Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis
Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved i...
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| Veröffentlicht in: | ACS chemical biology 2014-02, Vol.9 (2), p.562-569 |
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| creator | Minami, Atsushi Ose, Toyoyuki Sato, Kyohei Oikawa, Azusa Kuroki, Kimiko Maenaka, Katsumi Oguri, Hiroki Oikawa, Hideaki |
| description | Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analogue to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21 × 10–5 M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction. |
| doi_str_mv | 10.1021/cb4006485 |
| format | Article |
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A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analogue to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21 × 10–5 M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction.</description><identifier>ISSN: 1554-8929</identifier><identifier>EISSN: 1554-8937</identifier><identifier>DOI: 10.1021/cb4006485</identifier><identifier>PMID: 24320215</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Allosteric Regulation ; Crystallography, X-Ray ; Epoxide Hydrolases - chemistry ; Epoxide Hydrolases - genetics ; Epoxide Hydrolases - metabolism ; Models, Molecular ; Monensin - chemistry ; Monensin - metabolism ; Mutation ; Protein Conformation ; Protein Multimerization ; Streptomyces - chemistry ; Streptomyces - enzymology ; Streptomyces - genetics ; Streptomyces - metabolism</subject><ispartof>ACS chemical biology, 2014-02, Vol.9 (2), p.562-569</ispartof><rights>Copyright © 2013 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a425t-d6879701f9824de768c2f1b6bbb21ee422a72c051a046dab5cc471a96a1322833</citedby><cites>FETCH-LOGICAL-a425t-d6879701f9824de768c2f1b6bbb21ee422a72c051a046dab5cc471a96a1322833</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/cb4006485$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/cb4006485$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,778,782,2754,27063,27911,27912,56725,56775</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24320215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Minami, Atsushi</creatorcontrib><creatorcontrib>Ose, Toyoyuki</creatorcontrib><creatorcontrib>Sato, Kyohei</creatorcontrib><creatorcontrib>Oikawa, Azusa</creatorcontrib><creatorcontrib>Kuroki, Kimiko</creatorcontrib><creatorcontrib>Maenaka, Katsumi</creatorcontrib><creatorcontrib>Oguri, Hiroki</creatorcontrib><creatorcontrib>Oikawa, Hideaki</creatorcontrib><title>Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis</title><title>ACS chemical biology</title><addtitle>ACS Chem. Biol</addtitle><description>Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analogue to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21 × 10–5 M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction.</description><subject>Allosteric Regulation</subject><subject>Crystallography, X-Ray</subject><subject>Epoxide Hydrolases - chemistry</subject><subject>Epoxide Hydrolases - genetics</subject><subject>Epoxide Hydrolases - metabolism</subject><subject>Models, Molecular</subject><subject>Monensin - chemistry</subject><subject>Monensin - metabolism</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>Protein Multimerization</subject><subject>Streptomyces - chemistry</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces - genetics</subject><subject>Streptomyces - metabolism</subject><issn>1554-8929</issn><issn>1554-8937</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1LAzEQhoMotn4c_AOSi6CH1SSb7MexlmqFSkX0vCTZbE3ZJmtmF9x_70pr8eBpXphnXpgHoQtKbilh9E4rTkjCM3GAxlQIHmV5nB7uM8tH6ARgTQiPkyw_RiPGYzYcijFaT-raQ2uC1fjVrLpattY77Cs8a_yXLQ1eNsZZt8JTCVqWBrDqscQv0oa_1Lwvg68lDHvr8LN3xsEQ7q2H3rUfBiycoaNK1mDOd_MUvT_M3qbzaLF8fJpOFpHkTLRRmWRpnhJa5RnjpUmTTLOKqkQpxagxnDGZMk0ElYQnpVRCa55SmSeSxoxlcXyKrre9TfCfnYG22FjQpq6lM76DggpC45TEVAzozRbVwQMEUxVNsBsZ-oKS4kdtsVc7sJe72k5tTLknf10OwNUWkBqKte-CG778p-gbPw1-6A</recordid><startdate>20140221</startdate><enddate>20140221</enddate><creator>Minami, Atsushi</creator><creator>Ose, Toyoyuki</creator><creator>Sato, Kyohei</creator><creator>Oikawa, Azusa</creator><creator>Kuroki, Kimiko</creator><creator>Maenaka, Katsumi</creator><creator>Oguri, Hiroki</creator><creator>Oikawa, Hideaki</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></search><sort><creationdate>20140221</creationdate><title>Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis</title><author>Minami, Atsushi ; Ose, Toyoyuki ; Sato, Kyohei ; Oikawa, Azusa ; Kuroki, Kimiko ; Maenaka, Katsumi ; Oguri, Hiroki ; Oikawa, Hideaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a425t-d6879701f9824de768c2f1b6bbb21ee422a72c051a046dab5cc471a96a1322833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Allosteric Regulation</topic><topic>Crystallography, X-Ray</topic><topic>Epoxide Hydrolases - chemistry</topic><topic>Epoxide Hydrolases - genetics</topic><topic>Epoxide Hydrolases - metabolism</topic><topic>Models, Molecular</topic><topic>Monensin - chemistry</topic><topic>Monensin - metabolism</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>Protein Multimerization</topic><topic>Streptomyces - chemistry</topic><topic>Streptomyces - enzymology</topic><topic>Streptomyces - genetics</topic><topic>Streptomyces - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Minami, Atsushi</creatorcontrib><creatorcontrib>Ose, Toyoyuki</creatorcontrib><creatorcontrib>Sato, Kyohei</creatorcontrib><creatorcontrib>Oikawa, Azusa</creatorcontrib><creatorcontrib>Kuroki, Kimiko</creatorcontrib><creatorcontrib>Maenaka, Katsumi</creatorcontrib><creatorcontrib>Oguri, Hiroki</creatorcontrib><creatorcontrib>Oikawa, Hideaki</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><jtitle>ACS chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Minami, Atsushi</au><au>Ose, Toyoyuki</au><au>Sato, Kyohei</au><au>Oikawa, Azusa</au><au>Kuroki, Kimiko</au><au>Maenaka, Katsumi</au><au>Oguri, Hiroki</au><au>Oikawa, Hideaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis</atitle><jtitle>ACS chemical biology</jtitle><addtitle>ACS Chem. Biol</addtitle><date>2014-02-21</date><risdate>2014</risdate><volume>9</volume><issue>2</issue><spage>562</spage><epage>569</epage><pages>562-569</pages><issn>1554-8929</issn><eissn>1554-8937</eissn><abstract>Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analogue to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21 × 10–5 M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24320215</pmid><doi>10.1021/cb4006485</doi><tpages>8</tpages></addata></record> |
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| subjects | Allosteric Regulation Crystallography, X-Ray Epoxide Hydrolases - chemistry Epoxide Hydrolases - genetics Epoxide Hydrolases - metabolism Models, Molecular Monensin - chemistry Monensin - metabolism Mutation Protein Conformation Protein Multimerization Streptomyces - chemistry Streptomyces - enzymology Streptomyces - genetics Streptomyces - metabolism |
| title | Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis |
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