The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis
Acyl carrier protein (ACP) plays an essential role in fatty acid and polyketide biosynthesis, and most of the fatty acid synthases (FASs) and polyketide synthases (PKSs) known to date are characterized with a single ACP for each cycle of chain elongation. Polyunsaturated fatty acid (PUFA) biosynthes...
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| Veröffentlicht in: | Journal of the American Chemical Society 2008-05, Vol.130 (20), p.6336-6337 |
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| container_title | Journal of the American Chemical Society |
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| creator | Jiang, Hui Zirkle, Ross Metz, James G Braun, Lisa Richter, Leslie Van Lanen, Steven G Shen, Ben |
| description | Acyl carrier protein (ACP) plays an essential role in fatty acid and polyketide biosynthesis, and most of the fatty acid synthases (FASs) and polyketide synthases (PKSs) known to date are characterized with a single ACP for each cycle of chain elongation. Polyunsaturated fatty acid (PUFA) biosynthesis is catalyzed by the PUFA synthase, and all PUFA synthases known to date contain tandem ACPs (ranging from 5 to 9). Using the Pfa PUFA synthase from Shewanella japonica as a model system, we report here that these tandem ACPs are functionally equivalent regardless of their physical location within the PUFA synthase subunit, but the total number of ACPs controls the overall PUFA titer. These findings set the stage to interrogate other domains and subunits of PUFA synthase for their roles in controlling the final PUFA products and could potentially be exploited to improve PUFA production. |
| doi_str_mv | 10.1021/ja801911t |
| format | Article |
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Polyunsaturated fatty acid (PUFA) biosynthesis is catalyzed by the PUFA synthase, and all PUFA synthases known to date contain tandem ACPs (ranging from 5 to 9). Using the Pfa PUFA synthase from Shewanella japonica as a model system, we report here that these tandem ACPs are functionally equivalent regardless of their physical location within the PUFA synthase subunit, but the total number of ACPs controls the overall PUFA titer. 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Am. Chem. Soc</addtitle><description>Acyl carrier protein (ACP) plays an essential role in fatty acid and polyketide biosynthesis, and most of the fatty acid synthases (FASs) and polyketide synthases (PKSs) known to date are characterized with a single ACP for each cycle of chain elongation. Polyunsaturated fatty acid (PUFA) biosynthesis is catalyzed by the PUFA synthase, and all PUFA synthases known to date contain tandem ACPs (ranging from 5 to 9). Using the Pfa PUFA synthase from Shewanella japonica as a model system, we report here that these tandem ACPs are functionally equivalent regardless of their physical location within the PUFA synthase subunit, but the total number of ACPs controls the overall PUFA titer. These findings set the stage to interrogate other domains and subunits of PUFA synthase for their roles in controlling the final PUFA products and could potentially be exploited to improve PUFA production.</description><subject>Acyl Carrier Protein - metabolism</subject><subject>Docosahexaenoic Acids - metabolism</subject><subject>Eicosapentaenoic Acid - biosynthesis</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fatty Acid Synthase, Type II - biosynthesis</subject><subject>Fatty Acid Synthase, Type II - genetics</subject><subject>Fatty Acid Synthase, Type II - metabolism</subject><subject>Fatty Acids, Unsaturated - biosynthesis</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Shewanella - enzymology</subject><subject>Shewanella - genetics</subject><subject>Shewanella - metabolism</subject><subject>Shewanella japonica</subject><issn>0002-7863</issn><issn>1272-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1r3DAQBmARWppN0kP-QNGlhRzc6suSdcxum6QQ6JK6l1zE2JaJtraVSjLE_74Ku6SXQi4aDfNoBC9C55R8poTRLzuoCNWUpiO0oiUjRUmZfINWhBBWqEryY3QS4y63glX0HTqmlRBCUrFC9_WDxXd-sNj3uIapsyO-bJcBbyAEZwPeBp-sm_BXP4KbIs7XrR-WeYqQ5gDJdvgKUlryK9fhtfNxmdKDjS6eobc9DNG-P9RT9OvqW725KW5_XH_fXN4WIESVinx00Iu-o1Y0lgNvOs1k01aMgG4pI1yC7EWjtehlVSrSUyEV1UoS3nJQ_BR92u99DP7PbGMyo4utHQaYrJ-jUUQxTXT5KmSkEppRkuHFHrbBxxhsbx6DGyEshhLznLh5STzbD4elczPa7p88RJxBsQcuJvv0Mofw20jFVWnq7U9zL6_XvFS1WWf_ce-hjWbn5zDl8P7z8V8RSZV3</recordid><startdate>20080521</startdate><enddate>20080521</enddate><creator>Jiang, Hui</creator><creator>Zirkle, Ross</creator><creator>Metz, James G</creator><creator>Braun, Lisa</creator><creator>Richter, Leslie</creator><creator>Van Lanen, Steven G</creator><creator>Shen, Ben</creator><general>American Chemical Society</general><scope>BSCLL</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><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20080521</creationdate><title>The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis</title><author>Jiang, Hui ; Zirkle, Ross ; Metz, James G ; Braun, Lisa ; Richter, Leslie ; Van Lanen, Steven G ; Shen, Ben</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a448t-448daf4fd1e4be3a3bd926bc820a9c12036a6f4b994f68570f1467197603c3a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Acyl Carrier Protein - metabolism</topic><topic>Docosahexaenoic Acids - metabolism</topic><topic>Eicosapentaenoic Acid - biosynthesis</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fatty Acid Synthase, Type II - biosynthesis</topic><topic>Fatty Acid Synthase, Type II - genetics</topic><topic>Fatty Acid Synthase, Type II - metabolism</topic><topic>Fatty Acids, Unsaturated - biosynthesis</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Shewanella - enzymology</topic><topic>Shewanella - genetics</topic><topic>Shewanella - metabolism</topic><topic>Shewanella japonica</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jiang, Hui</creatorcontrib><creatorcontrib>Zirkle, Ross</creatorcontrib><creatorcontrib>Metz, James G</creatorcontrib><creatorcontrib>Braun, Lisa</creatorcontrib><creatorcontrib>Richter, Leslie</creatorcontrib><creatorcontrib>Van Lanen, Steven G</creatorcontrib><creatorcontrib>Shen, Ben</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jiang, Hui</au><au>Zirkle, Ross</au><au>Metz, James G</au><au>Braun, Lisa</au><au>Richter, Leslie</au><au>Van Lanen, Steven G</au><au>Shen, Ben</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. 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These findings set the stage to interrogate other domains and subunits of PUFA synthase for their roles in controlling the final PUFA products and could potentially be exploited to improve PUFA production.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>18444614</pmid><doi>10.1021/ja801911t</doi><tpages>2</tpages></addata></record> |
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| subjects | Acyl Carrier Protein - metabolism Docosahexaenoic Acids - metabolism Eicosapentaenoic Acid - biosynthesis Escherichia coli - enzymology Escherichia coli - genetics Fatty Acid Synthase, Type II - biosynthesis Fatty Acid Synthase, Type II - genetics Fatty Acid Synthase, Type II - metabolism Fatty Acids, Unsaturated - biosynthesis Protein Structure, Tertiary Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - metabolism Shewanella - enzymology Shewanella - genetics Shewanella - metabolism Shewanella japonica |
| title | The Role of Tandem Acyl Carrier Protein Domains in Polyunsaturated Fatty Acid Biosynthesis |
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