Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway
Biosynthetic pathways containing multiple core enzymes have potential to produce structurally complex natural products. Here we mined a fungal gene cluster that contains two predicted terpene cyclases (TCs) and a nonribosomal peptide synthetase (NRPS). We showed the flv pathway produces flavunoidine...
Gespeichert in:
Veröffentlicht in: | Journal of the American Chemical Society 2020-01, Vol.142 (2), p.710-714 |
---|---|
Hauptverfasser: | , , , , , , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 714 |
---|---|
container_issue | 2 |
container_start_page | 710 |
container_title | Journal of the American Chemical Society |
container_volume | 142 |
creator | Yee, Danielle A Kakule, Thomas B Cheng, Wei Chen, Mengbin Chong, Christine T. Y Hai, Yang Hang, Leibniz F Hung, Yiu-Sun Liu, Nicholas Ohashi, Masao Okorafor, Ikechukwu C Song, Yongxiang Tang, Mancheng Zhang, Zhuan Tang, Yi |
description | Biosynthetic pathways containing multiple core enzymes have potential to produce structurally complex natural products. Here we mined a fungal gene cluster that contains two predicted terpene cyclases (TCs) and a nonribosomal peptide synthetase (NRPS). We showed the flv pathway produces flavunoidine 1, an alkaloidal terpenoid. The core of 1 is a tetracyclic, cage-like, and oxygenated sesquiterpene that is connected to dimethylcadaverine via a C–N bond and is acylated with 5,5-dimethyl-l-pipecolate. The roles of all flv enzymes are established on the basis of metabolite analysis from heterologous expression. |
doi_str_mv | 10.1021/jacs.9b13046 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7000236</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2331437039</sourcerecordid><originalsourceid>FETCH-LOGICAL-a454t-4cb840a35295f9390278429218af4dc559709921568c3bb4dd4e82989de7344a3</originalsourceid><addsrcrecordid>eNptUclOwzAUtBCIluXGGfnIgYDXxL4gAWKT2A7lbDmx07okdrFTUP-eVJQCEqenp5k38zQDwAFGJxgRfDrVVTqRJaaI5RtgiDlBGcck3wRDhBDJCpHTAdhJadqvjAi8DQYUC8FJToZgemN9aC18cN75MQw1PG9edROc0Q0c2TjrYWcSrGNooYa3izI6swIs1N7Ax-CjK0MKbX_xbGedMxZeuJAWvpvYzlXwWXeTD73YA1u1bpLdX81d8HJ9Nbq8ze6fbu4uz-8zzTjrMlaVgiFNOZG8llQiUghGJMFC18xUnMsCyX7luahoWTJjmBVECmlsQRnTdBecfenO5mVrTWV9F3WjZtG1Oi5U0E79RbybqHF4V8UyL5r3AkcrgRje5jZ1qnWpsk2jvQ3zpAilmNECUdlTj7-oVQwpRVuvbTBSy3rUsh61qqenH_5-bU3-7uPHenk1DfPo-6T-1_oEH3mZog</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2331437039</pqid></control><display><type>article</type><title>Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Yee, Danielle A ; Kakule, Thomas B ; Cheng, Wei ; Chen, Mengbin ; Chong, Christine T. Y ; Hai, Yang ; Hang, Leibniz F ; Hung, Yiu-Sun ; Liu, Nicholas ; Ohashi, Masao ; Okorafor, Ikechukwu C ; Song, Yongxiang ; Tang, Mancheng ; Zhang, Zhuan ; Tang, Yi</creator><creatorcontrib>Yee, Danielle A ; Kakule, Thomas B ; Cheng, Wei ; Chen, Mengbin ; Chong, Christine T. Y ; Hai, Yang ; Hang, Leibniz F ; Hung, Yiu-Sun ; Liu, Nicholas ; Ohashi, Masao ; Okorafor, Ikechukwu C ; Song, Yongxiang ; Tang, Mancheng ; Zhang, Zhuan ; Tang, Yi</creatorcontrib><description>Biosynthetic pathways containing multiple core enzymes have potential to produce structurally complex natural products. Here we mined a fungal gene cluster that contains two predicted terpene cyclases (TCs) and a nonribosomal peptide synthetase (NRPS). We showed the flv pathway produces flavunoidine 1, an alkaloidal terpenoid. The core of 1 is a tetracyclic, cage-like, and oxygenated sesquiterpene that is connected to dimethylcadaverine via a C–N bond and is acylated with 5,5-dimethyl-l-pipecolate. The roles of all flv enzymes are established on the basis of metabolite analysis from heterologous expression.