A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone
A novel plant-specific type III polyketide synthase (PKS) that catalyzes formation of a pentaketide chromone, 5,7-dihydroxy-2-methylchromone, from five molecules of malonyl-CoA, was cloned and sequenced from aloe (Aloe arborescens). Site-directed mutagenesis revealed that Met207 (corresponding to Th...
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| Veröffentlicht in: | Journal of the American Chemical Society 2005-02, Vol.127 (5), p.1362-1363 |
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| container_title | Journal of the American Chemical Society |
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| creator | Abe, Ikuro Utsumi, Yoriko Oguro, Satoshi Morita, Hiroyuki Sano, Yukie Noguchi, Hiroshi |
| description | A novel plant-specific type III polyketide synthase (PKS) that catalyzes formation of a pentaketide chromone, 5,7-dihydroxy-2-methylchromone, from five molecules of malonyl-CoA, was cloned and sequenced from aloe (Aloe arborescens). Site-directed mutagenesis revealed that Met207 (corresponding to Thr197 in CHS) determines the polyketide chain length and the product specificity of the enzyme; remarkably, replacement of a single amino acid residue, Met207, with Gly yielded a mutant enzyme that efficiently produces aromatic octaketides, SEK4 and SEK4b, the products of the minimal PKS for actinorhodin (act from Streptomyces coelicolor), from eight molecules of malonyl-CoA. This provided new insights into the catalytic functions and specificities of the CHS-superfamily type III PKS enzymes. |
| doi_str_mv | 10.1021/ja0431206 |
| format | Article |
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Site-directed mutagenesis revealed that Met207 (corresponding to Thr197 in CHS) determines the polyketide chain length and the product specificity of the enzyme; remarkably, replacement of a single amino acid residue, Met207, with Gly yielded a mutant enzyme that efficiently produces aromatic octaketides, SEK4 and SEK4b, the products of the minimal PKS for actinorhodin (act from Streptomyces coelicolor), from eight molecules of malonyl-CoA. This provided new insights into the catalytic functions and specificities of the CHS-superfamily type III PKS enzymes.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja0431206</identifier><identifier>PMID: 15686354</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acyltransferases - chemistry ; Acyltransferases - genetics ; Acyltransferases - metabolism ; Aloe - enzymology ; Aloe - genetics ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Aromatic and heterocyclic compounds ; Biological and medical sciences ; Biotechnology ; Chromones - metabolism ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; Heterocyclic compounds, pigments ; Kinetics ; Malonyl Coenzyme A - metabolism ; Methods. Procedures. Technologies ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Other biological molecules ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Site specific mutagenesis ; Substrate Specificity</subject><ispartof>Journal of the American Chemical Society, 2005-02, Vol.127 (5), p.1362-1363</ispartof><rights>Copyright © 2005 American Chemical Society</rights><rights>2005 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a381t-c6ad40d6943d93040e024cb5196f4dd0a2b9a01f85534d3a4569ae116a80b31e3</citedby><cites>FETCH-LOGICAL-a381t-c6ad40d6943d93040e024cb5196f4dd0a2b9a01f85534d3a4569ae116a80b31e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja0431206$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja0431206$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16477767$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15686354$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Abe, Ikuro</creatorcontrib><creatorcontrib>Utsumi, Yoriko</creatorcontrib><creatorcontrib>Oguro, Satoshi</creatorcontrib><creatorcontrib>Morita, Hiroyuki</creatorcontrib><creatorcontrib>Sano, Yukie</creatorcontrib><creatorcontrib>Noguchi, Hiroshi</creatorcontrib><title>A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>A novel plant-specific type III polyketide synthase (PKS) that catalyzes formation of a pentaketide chromone, 5,7-dihydroxy-2-methylchromone, from five molecules of malonyl-CoA, was cloned and sequenced from aloe (Aloe arborescens). Site-directed mutagenesis revealed that Met207 (corresponding to Thr197 in CHS) determines the polyketide chain length and the product specificity of the enzyme; remarkably, replacement of a single amino acid residue, Met207, with Gly yielded a mutant enzyme that efficiently produces aromatic octaketides, SEK4 and SEK4b, the products of the minimal PKS for actinorhodin (act from Streptomyces coelicolor), from eight molecules of malonyl-CoA. This provided new insights into the catalytic functions and specificities of the CHS-superfamily type III PKS enzymes.