Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity
Mg2+‐dependent catechol‐O‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta me...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2017-01, Vol.591 (2), p.312-321 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 321 |
|---|---|
| container_issue | 2 |
| container_start_page | 312 |
| container_title | FEBS letters |
| container_volume | 591 |
| creator | Siegrist, Jutta Netzer, Julia Mordhorst, Silja Karst, Lukas Gerhardt, Stefan Einsle, Oliver Richter, Michael Andexer, Jennifer N. |
| description | Mg2+‐dependent catechol‐O‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol‐O‐methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis. |
| doi_str_mv | 10.1002/1873-3468.12530 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1851290934</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1851290934</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3850-c302d6fa6cf233d06a47ec3e56a4dd49d4ebc2617dc34f2bed313af0347e75be3</originalsourceid><addsrcrecordid>eNqFkLtOAzEQRS0EIiFQ06EtaZL4sc8SogSQIqWB2vLa48RoH8HeBbbjE_hGvgQnG9LS2J7xmTPSReia4AnBmE5JmrAxC-N0QmjE8AkaHjunaIgxCcdRkrEBunDuFfs6Jdk5GtAky3DM8BB9LtpKNqauRBGISgWusa1sWutLuRFWyAascWJHBLUORJD3Lf-_-vn6LqHZdEVjReU0WOFgL9Geqa0LFHi0NJWp1oGFtakdFOC3vZumu0RnWhQOrg73CL0s5s-zx_Fy9fA0u1uOJUsj7E9MVaxFLDVlTOFYhAlIBpF_KBVmKoRc0pgkSrJQ0xwUI0xozDyWRDmwEbrtvVtbv7XgGl4aJ6EoRAV16zhJI0IznLHQo9MelbZ2zoLmW2tKYTtOMN_FzXfh8l24fB-3n7g5yNu8BHXk__L1QNwDH6aA7j8fX8zvaW_-BUfajqE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1851290934</pqid></control><display><type>article</type><title>Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Siegrist, Jutta ; Netzer, Julia ; Mordhorst, Silja ; Karst, Lukas ; Gerhardt, Stefan ; Einsle, Oliver ; Richter, Michael ; Andexer, Jennifer N.</creator><creatorcontrib>Siegrist, Jutta ; Netzer, Julia ; Mordhorst, Silja ; Karst, Lukas ; Gerhardt, Stefan ; Einsle, Oliver ; Richter, Michael ; Andexer, Jennifer N.</creatorcontrib><description>Mg2+‐dependent catechol‐O‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol‐O‐methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.12530</identifier><identifier>PMID: 27990630</identifier><language>eng</language><publisher>England</publisher><subject>Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; biocatalysis ; Catalytic Domain ; catechol ; Catechol O-Methyltransferase - chemistry ; Catechol O-Methyltransferase - metabolism ; catechol‐O‐methyltransferase ; Chromatography, High Pressure Liquid ; methylation ; Models, Molecular ; Myxococcus - enzymology ; SafC ; Stereoisomerism ; structure–function relationship ; Substrate Specificity</subject><ispartof>FEBS letters, 2017-01, Vol.591 (2), p.312-321</ispartof><rights>2016 Federation of European Biochemical Societies</rights><rights>2016 Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3850-c302d6fa6cf233d06a47ec3e56a4dd49d4ebc2617dc34f2bed313af0347e75be3</citedby><cites>FETCH-LOGICAL-c3850-c302d6fa6cf233d06a47ec3e56a4dd49d4ebc2617dc34f2bed313af0347e75be3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2F1873-3468.12530$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2F1873-3468.12530$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27990630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siegrist, Jutta</creatorcontrib><creatorcontrib>Netzer, Julia</creatorcontrib><creatorcontrib>Mordhorst, Silja</creatorcontrib><creatorcontrib>Karst, Lukas</creatorcontrib><creatorcontrib>Gerhardt, Stefan</creatorcontrib><creatorcontrib>Einsle, Oliver</creatorcontrib><creatorcontrib>Richter, Michael</creatorcontrib><creatorcontrib>Andexer, Jennifer N.</creatorcontrib><title>Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Mg2+‐dependent catechol‐O‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol‐O‐methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>biocatalysis</subject><subject>Catalytic Domain</subject><subject>catechol</subject><subject>Catechol O-Methyltransferase - chemistry</subject><subject>Catechol O-Methyltransferase - metabolism</subject><subject>catechol‐O‐methyltransferase</subject><subject>Chromatography, High Pressure Liquid</subject><subject>methylation</subject><subject>Models, Molecular</subject><subject>Myxococcus - enzymology</subject><subject>SafC</subject><subject>Stereoisomerism</subject><subject>structure–function relationship</subject><subject>Substrate Specificity</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOAzEQRS0EIiFQ06EtaZL4sc8SogSQIqWB2vLa48RoH8HeBbbjE_hGvgQnG9LS2J7xmTPSReia4AnBmE5JmrAxC-N0QmjE8AkaHjunaIgxCcdRkrEBunDuFfs6Jdk5GtAky3DM8BB9LtpKNqauRBGISgWusa1sWutLuRFWyAascWJHBLUORJD3Lf-_-vn6LqHZdEVjReU0WOFgL9Geqa0LFHi0NJWp1oGFtakdFOC3vZumu0RnWhQOrg73CL0s5s-zx_Fy9fA0u1uOJUsj7E9MVaxFLDVlTOFYhAlIBpF_KBVmKoRc0pgkSrJQ0xwUI0xozDyWRDmwEbrtvVtbv7XgGl4aJ6EoRAV16zhJI0IznLHQo9MelbZ2zoLmW2tKYTtOMN_FzXfh8l24fB-3n7g5yNu8BHXk__L1QNwDH6aA7j8fX8zvaW_-BUfajqE</recordid><startdate>201701</startdate><enddate>201701</enddate><creator>Siegrist, Jutta</creator><creator>Netzer, Julia</creator><creator>Mordhorst, Silja</creator><creator>Karst, Lukas</creator><creator>Gerhardt, Stefan</creator><creator>Einsle, Oliver</creator><creator>Richter, Michael</creator><creator>Andexer, Jennifer N.