ArticlePlant biotechnology journal2023
Structural and mechanistic insights into the precise product synthesis by a bifunctional miltiradiene synthase.
Article in Plant biotechnology journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Analysis genome of Pseudotaxus chienii reveals insights into the origin and evolution of taxane biosynthesis.Nature communications · 2025Article
- Investigating conserved aromatic residues in ent-copalyl pyrophosphate synthases required for gibberellin phytohormone biosynthesis.Phytochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.Biochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.bioRxiv : the preprint server for biology · 2025Article
- Dual distal insertions drive pimarane-to-miltiradiene rearrangement with enhanced enzymatic activity.Biodesign research · 2025Article
- The Dynamic Changes in Biosynthesis and Spatiotemporal Distribution of Phytohormones Under Jasmonic Acid Treatment Provide Insights into Hormonal Regulation inPlants (Basel, Switzerland) · 2025Article
- From functional plasticity of two diterpene synthases (IrTPS2/IrKSL3a) to enzyme evolution.ACS catalysis · 2024Article
- Sequence-Structure Analysis Unlocking the Potential Functional Application of the Local 3D Motifs of Plant-Derived Diterpene Synthases.Biomolecules · 2024Article
- Miltiradiene Production by Cytoplasmic Metabolic Engineering inMetabolites · 2023Article
- Structural and functional investigations of syn-copalyl diphosphate synthase from Oryza sativa.Communications chemistry · 2023Article
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10 authors.
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Abstract
Selaginella moellendorffii miltiradiene synthase (SmMDS) is a unique bifunctional diterpene synthase (diTPS) that catalyses the successive cyclization of (E,E,E)-geranylgeranyl diphosphate (GGPP) via (+)-copalyl diphosphate (CPP) to miltiradiene, which is a crucial precursor of important medicinal compounds, such as triptolide, ecabet sodium and carnosol. Miltiradiene synthetic processes have been studied in monofunctional diTPSs, while the precise mechanism by which active site amino acids determine product simplicity and the experimental evidence for reaction intermediates remain elusive. In addition, how bifunctional diTPSs work compared to monofunctional enzymes is attractive for detailed research. Here, by mutagenesis studies of SmMDS, we confirmed that pimar-15-en-8-yl
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