scholarly journals Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: From Structure, Functions to Applications

2021 ◽  
Vol 22 (17) ◽  
pp. 9373
Author(s):  
Kai Hong ◽  
Limin Wang ◽  
Agbaka Johnpaul ◽  
Chenyan Lv ◽  
Changwei Ma
Keyword(s):  
Geranyl Diphosphate ◽  
Key Enzymes ◽  
Monoterpene Synthase ◽  
Coa Ligase ◽  
Geranyl Diphosphate Synthase ◽  
Bitter Acids ◽  
Phytochemical Compounds ◽  
Branched Chain ◽  
Beer Production ◽  
Phytochemical Components

Humulus lupulus L. is an essential source of aroma compounds, hop bitter acids, and xanthohumol derivatives mainly exploited as flavourings in beer brewing and with demonstrated potential for the treatment of certain diseases. To acquire a comprehensive understanding of the biosynthesis of these compounds, the primary enzymes involved in the three major pathways of hops’ phytochemical composition are herein critically summarized. Hops’ phytochemical components impart bitterness, aroma, and antioxidant activity to beers. The biosynthesis pathways have been extensively studied and enzymes play essential roles in the processes. Here, we introduced the enzymes involved in the biosynthesis of hop bitter acids, monoterpenes and xanthohumol derivatives, including the branched-chain aminotransferase (BCAT), branched-chain keto-acid dehydrogenase (BCKDH), carboxyl CoA ligase (CCL), valerophenone synthase (VPS), prenyltransferase (PT), 1-deoxyxylulose-5-phosphate synthase (DXS), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HDR), Geranyl diphosphate synthase (GPPS), monoterpene synthase enzymes (MTS), cinnamate 4-hydroxylase (C4H), chalcone synthase (CHS_H1), chalcone isomerase (CHI)-like proteins (CHIL), and O-methyltransferase (OMT1). Furthermore, research advancements of each enzyme in terms of reaction conditions, substrate recognition, enzyme structures, and use in engineered microbes are described in depth. Hence, an extensive review of the key enzymes involved in the phytochemical compounds of hops will provide fundamentals for their applications in beer production.

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.

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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