</creator><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>201701</creationdate><title>Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity</title><author>Siegrist, Jutta ; Netzer, Julia ; Mordhorst, Silja ; Karst, Lukas ; Gerhardt, Stefan ; Einsle, Oliver ; Richter, Michael ; Andexer, Jennifer N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3850-c302d6fa6cf233d06a47ec3e56a4dd49d4ebc2617dc34f2bed313af0347e75be3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>biocatalysis</topic><topic>Catalytic Domain</topic><topic>catechol</topic><topic>Catechol O-Methyltransferase - chemistry</topic><topic>Catechol O-Methyltransferase - metabolism</topic><topic>catechol‐O‐methyltransferase</topic><topic>Chromatography, High Pressure Liquid</topic><topic>methylation</topic><topic>Models, Molecular</topic><topic>Myxococcus - enzymology</topic><topic>SafC</topic><topic>Stereoisomerism</topic><topic>structure–function relationship</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siegrist, Jutta</creatorcontrib><creatorcontrib>Netzer, Julia</creatorcontrib><creatorcontrib>Mordhorst, Silja</creatorcontrib><creatorcontrib>Karst, Lukas</creatorcontrib><creatorcontrib>Gerhardt, Stefan</creatorcontrib><creatorcontrib>Einsle, Oliver</creatorcontrib><creatorcontrib>Richter, Michael</creatorcontrib><creatorcontrib>Andexer, Jennifer N.</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siegrist, Jutta</au><au>Netzer, Julia</au><au>Mordhorst, Silja</au><au>Karst, Lukas</au><au>Gerhardt, Stefan</au><au>Einsle, Oliver</au><au>Richter, Michael</au><au>Andexer, Jennifer N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2017-01</date><risdate>2017</risdate><volume>591</volume><issue>2</issue><spage>312</spage><epage>321</epage><pages>312-321</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mg2+‐dependent catechol‐O‐methyltransferases occur in animals as well as in bacteria, fungi and plants, often with a pronounced selectivity towards one of the substrate's hydroxyl groups. Here, we show that the bacterial MxSafC exhibits excellent regioselectivity for para as well as for meta methylation, depending on the substrate's characteristics. The crystal structure of MxSafC was solved in apo and in holo form. The structure complexed with a full set of substrates clearly illustrates the plasticity of the active site region. The awareness that a wide range of factors influences the regioselectivity will aid the further development of catechol‐O‐methyltransferases as well as other methyltransferases as selective and efficient biocatalysts for chemical synthesis.</abstract><cop>England</cop><pmid>27990630</pmid><doi>10.1002/1873-3468.12530</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2017-01, Vol.591 (2), p.312-321 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1851290934 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Bacterial Proteins - chemistry Bacterial Proteins - metabolism biocatalysis Catalytic Domain catechol Catechol O-Methyltransferase - chemistry Catechol O-Methyltransferase - metabolism catechol‐O‐methyltransferase Chromatography, High Pressure Liquid methylation Models, Molecular Myxococcus - enzymology SafC Stereoisomerism structure–function relationship Substrate Specificity |
| title | Functional and structural characterisation of a bacterial O‐methyltransferase and factors determining regioselectivity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T00%3A22%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20and%20structural%20characterisation%20of%20a%20bacterial%20O%E2%80%90methyltransferase%20and%20factors%20determining%20regioselectivity&rft.jtitle=FEBS%20letters&rft.au=Siegrist,%20Jutta&rft.date=2017-01&rft.volume=591&rft.issue=2&rft.spage=312&rft.epage=321&rft.pages=312-321&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1002/1873-3468.12530&rft_dat=%3Cproquest_cross%3E1851290934%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1851290934&rft_id=info:pmid/27990630&rfr_iscdi=true |