Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity
The iso-migrastatin (iso-MGS) biosynthetic gene cluster from Streptomyces platensis NRRL 18993 consists of 11 genes, featuring an acyltransferase (AT)-less type I polyketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) ide...
Gespeichert in:
Veröffentlicht in: | Journal of the American Chemical Society 2013-02, Vol.135 (7), p.2489-2492 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2492 |
---|---|
container_issue | 7 |
container_start_page | 2489 |
container_title | Journal of the American Chemical Society |
container_volume | 135 |
creator | Ma, Ming Kwong, Thomas Lim, Si-Kyu Ju, Jianhua Lohman, Jeremy R Shen, Ben |
description | The iso-migrastatin (iso-MGS) biosynthetic gene cluster from Streptomyces platensis NRRL 18993 consists of 11 genes, featuring an acyltransferase (AT)-less type I polyketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) identify two nascent products of the iso-MGS AT-less type I PKS, establishing an unprecedented novel feature for AT-less type I PKSs, and (ii) account for the formation of all known post-PKS biosynthetic intermediates generated by the three tailoring enzymes MgsIJK, which possessed significant substrate promiscuities. |
doi_str_mv | 10.1021/ja4002635 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3582021</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1291596778</sourcerecordid><originalsourceid>FETCH-LOGICAL-a405t-e64962696c7e9d012c4f27c23cd876e2bd49ff6f3591d4791cc0b4cfede4143</originalsourceid><addsrcrecordid>eNptkd9rFDEQx4Mo9qw--A_IvggKrubXZjcvgi2tLRQsXN9DLjt7l3N3c2ayyop_vGmvPRT6NDOZD9-ZzJeQ14x-ZJSzT1srKeVKVE_IglWclhXj6ilZ0Pxa1o0SR-QF4jaXkjfsOTniQmhZabEgf64DpvI69PN3SL6FYjmPaWMxJwl2WPixuMRQDn4dLSabcn3iA95CgB4_FOdg0xT9uC5urO_DXXY2_p4HwOKXT5viJAbbFstphSnalHV34HznnU_zS_Kssz3Cq_t4TJbnZzenF-XVt6-Xp1-uyvyvKpWgpFZcaeVq0C1l3MmO144L1za1Ar5qpe461YlKs1bWmjlHV9J10IJkUhyTz3vV3bQaoHUw5kV6s4t-sHE2wXrzf2f0G7MOP42oGp7PmwXe3QvE8GMCTGbw6KDv7QhhQsO4ZpVWdd1k9P0edTEgRugOYxg1t16Zg1eZffPvXgfywZwMvN0D1qHZhimO-UiPCP0FTpKeLQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1291596778</pqid></control><display><type>article</type><title>Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity</title><source>MEDLINE</source><source>ACS Publications</source><creator>Ma, Ming ; Kwong, Thomas ; Lim, Si-Kyu ; Ju, Jianhua ; Lohman, Jeremy R ; Shen, Ben</creator><creatorcontrib>Ma, Ming ; Kwong, Thomas ; Lim, Si-Kyu ; Ju, Jianhua ; Lohman, Jeremy R ; Shen, Ben</creatorcontrib><description>The iso-migrastatin (iso-MGS) biosynthetic gene cluster from Streptomyces platensis NRRL 18993 consists of 11 genes, featuring an acyltransferase (AT)-less type I polyketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) identify two nascent products of the iso-MGS AT-less type I PKS, establishing an unprecedented novel feature for AT-less type I PKSs, and (ii) account for the formation of all known post-PKS biosynthetic intermediates generated by the three tailoring enzymes MgsIJK, which possessed significant substrate promiscuities.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja4002635</identifier><identifier>PMID: 23394593</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Biosynthetic Pathways ; Macrolides - chemistry ; Molecular Structure ; Piperidones - chemistry ; Polyketide Synthases - chemistry ; Streptomyces - enzymology ; Streptomyces - genetics ; Substrate Specificity</subject><ispartof>Journal of the American Chemical Society, 2013-02, Vol.135 (7), p.2489-2492</ispartof><rights>Copyright © 2013 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a405t-e64962696c7e9d012c4f27c23cd876e2bd49ff6f3591d4791cc0b4cfede4143</citedby><cites>FETCH-LOGICAL-a405t-e64962696c7e9d012c4f27c23cd876e2bd49ff6f3591d4791cc0b4cfede4143</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/ja4002635$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja4002635$$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/23394593$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ma, Ming</creatorcontrib><creatorcontrib>Kwong, Thomas</creatorcontrib><creatorcontrib>Lim, Si-Kyu</creatorcontrib><creatorcontrib>Ju, Jianhua</creatorcontrib><creatorcontrib>Lohman, Jeremy R</creatorcontrib><creatorcontrib>Shen, Ben</creatorcontrib><title>Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The iso-migrastatin (iso-MGS) biosynthetic gene cluster from Streptomyces platensis NRRL 18993 consists of 11 genes, featuring an acyltransferase (AT)-less type I polyketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) identify two nascent products of the iso-MGS AT-less type I PKS, establishing an unprecedented novel feature for AT-less type I PKSs, and (ii) account for the formation of all known post-PKS biosynthetic intermediates generated by the three tailoring enzymes MgsIJK, which possessed significant substrate promiscuities.