidation of  ent -kaurene to  ent -kaurenoic acid. Our results show that the fused enzyme SmKS-SmCPS  ent   increases  ent -kaurene production by several fold compared with separate expression of SmCPS  ent   and SmKS in yeast strains. In this study, we clarify the GA biosynthetic pathway from GGPP to  ent -kaurenoic acid and provide a foundation for further characterization of the subsequent enzymes involved in this pathway. These insights may allow for better growth and the improved accumulation of bioactive tanshinones in  S. miltiorrhiza  through the regulation of the expression of these genes during developmental processes.

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Functional characterization of ent-copalyl diphosphate synthase, kaurene synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin biosynthetic pathway