A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Sargassum fusiforme Exhibits Broad Substrate and Catalysis Specificity
A type III polyketide synthase (SfuPKS1) from the edible seaweed Sargassum fusiforme was molecularly cloned and biochemically characterized. The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2021-12, Vol.69 (48), p.14643-14649 |
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| container_issue | 48 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Zhao, Dong-Sheng Hu, Zhi-Wei Dong, Ling-Li Wan, Xiao-Jie Wang, Shengqin Li, Nan Wang, Yao Li, Shu-Ming Zou, Hui-Xi Yan, Xiufeng |
| description | A type III polyketide synthase (SfuPKS1) from the edible seaweed Sargassum fusiforme was molecularly cloned and biochemically characterized. The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri- and/or tetraketides. Moreover, it can also utilize phenylpropanoyl-CoA to synthesize phloroglucinol derivatives through Claisen-type cyclization, exhibiting broad substrate and catalysis specificity. Furthermore, the catalytic efficiency (kcat /KM ) for acetyl-CoA was 11.8-fold higher than that for 4-coumaroyl-CoA. A pathway for the synthesis of naringenin involving SfuPKS1 was also constructed in Escherichia coli by recombinant means, resulting in 4.9 mg of naringenin per liter. |
| doi_str_mv | 10.1021/acs.jafc.1c05868 |
| format | Article |
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The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri- and/or tetraketides. Moreover, it can also utilize phenylpropanoyl-CoA to synthesize phloroglucinol derivatives through Claisen-type cyclization, exhibiting broad substrate and catalysis specificity. Furthermore, the catalytic efficiency (kcat /KM ) for acetyl-CoA was 11.8-fold higher than that for 4-coumaroyl-CoA. A pathway for the synthesis of naringenin involving SfuPKS1 was also constructed in Escherichia coli by recombinant means, resulting in 4.9 mg of naringenin per liter.</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.1c05868</identifier><identifier>PMID: 34812623</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Acyltransferases ; Biotechnology and Biological Transformations ; Catalysis ; Kinetics ; Sargassum ; Seaweed ; Substrate Specificity</subject><ispartof>Journal of agricultural and food chemistry, 2021-12, Vol.69 (48), p.14643-14649</ispartof><rights>2021 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a402t-5a0b1c35230ea642bea1667e7ef37841263ad52f0e13b59a7e1d5d425b4dde13</citedby><cites>FETCH-LOGICAL-a402t-5a0b1c35230ea642bea1667e7ef37841263ad52f0e13b59a7e1d5d425b4dde13</cites><orcidid>0000-0001-5127-494X ; 0000-0001-6351-3055 ; 0000-0002-8141-8059 ; 0000-0002-2023-0028 ; 0000-0002-5513-6322 ; 0000-0002-9840-8981 ; 0000-0003-3337-209X ; 0000-0002-1795-4180 ; 0000-0002-4629-8151 ; 0000-0003-4583-2655</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jafc.1c05868$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jafc.1c05868$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34812623$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhao, Dong-Sheng</creatorcontrib><creatorcontrib>Hu, Zhi-Wei</creatorcontrib><creatorcontrib>Dong, Ling-Li</creatorcontrib><creatorcontrib>Wan, Xiao-Jie</creatorcontrib><creatorcontrib>Wang, Shengqin</creatorcontrib><creatorcontrib>Li, Nan</creatorcontrib><creatorcontrib>Wang, Yao</creatorcontrib><creatorcontrib>Li, Shu-Ming</creatorcontrib><creatorcontrib>Zou, Hui-Xi</creatorcontrib><creatorcontrib>Yan, Xiufeng</creatorcontrib><title>A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Sargassum fusiforme Exhibits Broad Substrate and Catalysis Specificity</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>A type III polyketide synthase (SfuPKS1) from the edible seaweed Sargassum fusiforme was molecularly cloned and biochemically characterized. The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri- and/or tetraketides. Moreover, it can also utilize phenylpropanoyl-CoA to synthesize phloroglucinol derivatives through Claisen-type cyclization, exhibiting broad substrate and catalysis specificity. Furthermore, the catalytic efficiency (kcat /KM ) for acetyl-CoA was 11.8-fold higher than that for 4-coumaroyl-CoA. A pathway for the synthesis of naringenin involving SfuPKS1 was also constructed in Escherichia coli by recombinant means, resulting in 4.9 mg of naringenin per liter.