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Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply
The heterologous production of fungal polyketides was investigated using 6-methylsalicylic acid synthase (6-MSAS) as a model polyketide synthase and Saccharomyces cerevisiae as a host. In order to improve the production of 6-MSA by enhancing the supply of precursors, the promoter of the gene ( ACC1)...
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| Published in: | Metabolic engineering 2008-09, Vol.10 (5), p.246-254 |
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| container_title | Metabolic engineering |
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| creator | Wattanachaisaereekul, Songsak Lantz, Anna Eliasson Nielsen, Michael Lynge Nielsen, Jens |
| description | The heterologous production of fungal polyketides was investigated using 6-methylsalicylic acid synthase (6-MSAS) as a model polyketide synthase and
Saccharomyces cerevisiae as a host. In order to improve the production of 6-MSA by enhancing the supply of precursors, the promoter of the gene (
ACC1) encoding acetyl-CoA carboxylase, which catalyzes the conversion of acetyl-CoA to malonyl-CoA, was replaced with a strong, constitutive promoter (
TEF1p) in a strain harboring two plasmids carrying the genes encoding 6-MSAS from
Penicillium patulum and PPTase from
Aspergillus nidulans, respectively. The strain was characterized in batch cultivations with a glucose minimal media (20
g/L), and a 60% increase in 6-MSA titer was observed compared to a strain having the native promoter in front of
ACC1. The production of 6-MSA was scaled up by the cultivation in minimal media containing 50
g/L of glucose, and hereby a final titer of 554±26
mg/L of 6-MSA was obtained. |
| doi_str_mv | 10.1016/j.ymben.2008.04.005 |
| format | article |
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Saccharomyces cerevisiae as a host. In order to improve the production of 6-MSA by enhancing the supply of precursors, the promoter of the gene (
ACC1) encoding acetyl-CoA carboxylase, which catalyzes the conversion of acetyl-CoA to malonyl-CoA, was replaced with a strong, constitutive promoter (
TEF1p) in a strain harboring two plasmids carrying the genes encoding 6-MSAS from
Penicillium patulum and PPTase from
Aspergillus nidulans, respectively. The strain was characterized in batch cultivations with a glucose minimal media (20
g/L), and a 60% increase in 6-MSA titer was observed compared to a strain having the native promoter in front of
ACC1. The production of 6-MSA was scaled up by the cultivation in minimal media containing 50
g/L of glucose, and hereby a final titer of 554±26
mg/L of 6-MSA was obtained.</description><identifier>ISSN: 1096-7176</identifier><identifier>EISSN: 1096-7184</identifier><identifier>DOI: 10.1016/j.ymben.2008.04.005</identifier><identifier>PMID: 18555717</identifier><language>eng</language><publisher>Belgium: Elsevier Inc</publisher><subject>Acetyl Coenzyme A - genetics ; Acetyl Coenzyme A - metabolism ; Acetyl-CoA carboxylase ; Acetyltransferases - biosynthesis ; Acetyltransferases - genetics ; Acyltransferases - biosynthesis ; Acyltransferases - genetics ; Aspergillus nidulans ; Aspergillus nidulans - enzymology ; Aspergillus nidulans - genetics ; Heterologous expression ; Ligases - biosynthesis ; Ligases - genetics ; Macrolides - metabolism ; Malonyl Coenzyme A - genetics ; Malonyl Coenzyme A - metabolism ; Malonyl-CoA ; Multienzyme Complexes - biosynthesis ; Multienzyme Complexes - genetics ; Oxidoreductases - biosynthesis ; Oxidoreductases - genetics ; Penicillium - enzymology ; Penicillium - genetics ; Penicillium patulum ; Peptide Elongation Factor 1 - genetics ; Peptide Elongation Factor 1 - metabolism ; Polyketides ; Precursor supply ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - growth & development ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Salicylates - metabolism</subject><ispartof>Metabolic engineering, 2008-09, Vol.10 (5), p.246-254</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-2ed83c49f7d630b140fc07c6c764abd4323d19f18e17034da00bf6d092928a693</citedby><cites>FETCH-LOGICAL-c454t-2ed83c49f7d630b140fc07c6c764abd4323d19f18e17034da00bf6d092928a693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18555717$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wattanachaisaereekul, Songsak</creatorcontrib><creatorcontrib>Lantz, Anna Eliasson</creatorcontrib><creatorcontrib>Nielsen, Michael Lynge</creatorcontrib><creatorcontrib>Nielsen, Jens</creatorcontrib><title>Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply</title><title>Metabolic engineering</title><addtitle>Metab Eng</addtitle><description>The heterologous production of fungal polyketides was investigated using 6-methylsalicylic acid synthase (6-MSAS) as a model polyketide synthase and
Saccharomyces cerevisiae as a host. In order to improve the production of 6-MSA by enhancing the supply of precursors, the promoter of the gene (
ACC1) encoding acetyl-CoA carboxylase, which catalyzes the conversion of acetyl-CoA to malonyl-CoA, was replaced with a strong, constitutive promoter (