</description><subject>Biosynthetic Pathways</subject><subject>Macrolides - chemistry</subject><subject>Molecular Structure</subject><subject>Piperidones - chemistry</subject><subject>Polyketide Synthases - chemistry</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces - genetics</subject><subject>Substrate Specificity</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkd9rFDEQx4Mo9qw--A_IvggKrubXZjcvgi2tLRQsXN9DLjt7l3N3c2ayyop_vGmvPRT6NDOZD9-ZzJeQ14x-ZJSzT1srKeVKVE_IglWclhXj6ilZ0Pxa1o0SR-QF4jaXkjfsOTniQmhZabEgf64DpvI69PN3SL6FYjmPaWMxJwl2WPixuMRQDn4dLSabcn3iA95CgB4_FOdg0xT9uC5urO_DXXY2_p4HwOKXT5viJAbbFstphSnalHV34HznnU_zS_Kssz3Cq_t4TJbnZzenF-XVt6-Xp1-uyvyvKpWgpFZcaeVq0C1l3MmO144L1za1Ar5qpe461YlKs1bWmjlHV9J10IJkUhyTz3vV3bQaoHUw5kV6s4t-sHE2wXrzf2f0G7MOP42oGp7PmwXe3QvE8GMCTGbw6KDv7QhhQsO4ZpVWdd1k9P0edTEgRugOYxg1t16Zg1eZffPvXgfywZwMvN0D1qHZhimO-UiPCP0FTpKeLQ</recordid><startdate>20130220</startdate><enddate>20130220</enddate><creator>Ma, Ming</creator><creator>Kwong, Thomas</creator><creator>Lim, Si-Kyu</creator><creator>Ju, Jianhua</creator><creator>Lohman, Jeremy R</creator><creator>Shen, Ben</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></search><sort><creationdate>20130220</creationdate><title>Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity</title><author>Ma, Ming ; Kwong, Thomas ; Lim, Si-Kyu ; Ju, Jianhua ; Lohman, Jeremy R ; Shen, Ben</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a405t-e64962696c7e9d012c4f27c23cd876e2bd49ff6f3591d4791cc0b4cfede4143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Biosynthetic Pathways</topic><topic>Macrolides - chemistry</topic><topic>Molecular Structure</topic><topic>Piperidones - chemistry</topic><topic>Polyketide Synthases - chemistry</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces - genetics</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ma, Ming</creatorcontrib><creatorcontrib>Kwong, Thomas</creatorcontrib><creatorcontrib>Lim, Si-Kyu</creatorcontrib><creatorcontrib>Ju, Jianhua</creatorcontrib><creatorcontrib>Lohman, Jeremy R</creatorcontrib><creatorcontrib>Shen, Ben</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>Ma, Ming</au><au>Kwong, Thomas</au><au>Lim, Si-Kyu</au><au>Ju, Jianhua</au><au>Lohman, Jeremy R</au><au>Shen, Ben</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2013-02-20</date><risdate>2013</risdate><volume>135</volume><issue>7</issue><spage>2489</spage><epage>2492</epage><pages>2489-2492</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>The iso-migrastatin (iso-MGS) biosynthetic gene cluster from Streptomyces platensis NRRL 18993 consists of 11 genes, featuring an acyltransferase (AT)-less type I polyketide synthase (PKS) and three tailoring enzymes MgsIJK. Systematic inactivation of mgsIJK in S. platensis enabled us to (i) identify two nascent products of the iso-MGS AT-less type I PKS, establishing an unprecedented novel feature for AT-less type I PKSs, and (ii) account for the formation of all known post-PKS biosynthetic intermediates generated by the three tailoring enzymes MgsIJK, which possessed significant substrate promiscuities.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>23394593</pmid><doi>10.1021/ja4002635</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0002-7863 |
ispartof | Journal of the American Chemical Society, 2013-02, Vol.135 (7), p.2489-2492 |
issn | 0002-7863 1520-5126 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3582021 |
source | MEDLINE; ACS Publications |
subjects | Biosynthetic Pathways Macrolides - chemistry Molecular Structure Piperidones - chemistry Polyketide Synthases - chemistry Streptomyces - enzymology Streptomyces - genetics Substrate Specificity |
title | Post-Polyketide Synthase Steps in Iso-migrastatin Biosynthesis, Featuring Tailoring Enzymes with Broad Substrate Specificity |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T23%3A56%3A57IST&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=Post-Polyketide%20Synthase%20Steps%20in%20Iso-migrastatin%20Biosynthesis,%20Featuring%20Tailoring%20Enzymes%20with%20Broad%20Substrate%20Specificity&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Ma,%20Ming&rft.date=2013-02-20&rft.volume=135&rft.issue=7&rft.spage=2489&rft.epage=2492&rft.pages=2489-2492&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/ja4002635&rft_dat=%3Cproquest_pubme%3E1291596778%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=1291596778&rft_id=info:pmid/23394593&rfr_iscdi=true |