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Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073
Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric a...
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| Published in: | Applied and Environmental Microbiology 2009-11, Vol.75 (22), p.6986-6991 |
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| cites | cdi_FETCH-LOGICAL-c522t-3b57447927dd4700cc0a8a62a2c269099565ab7c6849d31efcb8bda95d16f73b3 |
| container_end_page | 6991 |
| container_issue | 22 |
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| container_title | Applied and Environmental Microbiology |
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| creator | Li, Qingyan Seffernick, Jennifer L Sadowsky, Michael J Wackett, Lawrence P |
| description | Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications. |
| doi_str_mv | 10.1128/AEM.01605-09 |
| format | article |
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Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>EISSN: 1098-6596</identifier><identifier>DOI: 10.1128/AEM.01605-09</identifier><identifier>PMID: 19767460</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Bacteria - classification ; Bacteria - enzymology ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biochemistry ; Biological and medical sciences ; Chelating Agents - chemistry ; Chemical compounds ; Cloning, Molecular ; Cofactors ; E coli ; Enzyme Stability ; Enzymes ; Enzymology and Protein Engineering ; Escherichia coli ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Hydrogen-Ion Concentration ; Hydrolases - chemistry ; Hydrolases - genetics ; Hydrolases - isolation & purification ; Hydrolases - metabolism ; Metabolism ; Metals - analysis ; Metals - chemistry ; Microbiology ; Microorganisms ; Phylogeny ; Substrate Specificity ; Temperature ; Triazines - metabolism</subject><ispartof>Applied and Environmental Microbiology, 2009-11, Vol.75 (22), p.6986-6991</ispartof><rights>2015 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Nov 2009</rights><rights>Copyright © 2009, American Society for Microbiology 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-3b57447927dd4700cc0a8a62a2c269099565ab7c6849d31efcb8bda95d16f73b3</citedby><cites>FETCH-LOGICAL-c522t-3b57447927dd4700cc0a8a62a2c269099565ab7c6849d31efcb8bda95d16f73b3</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/PMC2786514/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2786514/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,3177,3178,27913,27914,53780,53782</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22137080$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19767460$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Qingyan</creatorcontrib><creatorcontrib>Seffernick, Jennifer L</creatorcontrib><creatorcontrib>Sadowsky, Michael J</creatorcontrib><creatorcontrib>Wackett, Lawrence P</creatorcontrib><title>Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.</description><subject>Bacteria - classification</subject><subject>Bacteria - enzymology</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chelating Agents - chemistry</subject><subject>Chemical compounds</subject><subject>Cloning, Molecular</subject><subject>Cofactors</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Enzymology and Protein Engineering</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases - chemistry</subject><subject>Hydrolases - genetics</subject><subject>Hydrolases - isolation & purification</subject><subject>Hydrolases - metabolism</subject><subject>Metabolism</subject><subject>Metals - analysis</subject><subject>Metals - chemistry</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Phylogeny</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>Triazines - metabolism</subject><issn>0099-2240</issn><issn>1098-5336</issn><issn>1098-6596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNp9kU1v1DAQhiMEotvCjTNESIULKeNv-4K0WhWKaMWB7dmaOM5uqiRu7Sxo_z3e7qoFDpx88DOP3pm3KF4ROCOE6o_z86szIBJEBeZJMSNgdCUYk0-LGYAxFaUcjorjlG4AgIPUz4sjYpRUXMKs-LZc-ziENGHd-3KxxXETO1fOXdeUF9smhh6TL9sYhvIqhOj7HsvpfgSdnzqH5Xy5WJTMgGIvimct9sm_PLwnxfXn8-Xiorr8_uXrYn5ZOUHpVLFaKM6VoappuAJwDlCjpEgdlSZHFlJgrZzU3DSM-NbVum7QiIbIVrGanRSf9t7bTT34xvlxitjb29gNGLc2YGf__hm7tV2Fn5YqLQXhWfD-IIjhbuPTZIcuud1uow-bZFU-H3BJaCbf_ZekhBtGlcng23_Am7CJYz6DpSCM0IrubB_2kIshpejbh8wE7K5Mm8u092Va2Dlf_7nnI3xoLwOnBwCTw76NOLouPXCUEqZAw2O4dbda_-qit5gGi36wSmTKSqNlht7soRaDxVXMousfFAjLeYxWnLHfLB25eQ</recordid><startdate>20091101</startdate><enddate>20091101</enddate><creator>Li, Qingyan</creator><creator>Seffernick, Jennifer