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A high-throughput colorimetric screening assay for terpene synthase activity based on substrate consumption
Terpene synthases catalyze the formation of a variety of terpene chemical structures. Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical str...
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| Published in: | PloS one 2014-03, Vol.9 (3), p.e93317 |
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| creator | Furubayashi, Maiko Ikezumi, Mayu Kajiwara, Jun Iwasaki, Miki Fujii, Akira Li, Ling Saito, Kyoichi Umeno, Daisuke |
| description | Terpene synthases catalyze the formation of a variety of terpene chemical structures. Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical structures. In addition, there is growing demand to increase terpene synthase activity in heterologous hosts, given the maturation of metabolic engineering and host breeding for terpenoid synthesis. We have developed a simple screening method for the cellular activities of terpene synthases by scoring their substrate consumption based on the color loss of the cell harboring carotenoid pathways. We demonstrate that this method can be used to detect activities of various terpene synthase or prenyltransferase genes in a high-throughput manner, irrespective of the product type, enabling the mutation analysis and directed evolution of terpene synthases. We also report the possibility for substrate-specific screening system of terpene synthases by taking advantage of the substrate-size specificity of C30 and C40 carotenoid pathways. |
| doi_str_mv | 10.1371/journal.pone.0093317 |
| format | article |
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Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical structures. In addition, there is growing demand to increase terpene synthase activity in heterologous hosts, given the maturation of metabolic engineering and host breeding for terpenoid synthesis. We have developed a simple screening method for the cellular activities of terpene synthases by scoring their substrate consumption based on the color loss of the cell harboring carotenoid pathways. We demonstrate that this method can be used to detect activities of various terpene synthase or prenyltransferase genes in a high-throughput manner, irrespective of the product type, enabling the mutation analysis and directed evolution of terpene synthases. We also report the possibility for substrate-specific screening system of terpene synthases by taking advantage of the substrate-size specificity of C30 and C40 carotenoid pathways.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0093317</identifier><identifier>PMID: 24681801</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alkyl and Aryl Transferases - chemistry ; Amino Acid Sequence ; Analysis ; Binding sites ; Biology and Life Sciences ; Biosynthesis ; Biotechnology ; Breeding ; Carbon-carbon composites ; Carotenoids ; Carotenoids - chemistry ; Colorimetry ; Colorimetry - methods ; Consumption data ; Directed evolution ; E coli ; Engineering ; Enzymes ; Escherichia coli ; Escherichia coli - chemistry ; Evolution ; Genomes ; High-Throughput Screening Assays - methods ; Medical screening ; Metabolic engineering ; Metabolism ; Molecular Sequence Data ; Mutagenesis ; Mutation ; Pathways ; Proteins ; Screening ; Substrate Specificity ; Substrates ; Terpene synthase</subject><ispartof>PloS one, 2014-03, Vol.9 (3), p.e93317</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Furubayashi et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Furubayashi et al 2014 Furubayashi et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-1b7cf0f14e916230304d0fdf2b61feffc8cae33ea90b661c57c4b1991859b7683</citedby><cites>FETCH-LOGICAL-c758t-1b7cf0f14e916230304d0fdf2b61feffc8cae33ea90b661c57c4b1991859b7683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1511109921/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1511109921?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24681801$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Roccatano, Danilo</contributor><creatorcontrib>Furubayashi, Maiko</creatorcontrib><creatorcontrib>Ikezumi, Mayu</creatorcontrib><creatorcontrib>Kajiwara, Jun</creatorcontrib><creatorcontrib>Iwasaki, Miki</creatorcontrib><creatorcontrib>Fujii, Akira</creatorcontrib><creatorcontrib>Li, Ling</creatorcontrib><creatorcontrib>Saito, Kyoichi</creatorcontrib><creatorcontrib>Umeno, Daisuke</creatorcontrib><title>A high-throughput colorimetric screening assay for terpene synthase activity based on substrate consumption</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Terpene synthases catalyze the formation of a variety of terpene chemical structures. Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical structures. In addition, there is growing demand to increase terpene synthase activity in heterologous hosts, given the maturation of metabolic engineering and host breeding for terpenoid synthesis. We have developed a simple screening method for the cellular activities of terpene synthases by scoring their substrate consumption based on the color loss of the cell harboring carotenoid pathways. We demonstrate that this method can be used to detect activities of various terpene synthase or prenyltransferase genes in a high-throughput manner, irrespective of the product type, enabling the mutation analysis and directed evolution of terpene synthases. 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Systematic mutagenesis studies have been effective in providing insights into the characteristic and complex mechanisms of C-C bond formations and in exploring the enzymatic potential for inventing new chemical structures. In addition, there is growing demand to increase terpene synthase activity in heterologous hosts, given the maturation of metabolic engineering and host breeding for terpenoid synthesis. We have developed a simple screening method for the cellular activities of terpene synthases by scoring their substrate consumption based on the color loss of the cell harboring carotenoid pathways. We demonstrate that this method can be used to detect activities of various terpene synthase or prenyltransferase genes in a high-throughput manner, irrespective of the product type, enabling the mutation analysis and directed evolution of terpene synthases. We also report the possibility for substrate-specific screening system of terpene synthases by taking advantage of the substrate-size specificity of C30 and C40 carotenoid pathways.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24681801</pmid><doi>10.1371/journal.pone.0093317</doi><tpages>e93317</tpages><oa>free_for_read</oa></addata></record> |
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| source | Open Access: PubMed Central; Publicly Available Content Database (Proquest) (PQ_SDU_P3) |
| subjects | Alkyl and Aryl Transferases - chemistry Amino Acid Sequence Analysis Binding sites Biology and Life Sciences Biosynthesis Biotechnology Breeding Carbon-carbon composites Carotenoids Carotenoids - chemistry Colorimetry Colorimetry - methods Consumption data Directed evolution E coli Engineering Enzymes Escherichia coli Escherichia coli - chemistry Evolution Genomes High-Throughput Screening Assays - methods Medical screening Metabolic engineering Metabolism Molecular Sequence Data Mutagenesis Mutation Pathways Proteins Screening Substrate Specificity Substrates Terpene synthase |
| title | A high-throughput colorimetric screening assay for terpene synthase activity based on substrate consumption |
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