</description><subject>Acyltransferases</subject><subject>Biotechnology and Biological Transformations</subject><subject>Catalysis</subject><subject>Kinetics</subject><subject>Sargassum</subject><subject>Seaweed</subject><subject>Substrate Specificity</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtLxDAUhYMoOj72riRLBTsmadPWpQ4-ioJCZ19umxsn2k6HJEX7L_zJRmd05-rC4TsH7kfIMWdTzgS_gMZNX0E3U94wmaf5FplwKVgkOc-3yYQFJsplyvfIvnOvjLFcZmyX7MVJzkUq4gn5vKLzcYW0KAr63LfjG3qjkJbj0i_AIT0t9fD8UPIzWri-BY-Katt31C-Q3ihTt4FFeMeQl2BfwLmho3pwRve2C8jHwtTGO3ptewjIUDtvwwqFpaIz8NCOzjharrAx2jTGj4dkR0Pr8GhzD8j89mY-u48en-6K2dVjBAkTPpLAat7EUsQMIU1EjcDTNMMMdZzlSfguBiWFZsjjWl5ChlxJlQhZJ0qF7ICw9Wxje-cs6mplTQd2rDirvt1WwW317bbauA2Vk3VlNdQdqr_Cr8wAnK-Bn2o_2GV44P-9L1fmhtM</recordid><startdate>20211208</startdate><enddate>20211208</enddate><creator>Zhao, Dong-Sheng</creator><creator>Hu, Zhi-Wei</creator><creator>Dong, Ling-Li</creator><creator>Wan, Xiao-Jie</creator><creator>Wang, Shengqin</creator><creator>Li, Nan</creator><creator>Wang, Yao</creator><creator>Li, Shu-Ming</creator><creator>Zou, Hui-Xi</creator><creator>Yan, Xiufeng</creator><general>American Chemical Society</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><orcidid>https://orcid.org/0000-0001-5127-494X</orcidid><orcidid>https://orcid.org/0000-0001-6351-3055</orcidid><orcidid>https://orcid.org/0000-0002-8141-8059</orcidid><orcidid>https://orcid.org/0000-0002-2023-0028</orcidid><orcidid>https://orcid.org/0000-0002-5513-6322</orcidid><orcidid>https://orcid.org/0000-0002-9840-8981</orcidid><orcidid>https://orcid.org/0000-0003-3337-209X</orcidid><orcidid>https://orcid.org/0000-0002-1795-4180</orcidid><orcidid>https://orcid.org/0000-0002-4629-8151</orcidid><orcidid>https://orcid.org/0000-0003-4583-2655</orcidid></search><sort><creationdate>20211208</creationdate><title>A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Sargassum fusiforme Exhibits Broad Substrate and Catalysis Specificity</title><author>Zhao, Dong-Sheng ; Hu, Zhi-Wei ; Dong, Ling-Li ; Wan, Xiao-Jie ; Wang, Shengqin ; Li, Nan ; Wang, Yao ; Li, Shu-Ming ; Zou, Hui-Xi ; Yan, Xiufeng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a402t-5a0b1c35230ea642bea1667e7ef37841263ad52f0e13b59a7e1d5d425b4dde13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Acyltransferases</topic><topic>Biotechnology and Biological Transformations</topic><topic>Catalysis</topic><topic>Kinetics</topic><topic>Sargassum</topic><topic>Seaweed</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhao, Dong-Sheng</creatorcontrib><creatorcontrib>Hu, Zhi-Wei</creatorcontrib><creatorcontrib>Dong, Ling-Li</creatorcontrib><creatorcontrib>Wan, Xiao-Jie</creatorcontrib><creatorcontrib>Wang, Shengqin</creatorcontrib><creatorcontrib>Li, Nan</creatorcontrib><creatorcontrib>Wang, Yao</creatorcontrib><creatorcontrib>Li, Shu-Ming</creatorcontrib><creatorcontrib>Zou, Hui-Xi</creatorcontrib><creatorcontrib>Yan, Xiufeng</creatorcontrib><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 agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhao, Dong-Sheng</au><au>Hu, Zhi-Wei</au><au>Dong, Ling-Li</au><au>Wan, Xiao-Jie</au><au>Wang, Shengqin</au><au>Li, Nan</au><au>Wang, Yao</au><au>Li, Shu-Ming</au><au>Zou, Hui-Xi</au><au>Yan, Xiufeng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Sargassum fusiforme Exhibits Broad Substrate and Catalysis Specificity</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2021-12-08</date><risdate>2021</risdate><volume>69</volume><issue>48</issue><spage>14643</spage><epage>14649</epage><pages>14643-14649</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><abstract>A type III polyketide synthase (SfuPKS1) from the edible seaweed Sargassum fusiforme was molecularly cloned and biochemically characterized. The recombinant SfuPKS1 catalyzed the condensation of fatty acyl-CoA with two or three malonyl-CoA using lactone-type intramolecular cyclization to produce tri- and/or tetraketides. Moreover, it can also utilize phenylpropanoyl-CoA to synthesize phloroglucinol derivatives through Claisen-type cyclization, exhibiting broad substrate and catalysis specificity. Furthermore, the catalytic efficiency (kcat /KM ) for acetyl-CoA was 11.8-fold higher than that for 4-coumaroyl-CoA. 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| subjects | Acyltransferases Biotechnology and Biological Transformations Catalysis Kinetics Sargassum Seaweed Substrate Specificity |
| title | A Type III Polyketide Synthase (SfuPKS1) Isolated from the Edible Seaweed Sargassum fusiforme Exhibits Broad Substrate and Catalysis Specificity |
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