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/jacs.9b13046</identifier><identifier>PMID: 31885262</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Alkaloids - chemistry ; Genome ; Peptides - chemistry ; Ribosomes - chemistry ; Terpenes - chemistry</subject><ispartof>Journal of the American Chemical Society, 2020-01, Vol.142 (2), p.710-714</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a454t-4cb840a35295f9390278429218af4dc559709921568c3bb4dd4e82989de7344a3</citedby><cites>FETCH-LOGICAL-a454t-4cb840a35295f9390278429218af4dc559709921568c3bb4dd4e82989de7344a3</cites><orcidid>0000-0003-1597-0141 ; 0000-0002-2039-5367</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/jacs.9b13046$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jacs.9b13046$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31885262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yee, Danielle A</creatorcontrib><creatorcontrib>Kakule, Thomas B</creatorcontrib><creatorcontrib>Cheng, Wei</creatorcontrib><creatorcontrib>Chen, Mengbin</creatorcontrib><creatorcontrib>Chong, Christine T. Y</creatorcontrib><creatorcontrib>Hai, Yang</creatorcontrib><creatorcontrib>Hang, Leibniz F</creatorcontrib><creatorcontrib>Hung, Yiu-Sun</creatorcontrib><creatorcontrib>Liu, Nicholas</creatorcontrib><creatorcontrib>Ohashi, Masao</creatorcontrib><creatorcontrib>Okorafor, Ikechukwu C</creatorcontrib><creatorcontrib>Song, Yongxiang</creatorcontrib><creatorcontrib>Tang, Mancheng</creatorcontrib><creatorcontrib>Zhang, Zhuan</creatorcontrib><creatorcontrib>Tang, Yi</creatorcontrib><title>Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Biosynthetic pathways containing multiple core enzymes have potential to produce structurally complex natural products. Here we mined a fungal gene cluster that contains two predicted terpene cyclases (TCs) and a nonribosomal peptide synthetase (NRPS). We showed the flv pathway produces flavunoidine 1, an alkaloidal terpenoid. The core of 1 is a tetracyclic, cage-like, and oxygenated sesquiterpene that is connected to dimethylcadaverine via a C–N bond and is acylated with 5,5-dimethyl-l-pipecolate. The roles of all flv enzymes are established on the basis of metabolite analysis from heterologous expression.</description><subject>Alkaloids - chemistry</subject><subject>Genome</subject><subject>Peptides - chemistry</subject><subject>Ribosomes - chemistry</subject><subject>Terpenes - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUclOwzAUtBCIluXGGfnIgYDXxL4gAWKT2A7lbDmx07okdrFTUP-eVJQCEqenp5k38zQDwAFGJxgRfDrVVTqRJaaI5RtgiDlBGcck3wRDhBDJCpHTAdhJadqvjAi8DQYUC8FJToZgemN9aC18cN75MQw1PG9edROc0Q0c2TjrYWcSrGNooYa3izI6swIs1N7Ax-CjK0MKbX_xbGedMxZeuJAWvpvYzlXwWXeTD73YA1u1bpLdX81d8HJ9Nbq8ze6fbu4uz-8zzTjrMlaVgiFNOZG8llQiUghGJMFC18xUnMsCyX7luahoWTJjmBVECmlsQRnTdBecfenO5mVrTWV9F3WjZtG1Oi5U0E79RbybqHF4V8UyL5r3AkcrgRje5jZ1qnWpsk2jvQ3zpAilmNECUdlTj7-oVQwpRVuvbTBSy3rUsh61qqenH_5-bU3-7uPHenk1DfPo-6T-1_oEH3mZog</recordid><startdate>20200115</startdate><enddate>20200115</enddate><creator>Yee, Danielle A</creator><creator>Kakule, Thomas B</creator><creator>Cheng, Wei</creator><creator>Chen, Mengbin</creator><creator>Chong, Christine T. Y</creator><creator>Hai, Yang</creator><creator>Hang, Leibniz F</creator><creator>Hung, Yiu-Sun</creator><creator>Liu, Nicholas</creator><creator>Ohashi, Masao</creator><creator>Okorafor, Ikechukwu C</creator><creator>Song, Yongxiang</creator><creator>Tang, Mancheng</creator><creator>Zhang, Zhuan</creator><creator>Tang, Yi</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><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-1597-0141</orcidid><orcidid>https://orcid.org/0000-0002-2039-5367</orcidid></search><sort><creationdate>20200115</creationdate><title>Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway</title><author>Yee, Danielle A ; Kakule, Thomas B ; Cheng, Wei ; Chen, Mengbin ; Chong, Christine