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Cloning and Characterization of δ-Guaiene Synthase Genes Encoding a Sesquiterpene Cyclase from Aquilaria microcarpa Cell Cultures 被引量:2
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作者 Fumiya Kurosaki Syun Hirohashi +2 位作者 Takahiro Katoh futoshi taura Jung-Bum Lee 《American Journal of Plant Sciences》 2015年第16期2603-2611,共9页
Three cDNA clones encoding δ-guaiene synthase, a sesquiterpene cyclase, were isolated from tissue cultures of Aquilaria microcarpa, and data mining analysis of the orthologous genes suggested that 10 and 9 amino acid... Three cDNA clones encoding δ-guaiene synthase, a sesquiterpene cyclase, were isolated from tissue cultures of Aquilaria microcarpa, and data mining analysis of the orthologous genes suggested that 10 and 9 amino acid residues of N- and C-terminal ends of the translated products of these clones remained undefined. The recombinant enzyme proteins, to which the putative missing Nand C-terminal amino acid sequences (MSSAKLGSAS and ALLRHAIEI, respectively) were ligated, exhibited the catalytic activities of sesquiterpene biosynthesis. Among these three δ-guaiene synthases, two isoforms were capable of liberating α-guaiene, δ-guaiene, β-elemene plus α-humulene as a minor product, while remaining one isoenzyme generated α-, δ-guaiene and β-elemene but not α-humulene. Although the enzyme protein solely lacking in the N-terminal 10 amino acid residues was capable of synthesizing the sesquiterpenoids, the protein without 9 amino acids at Cterminal did not exhibit the catalytic activity. These results suggest that two types of δ-guaiene synthase;α-, δ-guaiene, β-elemene-producing type, and α-, δ-guaiene, β-elemene plus α-humulene-producing type;concomitantly occur in A. microcarpa cell cultures, and several amino acid residues at C-terminal of the synthase protein are essential to exhibit the catalytic activities as the sesquiterpene cyclase. 展开更多
关键词 METHYL JASMONATE YEAST Extract SESQUITERPENE δ-Guaiene SYNTHASE Aquilaria microcarpa
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Efficient Production of δ-Guaiene, an Aroma Sesquiterpene Compound Accumulated in Agarwood, by Mevalonate Pathway-Engineered Escherichia coli Cells
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作者 Fumiya Kurosaki Takahiro Kato +1 位作者 Norihiko Misawa futoshi taura 《Advances in Bioscience and Biotechnology》 2016年第11期435-445,共11页
Mevalonate pathway for isoprenoid biosynthesis was constructed in Escherichia coli cells by the transformation with a gene cluster isolated from Streptomyces sp., and farnesyl diphosphate synthase and δ-guaiene synth... Mevalonate pathway for isoprenoid biosynthesis was constructed in Escherichia coli cells by the transformation with a gene cluster isolated from Streptomyces sp., and farnesyl diphosphate synthase and δ-guaiene synthase genes were coexpressed in this strain. This transformant was capable of liberating an appreciable amount of δ-guaiene, an aroma sesquiterpene compound accumulated in agarwood, and its concentration was elevated to more than 30 μg/ml culture by the incubation with mevalonolactone as an isoprene precursor in a nutrient-enriched Terrific broth. Coexpression of type 1 isopentenyl diphosphate isomerase plus acetoacetyl-CoA ligase genes also enhanced δ-guaiene production, and the concentration of the compound was approximately 38 - 42 μg/ml culture in the presence of mevalonolactone or lithium acetoacetate. These results clearly indicate that mevalonate pathway-engineered E. coli cells showed an appreciable δ-guaiene producing activity in the en- riched medium in the presence of appropriate isoprene precursors. 展开更多
关键词 Engineered Escherichia coli δ-Guaiene Production ISOPRENOIDS Mevalonate Pathway Secondary Metabolism SESQUITERPENE
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