ArticleMicrobial cell factories2024
Identification of squalene epoxidase in triterpenes biosynthesis in Poria cocos by molecular docking and CRISPR-Cas9 gene editing.
Article in Microbial cell factories, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Recent developments in CRISPR/Cas9 genome editing research for edible fungiculture.Functional & integrative genomics · 2026Review
- Recent trends in the elucidation of complex triterpene biosynthetic pathways in horticultural trees.Horticulture research · 2025Article
- Insights into microbiome-triterpenoid correlation inFrontiers in microbiology · 2025Article
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7 authors at 2 institutions in 1 country.
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Abstract
backgroundSqualene epoxidase is one of the rate-limiting enzymes in the biosynthetic pathway of membrane sterols and triterpenoids. The enzyme catalyzes the formation of oxidized squalene, which is a common precursor of sterols and triterpenoids.
resultIn this study, the squalene epoxidase gene (PcSE) was evaluated in Poria cocos. Molecular docking between PcSE and squalene was performed and the active amino acids were identified. The sgRNA were designed based on the active site residues. The effect on triterpene synthesis in P. cocos was consistent with the results from ultra-high-performance liquid chromatography-quadruplex time-of-flight-double mass spectrometry (UHPLC-QTOF-MS/MS) analysis. The results showed that deletion of PcSE inhibited triterpene synthesis. In vivo verification of PcSE function was performed using a PEG-mediated protoplast transformation approach.
conclusionThe findings from this study provide a foundation for further studies on heterologous biosynthesis of P. cocos secondary metabolites.
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