Heteromeric geranyl diphosphate synthase from mint: construction of a functional fusion protein and inhibition by bisphosphonate substrate analogs

2004 ◽  
Vol 422 (1) ◽  
pp. 52-60 ◽  
Author(s):  
Charles Burke ◽  
Karin Klettke ◽  
Rodney Croteau
Keyword(s):  
Fusion Protein ◽  
Geranyl Diphosphate ◽  
Substrate Analogs ◽  
Geranyl Diphosphate Synthase

scholarly journals Biosynthesis of pinene in purple non-sulfur photosynthetic bacteria

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Xiaomin Wu ◽  
Guang Ma ◽  
Chuanyang Liu ◽  
Xin-yuan Qiu ◽  
Lu Min ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Heterologous Expression ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Fine Chemicals ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Geranyl Diphosphate ◽  
Ribosome Binding ◽  
Geranyl Diphosphate Synthase

Abstract Background Pinene is a monoterpene, that is used in the manufacture of fragrances, insecticide, fine chemicals, and renewable fuels. Production of pinene by metabolic-engineered microorganisms is a sustainable method. Purple non-sulfur photosynthetic bacteria belong to photosynthetic chassis that are widely used to synthesize natural chemicals. To date, researches on the synthesis of pinene by purple non-sulfur photosynthetic bacteria has not been reported, leaving the potential of purple non-sulfur photosynthetic bacteria synthesizing pinene unexplored. Results Rhodobacter sphaeroides strain was applied as a model and engineered to express the fusion protein of heterologous geranyl diphosphate synthase (GPPS) and pinene synthase (PS), hence achieving pinene production. The reaction condition of pinene production was optimized and 97.51 μg/L of pinene was yielded. Then, genes of 1-deoxy-d-xylulose 5-phosphate synthase, 1-deoxy-d-xylulose 5-phosphate reductoisomerase and isopentenyl diphosphate isomerase were overexpressed, and the ribosome binding site of GPPS-PS mRNA was optimized, improving pinene titer to 539.84 μg/L. Conclusions In this paper, through heterologous expression of GPPS-PS, pinene was successfully produced in R. sphaeroides, and pinene production was greatly improved by optimizing the expression of key enzymes. This is the first report on pinene produce by purple non-sulfur photosynthetic bacteria, which expands the availability of photosynthetic chassis for pinene production.

scholarly journals Biosynthesis of Pinene in Purple Non-Sulfur Photosynthetic Bacteria

2021 ◽  
Author(s):  
Xiaomin Wu ◽  
Guang Ma ◽  
Chuanyang Liu ◽  
Xin-yuan Qiu ◽  
Lu Min ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Heterologous Expression ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Fine Chemicals ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Geranyl Diphosphate ◽  
Ribosome Binding ◽  
Geranyl Diphosphate Synthase

Abstract Background: Pinene is a monoterpene, that is used in the manufacture of fragrances, insecticide, fine chemicals, and renewable fuels. Production of pinene by metabolic-engineered microorganisms is a sustainable method. Purple non-sulfur photosynthetic bacteria belong to photosynthetic chassis that are widely used to synthesize natural chemicals. To date, researches on the synthesis of pinene by purple non-sulfur photosynthetic bacteria has not been reported, leaving the potential of purple non-sulfur photosynthetic bacteria synthesizing pinene unexplored. Results: Rhodobacter sphaeroides strain was applied as a model and engineered to express the fusion protein of heterologous geranyl diphosphate synthase (GPPS) and pinene synthase (PS), hence achieving pinene production. The reaction condition of pinene production was optimized and 97.51 μg/L of pinene was yielded. Then, genes of 1-deoxy-D-xylulose 5-phosphate synthase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase and isopentenyl diphosphate isomerase were overexpressed, and the ribosome binding site of GPPS-PS mRNA was optimized, improving pinene titer to 539.84 μg/L. Conclusions: In this paper, through heterologous expression of GPPS-PS, pinene was successfully produced in R. sphaeroides, and pinene production was greatly improved by optimizing the expression of key enzymes. This is the first report on pinene produce by purple non-sulfur photosynthetic bacteria, which expands the availability of photosynthetic chassis for pinene production.

