5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate
The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) catalyzes the penultimate step of the shikimate pathway, and is the target of the broad-spectrum herbicide glyphosate. Kinetic analysis of the cloned EPSPS from Staphylococcus aureus revealed that this enzyme exerts a high tolerance to g...
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| Veröffentlicht in: | FEBS letters 2005-01, Vol.579 (3), p.728-732 |
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| creator | Priestman, Melanie A. Funke, Todd Singh, Inder M. Crupper, Scott S. Schönbrunn, Ernst |
| description | The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) catalyzes the penultimate step of the shikimate pathway, and is the target of the broad-spectrum herbicide glyphosate. Kinetic analysis of the cloned EPSPS from
Staphylococcus aureus revealed that this enzyme exerts a high tolerance to glyphosate, while maintaining a high affinity for its substrate phosphoenolpyruvate. Enzymatic activity is markedly influenced by monovalent cations such as potassium or ammonium, which is due to an increase in catalytic turnover. However, insensitivity to glyphosate appears to be independent from the presence of cations. Therefore, we propose that the
Staphylococcus aureus EPSPS should be classified as a class II EPSPS. This research illustrates a critical mechanism of glyphosate resistance naturally occurring in certain pathogenic bacteria. |
| doi_str_mv | 10.1016/j.febslet.2004.12.057 |
| format | Article |
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Staphylococcus aureus revealed that this enzyme exerts a high tolerance to glyphosate, while maintaining a high affinity for its substrate phosphoenolpyruvate. Enzymatic activity is markedly influenced by monovalent cations such as potassium or ammonium, which is due to an increase in catalytic turnover. However, insensitivity to glyphosate appears to be independent from the presence of cations. Therefore, we propose that the
Staphylococcus aureus EPSPS should be classified as a class II EPSPS. This research illustrates a critical mechanism of glyphosate resistance naturally occurring in certain pathogenic bacteria.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2004.12.057</identifier><identifier>PMID: 15670836</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>3-Phosphoshikimate 1-Carboxyvinyltransferase ; 5-enolpyruvylshikimate-3-phosphate synthase ; Alkyl and Aryl Transferases - drug effects ; Alkyl and Aryl Transferases - genetics ; Alkyl and Aryl Transferases - isolation & purification ; Antibiotic ; Base Sequence ; Cloning, Molecular ; DNA Primers ; Electrophoresis, Polyacrylamide Gel ; Enzyme kinetics ; EPSPS ; Glycine - analogs & derivatives ; Glycine - pharmacology ; Glyphosate ; Herbicide resistance ; Kinetics ; Pathogen ; PEP ; phosphoenolpyruvate ; Polymerase Chain Reaction ; S3P ; shikimate-3-phosphate ; Staphylococcus aureus ; Staphylococcus aureus - enzymology</subject><ispartof>FEBS letters, 2005-01, Vol.579 (3), p.728-732</ispartof><rights>2005</rights><rights>FEBS Letters 579 (2005) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5068-85221c5ca74efa558afd8c9b547f5b733167966d768513592abfa1567488c0c43</citedby><cites>FETCH-LOGICAL-c5068-85221c5ca74efa558afd8c9b547f5b733167966d768513592abfa1567488c0c43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2004.12.057$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2004.12.057$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15670836$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Priestman, Melanie A.</creatorcontrib><creatorcontrib>Funke, Todd</creatorcontrib><creatorcontrib>Singh, Inder M.</creatorcontrib><creatorcontrib>Crupper, Scott S.</creatorcontrib><creatorcontrib>Schönbrunn, Ernst</creatorcontrib><title>5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) catalyzes the penultimate step of the shikimate pathway, and is the target of the broad-spectrum herbicide glyphosate. Kinetic analysis of the cloned EPSPS from
Staphylococcus aureus revealed that this enzyme exerts a high tolerance to glyphosate, while maintaining a high affinity for its substrate phosphoenolpyruvate. Enzymatic activity is markedly influenced by monovalent cations such as potassium or ammonium, which is due to an increase in catalytic turnover. However, insensitivity to glyphosate appears to be independent from the presence of cations. Therefore, we propose that the
