Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides
Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the cry...
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| Veröffentlicht in: | PloS one 2015-04, Vol.10 (4), p.e0123430-e0123430 |
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| creator | Leite, José P Duarte, Márcia Paiva, Ana M Ferreira-da-Silva, Frederico Matias, Pedro M Nunes, Olga C Gales, Luís |
| description | Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the crystal structure of recombinant molinate hydrolase at 2.27 Å. The structure reveals a homotetramer with a single mononuclear metal-dependent active site per monomer. The active site architecture shows similarities with other amidohydrolases and enables us to propose a general acid-base catalysis mechanism for molinate hydrolysis. Molinate hydrolase is unable to degrade bulkier thiocarbamate pesticides such as thiobencarb which is used mostly in rice crops. Using a structural-based approach, we were able to generate a mutant (Arg187Ala) that efficiently degrades thiobencarb. The engineered enzyme is suitable for the development of a broader thiocarbamate bioremediation system. |
| doi_str_mv | 10.1371/journal.pone.0123430 |
| format | Article |
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The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the crystal structure of recombinant molinate hydrolase at 2.27 Å. The structure reveals a homotetramer with a single mononuclear metal-dependent active site per monomer. The active site architecture shows similarities with other amidohydrolases and enables us to propose a general acid-base catalysis mechanism for molinate hydrolysis. Molinate hydrolase is unable to degrade bulkier thiocarbamate pesticides such as thiobencarb which is used mostly in rice crops. Using a structural-based approach, we were able to generate a mutant (Arg187Ala) that efficiently degrades thiobencarb. The engineered enzyme is suitable for the development of a broader thiocarbamate bioremediation system.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0123430</identifier><identifier>PMID: 25905461</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Agrochemicals ; Amidohydrolases - chemistry ; Azepines - chemistry ; Biodegradation, Environmental ; Bioremediation ; Catalysis ; Catalytic Domain ; Cereal crops ; Crop fields ; Crystal structure ; Crystallography, X-Ray - methods ; Degradation ; Hydrolase ; Hydrolases ; Hydrolases - chemistry ; Hydrolysis ; Molinate ; Oryza ; Oryza - growth & development ; Pesticides ; Pesticides - chemistry ; Rice fields ; Thiobencarb ; Thiocarbamate pesticides ; Thiocarbamates - chemistry</subject><ispartof>PloS one, 2015-04, Vol.10 (4), p.e0123430-e0123430</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Leite et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Leite et al 2015 Leite et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c719t-14bfaf5e5e15457d835ccd9a28f77aadf466034fbc4664cf246ec99ac034f0683</citedby><cites>FETCH-LOGICAL-c719t-14bfaf5e5e15457d835ccd9a28f77aadf466034fbc4664cf246ec99ac034f0683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4407906/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4407906/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25905461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Hofmann, Andreas</contributor><creatorcontrib>Leite, José P</creatorcontrib><creatorcontrib>Duarte, Márcia</creatorcontrib><creatorcontrib>Paiva, Ana M</creatorcontrib><creatorcontrib>Ferreira-da-Silva, Frederico</creatorcontrib><creatorcontrib>Matias, Pedro M</creatorcontrib><creatorcontrib>Nunes, Olga C</creatorcontrib><creatorcontrib>Gales, Luís</creatorcontrib><title>Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the crystal structure of recombinant molinate hydrolase at 2.27 Å. The structure reveals a homotetramer with a single mononuclear metal-dependent active site per monomer. The active site architecture shows similarities with other amidohydrolases and enables us to propose a general acid-base catalysis mechanism for molinate hydrolysis. Molinate hydrolase is unable to degrade bulkier thiocarbamate pesticides such as thiobencarb which is used mostly in rice crops. Using a structural-based approach, we were able to generate a mutant (Arg187Ala) that efficiently degrades thiobencarb. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leite, José P</au><au>Duarte, Márcia</au><au>Paiva, Ana M</au><au>Ferreira-da-Silva, Frederico</au><au>Matias, Pedro M</au><au>Nunes, Olga C</au><au>Gales, Luís</au><au>Hofmann, Andreas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-04-23</date><risdate>2015</risdate><volume>10</volume><issue>4</issue><spage>e0123430</spage><epage>e0123430</epage><pages>e0123430-e0123430</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Molinate is a recalcitrant thiocarbamate used to control grass weeds in rice fields. The recently described molinate hydrolase, from Gulosibacter molinativorax ON4T, plays a key role in the only known molinate degradation pathway ending in the formation of innocuous compounds. Here we report the crystal structure of recombinant molinate hydrolase at 2.27 Å. The structure reveals a homotetramer with a single mononuclear metal-dependent active site per monomer. The active site architecture shows similarities with other amidohydrolases and enables us to propose a general acid-base catalysis mechanism for molinate hydrolysis. Molinate hydrolase is unable to degrade bulkier thiocarbamate pesticides such as thiobencarb which is used mostly in rice crops. Using a structural-based approach, we were able to generate a mutant (Arg187Ala) that efficiently degrades thiobencarb. The engineered enzyme is suitable for the development of a broader thiocarbamate bioremediation system.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25905461</pmid><doi>10.1371/journal.pone.0123430</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Agrochemicals Amidohydrolases - chemistry Azepines - chemistry Biodegradation, Environmental Bioremediation Catalysis Catalytic Domain Cereal crops Crop fields Crystal structure Crystallography, X-Ray - methods Degradation Hydrolase Hydrolases Hydrolases - chemistry Hydrolysis Molinate Oryza Oryza - growth & development Pesticides Pesticides - chemistry Rice fields Thiobencarb Thiocarbamate pesticides Thiocarbamates - chemistry |
| title | Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides |
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