T. Y ; Hai, Yang ; Hang, Leibniz F ; Hung, Yiu-Sun ; Liu, Nicholas ; Ohashi, Masao ; Okorafor, Ikechukwu C ; Song, Yongxiang ; Tang, Mancheng ; Zhang, Zhuan ; Tang, Yi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a454t-4cb840a35295f9390278429218af4dc559709921568c3bb4dd4e82989de7344a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Alkaloids - chemistry</topic><topic>Genome</topic><topic>Peptides - chemistry</topic><topic>Ribosomes - chemistry</topic><topic>Terpenes - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yee, Danielle A</creatorcontrib><creatorcontrib>Kakule, Thomas B</creatorcontrib><creatorcontrib>Cheng, Wei</creatorcontrib><creatorcontrib>Chen, Mengbin</creatorcontrib><creatorcontrib>Chong, Christine T. Y</creatorcontrib><creatorcontrib>Hai, Yang</creatorcontrib><creatorcontrib>Hang, Leibniz F</creatorcontrib><creatorcontrib>Hung, Yiu-Sun</creatorcontrib><creatorcontrib>Liu, Nicholas</creatorcontrib><creatorcontrib>Ohashi, Masao</creatorcontrib><creatorcontrib>Okorafor, Ikechukwu C</creatorcontrib><creatorcontrib>Song, Yongxiang</creatorcontrib><creatorcontrib>Tang, Mancheng</creatorcontrib><creatorcontrib>Zhang, Zhuan</creatorcontrib><creatorcontrib>Tang, Yi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yee, Danielle A</au><au>Kakule, Thomas B</au><au>Cheng, Wei</au><au>Chen, Mengbin</au><au>Chong, Christine T. Y</au><au>Hai, Yang</au><au>Hang, Leibniz F</au><au>Hung, Yiu-Sun</au><au>Liu, Nicholas</au><au>Ohashi, Masao</au><au>Okorafor, Ikechukwu C</au><au>Song, Yongxiang</au><au>Tang, Mancheng</au><au>Zhang, Zhuan</au><au>Tang, Yi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2020-01-15</date><risdate>2020</risdate><volume>142</volume><issue>2</issue><spage>710</spage><epage>714</epage><pages>710-714</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>Biosynthetic pathways containing multiple core enzymes have potential to produce structurally complex natural products. Here we mined a fungal gene cluster that contains two predicted terpene cyclases (TCs) and a nonribosomal peptide synthetase (NRPS). We showed the flv pathway produces flavunoidine 1, an alkaloidal terpenoid. The core of 1 is a tetracyclic, cage-like, and oxygenated sesquiterpene that is connected to dimethylcadaverine via a C–N bond and is acylated with 5,5-dimethyl-l-pipecolate. The roles of all flv enzymes are established on the basis of metabolite analysis from heterologous expression.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>31885262</pmid><doi>10.1021/jacs.9b13046</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0003-1597-0141</orcidid><orcidid>https://orcid.org/0000-0002-2039-5367</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0002-7863 |
ispartof | Journal of the American Chemical Society, 2020-01, Vol.142 (2), p.710-714 |
issn | 0002-7863 1520-5126 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7000236 |
source | MEDLINE; American Chemical Society Journals |
subjects | Alkaloids - chemistry Genome Peptides - chemistry Ribosomes - chemistry Terpenes - chemistry |
title | Genome Mining of Alkaloidal Terpenoids from a Hybrid Terpene and Nonribosomal Peptide Biosynthetic Pathway |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T15%3A35%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Genome%20Mining%20of%20Alkaloidal%20Terpenoids%20from%20a%20Hybrid%20Terpene%20and%20Nonribosomal%20Peptide%20Biosynthetic%20Pathway&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Yee,%20Danielle%20A&rft.date=2020-01-15&rft.volume=142&rft.issue=2&rft.spage=710&rft.epage=714&rft.pages=710-714&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/jacs.9b13046&rft_dat=%3Cproquest_pubme%3E2331437039%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2331437039&rft_id=info:pmid/31885262&rfr_iscdi=true |