A novel homodimeric geranyl diphosphate synthase from the orchidPhalaenopsis bellinalacking a DD(X)2-4D motif

2008 ◽  
Vol 55 (5) ◽  
pp. 719-733 ◽  
Author(s):  
Yu-Yun Hsiao ◽  
Mei-Fen Jeng ◽  
Wen-Chieh Tsai ◽  
Yu-Chen Chuang ◽  
Chia-Ying Li ◽  
...  
Keyword(s):  
Geranyl Diphosphate ◽  
Geranyl Diphosphate Synthase

scholarly journals Geranyl diphosphate synthase is required for biosynthesis of gibberellins

2007 ◽  
Vol 52 (4) ◽  
pp. 752-762 ◽  
Author(s):  
Chris C. N. Van Schie ◽  
Kai Ament ◽  
Axel Schmidt ◽  
Theo Lange ◽  
Michel A. Haring ◽  
...  
Keyword(s):  
Geranyl Diphosphate ◽  
Geranyl Diphosphate Synthase

scholarly journals A Cytosol-Localized Geranyl Diphosphate Synthase from Lithospermum erythrorhizon and Its Molecular Evolution

2020 ◽  
Vol 182 (4) ◽  
pp. 1933-1945 ◽  
Author(s):  
Hayato Ueoka ◽  
Kanako Sasaki ◽  
Tatsuya Miyawaki ◽  
Takuji Ichino ◽  
Kanade Tatsumi ◽  
...  
Keyword(s):  
Molecular Evolution ◽  
Lithospermum Erythrorhizon ◽  
Geranyl Diphosphate ◽  
Geranyl Diphosphate Synthase

scholarly journals Identification and Molecular Characterization of Geranyl Diphosphate Synthase (GPPS) Genes in Wintersweet Flower

Plants ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 666
Author(s):  
Hafiz Muhammad Kamran ◽  
Syed Bilal Hussain ◽  
Shang Junzhong ◽  
Lin Xiang ◽  
Long-Qing Chen
Keyword(s):  
Floral Scent ◽  
Sequence Similarity ◽  
Constitutive Expression ◽  
Transcript Level ◽  
Open Flower ◽  
Specific Expression ◽  
Geranyl Diphosphate ◽  
Geranyl Diphosphate Synthase ◽  
Transcriptome Database ◽  
Flower Stage

Geranyl diphosphate synthase (GPPS) is a plastid localized enzyme that catalyzes the biosynthesis of Geranyl diphosphate (GPP), which is a universal precursor of monoterpenes. Wintersweet (Chimonanthus praecox L.), a famous deciduous flowering shrub with a strong floral scent character, could have GPPS-like homologs that are involved in monoterpenes biosynthesis, but it remains unclear. In the present study, five full-length GPPS and geranylgeranyl diphosphate synthases (GGPPS) genes were identified in the wintersweet transcriptome database. The isolated cDNAs showed high protein sequence similarity with the other plants GPPS and GGPPS. The phylogenetic analysis further classified these cDNAs into four distinct clades, representing heterodimeric GPPS small subunits (SSU1 and SSU2), homodimeric GPPS, and GGPPS. Analysis of temporal expression revealed that all genes have the highest transcript level at the full-open flower stage. From tissue-specific expression analysis, CpGPPS.SSU1 and CpGGPPS1 were predominantly expressed in petal and flower, whereas CpGPPS.SSU2, GPPS, and GGPPS2 showed a constitutive expression. Additionally, the subcellular localization assay identified the chloroplast localization of SSUs and GGPPSs proteins, and the yeast two-hybrid assay showed that both CpGPPS.SSU1 and CpGPPS.SSU2 can interact with the GGPPS proteins. Taken together, these preliminary results suggest that the heterodimeric GPPS can regulate floral scent biosynthesis in wintersweet flower.

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