Staphylococcus aureus EPSPS should be classified as a class II EPSPS. This research illustrates a critical mechanism of glyphosate resistance naturally occurring in certain pathogenic bacteria.</description><subject>3-Phosphoshikimate 1-Carboxyvinyltransferase</subject><subject>5-enolpyruvylshikimate-3-phosphate synthase</subject><subject>Alkyl and Aryl Transferases - drug effects</subject><subject>Alkyl and Aryl Transferases - genetics</subject><subject>Alkyl and Aryl Transferases - isolation & purification</subject><subject>Antibiotic</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA Primers</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme kinetics</subject><subject>EPSPS</subject><subject>Glycine - analogs & derivatives</subject><subject>Glycine - pharmacology</subject><subject>Glyphosate</subject><subject>Herbicide resistance</subject><subject>Kinetics</subject><subject>Pathogen</subject><subject>PEP</subject><subject>phosphoenolpyruvate</subject><subject>Polymerase Chain Reaction</subject><subject>S3P</subject><subject>shikimate-3-phosphate</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - enzymology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1q3DAURkVJaaZpHyHFq-zsSpb141VpwqQJBLpIuxayfF1rorFcyZ7gt4_MDGSZgOBK8N0j6R6ELgkuCCb8-67ooIkOpqLEuCpIWWAmPqANkYLmtOLyDG0wJlXORE3P0ecYdzidJak_oXPCuMCS8g0yLN8O3o1LmA-Li719sns9QU7zsfdx7NM-i8sw9TpC1gW_zx4nPfaL88YbM8dMzwFSsWkNEYZoJ3uAbPLZP7esiAT4gj522kX4eqoX6O_t9s_NXf7w-9f9zc-H3DDMZS5ZWRLDjBYVdJoxqbtWmrphlehYIyglXNSct4JLRiirS910ev1JJaXBpqIX6OrIHYP_P0Oc1N5GA87pAfwcFRdUYkrYm0FSCyw4JinIjkETfIwBOjWGNJ-wKILVqkHt1EmDWjUoUqqkIfV9O10wN3toX7tOc0-Bu2Pg2TpY3kdVt9vr8nF1uirFbNVZyoT6cURBGu3BQlDRWBgMtDaAmVTr7RuvfQFEHbJg</recordid><startdate>20050131</startdate><enddate>20050131</enddate><creator>Priestman, Melanie A.</creator><creator>Funke, Todd</creator><creator>Singh, Inder M.</creator><creator>Crupper, Scott S.</creator><creator>Schönbrunn, Ernst</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20050131</creationdate><title>5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate</title><author>Priestman, Melanie A. ; Funke, Todd ; Singh, Inder M. ; Crupper, Scott S. ; Schönbrunn, Ernst</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5068-85221c5ca74efa558afd8c9b547f5b733167966d768513592abfa1567488c0c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>3-Phosphoshikimate 1-Carboxyvinyltransferase</topic><topic>5-enolpyruvylshikimate-3-phosphate synthase</topic><topic>Alkyl and Aryl Transferases - drug effects</topic><topic>Alkyl and Aryl Transferases - genetics</topic><topic>Alkyl and Aryl Transferases - isolation & purification</topic><topic>Antibiotic</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA Primers</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme kinetics</topic><topic>EPSPS</topic><topic>Glycine - analogs & derivatives</topic><topic>Glycine - pharmacology</topic><topic>Glyphosate</topic><topic>Herbicide resistance</topic><topic>Kinetics</topic><topic>Pathogen</topic><topic>PEP</topic><topic>phosphoenolpyruvate</topic><topic>Polymerase Chain Reaction</topic><topic>S3P</topic><topic>shikimate-3-phosphate</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Priestman, Melanie A.</creatorcontrib><creatorcontrib>Funke, Todd</creatorcontrib><creatorcontrib>Singh, Inder M.</creatorcontrib><creatorcontrib>Crupper, Scott S.</creatorcontrib><creatorcontrib>Schönbrunn, Ernst</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Priestman, Melanie A.</au><au>Funke, Todd</au><au>Singh, Inder M.</au><au>Crupper, Scott S.</au><au>Schönbrunn, Ernst</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2005-01-31</date><risdate>2005</risdate><volume>579</volume><issue>3</issue><spage>728</spage><epage>732</epage><pages>728-732</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The enzyme 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) catalyzes the penultimate step of the shikimate pathway, and is the target of the broad-spectrum herbicide glyphosate. Kinetic analysis of the cloned EPSPS from
Staphylococcus aureus revealed that this enzyme exerts a high tolerance to glyphosate, while maintaining a high affinity for its substrate phosphoenolpyruvate. Enzymatic activity is markedly influenced by monovalent cations such as potassium or ammonium, which is due to an increase in catalytic turnover. However, insensitivity to glyphosate appears to be independent from the presence of cations. Therefore, we propose that the
Staphylococcus aureus EPSPS should be classified as a class II EPSPS. This research illustrates a critical mechanism of glyphosate resistance naturally occurring in certain pathogenic bacteria.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15670836</pmid><doi>10.1016/j.febslet.2004.12.057</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 3-Phosphoshikimate 1-Carboxyvinyltransferase 5-enolpyruvylshikimate-3-phosphate synthase Alkyl and Aryl Transferases - drug effects Alkyl and Aryl Transferases - genetics Alkyl and Aryl Transferases - isolation & purification Antibiotic Base Sequence Cloning, Molecular DNA Primers Electrophoresis, Polyacrylamide Gel Enzyme kinetics EPSPS Glycine - analogs & derivatives Glycine - pharmacology Glyphosate Herbicide resistance Kinetics Pathogen PEP phosphoenolpyruvate Polymerase Chain Reaction S3P shikimate-3-phosphate Staphylococcus aureus Staphylococcus aureus - enzymology |
| title | 5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate |
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