L</creator><creator>Sadowsky, Michael J</creator><creator>Wackett, Lawrence P</creator><general>American Society for Microbiology</general><general>American Society for Microbiology (ASM)</general><scope>FBQ</scope><scope>IQODW</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>7QO</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20091101</creationdate><title>Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073</title><author>Li, Qingyan ; Seffernick, Jennifer L ; Sadowsky, Michael J ; Wackett, Lawrence P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-3b57447927dd4700cc0a8a62a2c269099565ab7c6849d31efcb8bda95d16f73b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Bacteria - classification</topic><topic>Bacteria - enzymology</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Chelating Agents - chemistry</topic><topic>Chemical compounds</topic><topic>Cloning, Molecular</topic><topic>Cofactors</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Enzymology and Protein Engineering</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases - chemistry</topic><topic>Hydrolases - genetics</topic><topic>Hydrolases - isolation & purification</topic><topic>Hydrolases - metabolism</topic><topic>Metabolism</topic><topic>Metals - analysis</topic><topic>Metals - chemistry</topic><topic>Microbiology</topic><topic>Microorganisms</topic><topic>Phylogeny</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>Triazines - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Qingyan</creatorcontrib><creatorcontrib>Seffernick, Jennifer L</creatorcontrib><creatorcontrib>Sadowsky, Michael J</creatorcontrib><creatorcontrib>Wackett, Lawrence P</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Qingyan</au><au>Seffernick, Jennifer L</au><au>Sadowsky, Michael J</au><au>Wackett, Lawrence P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2009-11-01</date><risdate>2009</risdate><volume>75</volume><issue>22</issue><spage>6986</spage><epage>6991</epage><pages>6986-6991</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><eissn>1098-6596</eissn><coden>AEMIDF</coden><abstract>Cyanuric acid, a metabolic intermediate in the degradation of many s-triazine compounds, is further metabolized by cyanuric acid hydrolase. Cyanuric acid also accumulates in swimming pools due to the breakdown of the sanitizing agents di- and trichloroisocyanuric acid. Structurally stable cyanuric acid hydrolases are being considered for usage in pool water remediation. In this study, cyanuric acid hydrolase from the thermophile Moorella thermoacetica ATCC 39073 was cloned, expressed in Escherichia coli, and purified to homogeneity. The recombinant enzyme was found to have a broader temperature range and greater stability, at both elevated and low temperatures, than previously described cyanuric acid hydrolases. The enzyme had a narrow substrate specificity, acting only on cyanuric acid and N-methylisocyanuric acid. The M. thermoacetica enzyme did not require metals or other discernible cofactors for activity. Cyanuric acid hydrolase from M. thermoacetica is the most promising enzyme to use for cyanuric acid remediation applications.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>19767460</pmid><doi>10.1128/AEM.01605-09</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0099-2240 |
| ispartof | Applied and Environmental Microbiology, 2009-11, Vol.75 (22), p.6986-6991 |
| issn | 0099-2240 1098-5336 1098-6596 |
| language | eng |
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| source | American Society for Microbiology (ASM) Journals; PubMed Central |
| subjects | Bacteria - classification Bacteria - enzymology Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biological and medical sciences Chelating Agents - chemistry Chemical compounds Cloning, Molecular Cofactors E coli Enzyme Stability Enzymes Enzymology and Protein Engineering Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Hydrolases - chemistry Hydrolases - genetics Hydrolases - isolation & purification Hydrolases - metabolism Metabolism Metals - analysis Metals - chemistry Microbiology Microorganisms Phylogeny Substrate Specificity Temperature Triazines - metabolism |
| title | Thermostable Cyanuric Acid Hydrolase from Moorella thermoacetica ATCC 39073 |
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