TEF1p) in a strain harboring two plasmids carrying the genes encoding 6-MSAS from
Penicillium patulum and PPTase from
Aspergillus nidulans, respectively. The strain was characterized in batch cultivations with a glucose minimal media (20
g/L), and a 60% increase in 6-MSA titer was observed compared to a strain having the native promoter in front of
ACC1. The production of 6-MSA was scaled up by the cultivation in minimal media containing 50
g/L of glucose, and hereby a final titer of 554±26
mg/L of 6-MSA was obtained.</description><subject>Acetyl Coenzyme A - genetics</subject><subject>Acetyl Coenzyme A - metabolism</subject><subject>Acetyl-CoA carboxylase</subject><subject>Acetyltransferases - biosynthesis</subject><subject>Acetyltransferases - genetics</subject><subject>Acyltransferases - biosynthesis</subject><subject>Acyltransferases - genetics</subject><subject>Aspergillus nidulans</subject><subject>Aspergillus nidulans - enzymology</subject><subject>Aspergillus nidulans - genetics</subject><subject>Heterologous expression</subject><subject>Ligases - biosynthesis</subject><subject>Ligases - genetics</subject><subject>Macrolides - metabolism</subject><subject>Malonyl Coenzyme A - genetics</subject><subject>Malonyl Coenzyme A - metabolism</subject><subject>Malonyl-CoA</subject><subject>Multienzyme Complexes - biosynthesis</subject><subject>Multienzyme Complexes - genetics</subject><subject>Oxidoreductases - biosynthesis</subject><subject>Oxidoreductases - genetics</subject><subject>Penicillium - enzymology</subject><subject>Penicillium - genetics</subject><subject>Penicillium patulum</subject><subject>Peptide Elongation Factor 1 - genetics</subject><subject>Peptide Elongation Factor 1 - metabolism</subject><subject>Polyketides</subject><subject>Precursor supply</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - growth & development</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Salicylates - metabolism</subject><issn>1096-7176</issn><issn>1096-7184</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNqFkEFP3DAQha2qVYEtv6AS8qm3hHHiOPGBw2oFLRKoSLTiaCX2BLwkcWonSPn39XZXcCunmXnz5o30EfKVQcqAifNtuvQNDmkGUKXAU4DiAzlmIEVSsop_fO1LcUROQtgCMFZI9pkcsaooirg4Jg933plZT9YN1LV0ekI6um55xskapCK5vV9TO9AF6zBRHB7tgOjR0Nb5qGsf9Tj1deeGpUs2bk3DPI7d8oV8ausu4Omhrsjvq8tfmx_Jzc_v15v1TaJ5wackQ1Plmsu2NCKHhnFoNZRa6FLwujE8z3LDZMsqZCXk3NQATSsMyExmVS1kviLf9rmjd39mDJPqbdDYdfWAbg5KSC5lxdm7xgyynGdyl5jvjdq7EDy2avS2r_2iGKgdeLVV_8CrHXgFXEXw8ersED83PZq3mwPpaLjYGzDSeLHoVdAWB43GetSTMs7-98Ffvn-Umw</recordid><startdate>20080901</startdate><enddate>20080901</enddate><creator>Wattanachaisaereekul, Songsak</creator><creator>Lantz, Anna Eliasson</creator><creator>Nielsen, Michael Lynge</creator><creator>Nielsen, Jens</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20080901</creationdate><title>Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply</title><author>Wattanachaisaereekul, Songsak ; 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Saccharomyces cerevisiae as a host. In order to improve the production of 6-MSA by enhancing the supply of precursors, the promoter of the gene (
ACC1) encoding acetyl-CoA carboxylase, which catalyzes the conversion of acetyl-CoA to malonyl-CoA, was replaced with a strong, constitutive promoter (
TEF1p) in a strain harboring two plasmids carrying the genes encoding 6-MSAS from
Penicillium patulum and PPTase from
Aspergillus nidulans, respectively. The strain was characterized in batch cultivations with a glucose minimal media (20
g/L), and a 60% increase in 6-MSA titer was observed compared to a strain having the native promoter in front of
ACC1. The production of 6-MSA was scaled up by the cultivation in minimal media containing 50
g/L of glucose, and hereby a final titer of 554±26
mg/L of 6-MSA was obtained.</abstract><cop>Belgium</cop><pub>Elsevier Inc</pub><pmid>18555717</pmid><doi>10.1016/j.ymben.2008.04.005</doi><tpages>9</tpages></addata></record> |
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| ispartof | Metabolic engineering, 2008-09, Vol.10 (5), p.246-254 |
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| source | ScienceDirect Freedom Collection |
| subjects | Acetyl Coenzyme A - genetics Acetyl Coenzyme A - metabolism Acetyl-CoA carboxylase Acetyltransferases - biosynthesis Acetyltransferases - genetics Acyltransferases - biosynthesis Acyltransferases - genetics Aspergillus nidulans Aspergillus nidulans - enzymology Aspergillus nidulans - genetics Heterologous expression Ligases - biosynthesis Ligases - genetics Macrolides - metabolism Malonyl Coenzyme A - genetics Malonyl Coenzyme A - metabolism Malonyl-CoA Multienzyme Complexes - biosynthesis Multienzyme Complexes - genetics Oxidoreductases - biosynthesis Oxidoreductases - genetics Penicillium - enzymology Penicillium - genetics Penicillium patulum Peptide Elongation Factor 1 - genetics Peptide Elongation Factor 1 - metabolism Polyketides Precursor supply Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Salicylates - metabolism |
| title | Production of the polyketide 6-MSA in yeast engineered for increased malonyl-CoA supply |
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