</description><subject>Acyltransferases - chemistry</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Aloe - enzymology</subject><subject>Aloe - genetics</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Aromatic and heterocyclic compounds</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Chromones - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic engineering</subject><subject>Genetic technics</subject><subject>Heterocyclic compounds, pigments</subject><subject>Kinetics</subject><subject>Malonyl Coenzyme A - metabolism</subject><subject>Methods. Procedures. Technologies</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Other biological molecules</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Site specific mutagenesis</subject><subject>Substrate Specificity</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M9PwjAUB_DGaATRg_-A6cWDh2m7_th2JERhCnERPDdvaxcGYyPtSNx_7wwLXLz0pe998tJ-Ebqn5JkSn75sgHBGfSIv0JAKn3iC-vISDQkhvheEkg3QjXOb7sr9kF6jARWy6wo-RNMxTkqoGrxq9wbHcYyTumy3pim0wcu2atbgDO7OBie21ofMOJyYqoGeTNa23tWVuUVXOZTO3PV1hL7fXleTmTf_nMaT8dwDFtLGyyRoTrSMONMRI5wY4vMsFTSSOdeagJ9GQGgeCsG4ZsCFjMBQKiEkKaOGjdDTcW9ma-esydXeFjuwraJE_YWhTmF09uFo94d0Z_RZ9r_vwGMPwGVQ5haqrHBnJ3kQBDLonHd0hWvMz2kOdqu6aSDUKlmqZLKYzz6-3tXivBcypzb1wVZdJP888BcO0X_O</recordid><startdate>20050209</startdate><enddate>20050209</enddate><creator>Abe, Ikuro</creator><creator>Utsumi, Yoriko</creator><creator>Oguro, Satoshi</creator><creator>Morita, Hiroyuki</creator><creator>Sano, Yukie</creator><creator>Noguchi, Hiroshi</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20050209</creationdate><title>A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone</title><author>Abe, Ikuro ; Utsumi, Yoriko ; Oguro, Satoshi ; Morita, Hiroyuki ; Sano, Yukie ; Noguchi, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-c6ad40d6943d93040e024cb5196f4dd0a2b9a01f85534d3a4569ae116a80b31e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Acyltransferases - chemistry</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Aloe - enzymology</topic><topic>Aloe - genetics</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Aromatic and heterocyclic compounds</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Chromones - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic engineering</topic><topic>Genetic technics</topic><topic>Heterocyclic compounds, pigments</topic><topic>Kinetics</topic><topic>Malonyl Coenzyme A - metabolism</topic><topic>Methods. Procedures. Technologies</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Other biological molecules</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Site specific mutagenesis</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Abe, Ikuro</creatorcontrib><creatorcontrib>Utsumi, Yoriko</creatorcontrib><creatorcontrib>Oguro, Satoshi</creatorcontrib><creatorcontrib>Morita, Hiroyuki</creatorcontrib><creatorcontrib>Sano, Yukie</creatorcontrib><creatorcontrib>Noguchi, Hiroshi</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Abe, Ikuro</au><au>Utsumi, Yoriko</au><au>Oguro, Satoshi</au><au>Morita, Hiroyuki</au><au>Sano, Yukie</au><au>Noguchi, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2005-02-09</date><risdate>2005</risdate><volume>127</volume><issue>5</issue><spage>1362</spage><epage>1363</epage><pages>1362-1363</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>A novel plant-specific type III polyketide synthase (PKS) that catalyzes formation of a pentaketide chromone, 5,7-dihydroxy-2-methylchromone, from five molecules of malonyl-CoA, was cloned and sequenced from aloe (Aloe arborescens). Site-directed mutagenesis revealed that Met207 (corresponding to Thr197 in CHS) determines the polyketide chain length and the product specificity of the enzyme; remarkably, replacement of a single amino acid residue, Met207, with Gly yielded a mutant enzyme that efficiently produces aromatic octaketides, SEK4 and SEK4b, the products of the minimal PKS for actinorhodin (act from Streptomyces coelicolor), from eight molecules of malonyl-CoA. This provided new insights into the catalytic functions and specificities of the CHS-superfamily type III PKS enzymes.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15686354</pmid><doi>10.1021/ja0431206</doi><tpages>2</tpages></addata></record> |
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| subjects | Acyltransferases - chemistry Acyltransferases - genetics Acyltransferases - metabolism Aloe - enzymology Aloe - genetics Amino Acid Sequence Analytical, structural and metabolic biochemistry Aromatic and heterocyclic compounds Biological and medical sciences Biotechnology Chromones - metabolism Fundamental and applied biological sciences. Psychology Genetic engineering Genetic technics Heterocyclic compounds, pigments Kinetics Malonyl Coenzyme A - metabolism Methods. Procedures. Technologies Molecular Sequence Data Mutagenesis, Site-Directed Other biological molecules Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Site specific mutagenesis Substrate Specificity |
| title | A Plant Type III Polyketide Synthase that Produces Pentaketide Chromone |
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