Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134
2,4,5-TCP 4-monooxygenase (TftD) and 2,4,6-TCP 4-monooxygenase (TcpA) have been discovered in the biodegradation of 2,4,5-trichlorophenol (2,4,5-TCP) and 2,4,6-trichlorophenol (2,4,6-TCP). TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2...
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description | 2,4,5-TCP 4-monooxygenase (TftD) and 2,4,6-TCP 4-monooxygenase (TcpA) have been discovered in the biodegradation of 2,4,5-trichlorophenol (2,4,5-TCP) and 2,4,6-trichlorophenol (2,4,6-TCP). TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2,4,6-TCP as a substrate; however, the two enzymes produce different end products. TftD catalyzes a typical monooxygenase reaction, while TcpA catalyzes a typical monooxygenase reaction followed by a hydrolytic dechlorination. We have previously reported the 3D structure of TftD and confirmed the catalytic residue, His289. Here we have determined the crystal structure of TcpA and investigated the apparent differences in specificity and catalysis between these two closely related monooxygenases through structural comparison. Our computational docking results suggest that Ala293 in TcpA (Ile292 in TftD) is possibly responsible for the differences in substrate specificity between the two monooxygenases. We have also identified that Arg101 in TcpA could provide inductive effects/charge stabilization during hydrolytic dechlorination. The collective information provides a fundamental understanding of the catalytic reaction mechanism and the parameters for substrate specificity. The information may provide guidance for designing bioremediation strategies for polychlorophenols, a major group of environmental pollutants. |
doi_str_mv | 10.3390/ijms13089769 |
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TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2,4,6-TCP as a substrate; however, the two enzymes produce different end products. TftD catalyzes a typical monooxygenase reaction, while TcpA catalyzes a typical monooxygenase reaction followed by a hydrolytic dechlorination. We have previously reported the 3D structure of TftD and confirmed the catalytic residue, His289. Here we have determined the crystal structure of TcpA and investigated the apparent differences in specificity and catalysis between these two closely related monooxygenases through structural comparison. Our computational docking results suggest that Ala293 in TcpA (Ile292 in TftD) is possibly responsible for the differences in substrate specificity between the two monooxygenases. We have also identified that Arg101 in TcpA could provide inductive effects/charge stabilization during hydrolytic dechlorination. The collective information provides a fundamental understanding of the catalytic reaction mechanism and the parameters for substrate specificity. The information may provide guidance for designing bioremediation strategies for polychlorophenols, a major group of environmental pollutants.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms13089769</identifier><identifier>PMID: 22949829</identifier><language>eng</language><publisher>Basel: MDPI AG</publisher><subject>Biodegradation ; Bioremediation ; Crystal structure ; Enzymes ; Metabolism ; Pollutants ; Toxicity</subject><ispartof>International journal of molecular sciences, 2012-08, Vol.13 (8), p.9769-9784</ispartof><rights>Copyright MDPI AG 2012</rights><rights>2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2019-4b43cb37d6a9d514bd74530faccb06d365004ac411525b219dafd58721ddb4273</citedby><cites>FETCH-LOGICAL-c2019-4b43cb37d6a9d514bd74530faccb06d365004ac411525b219dafd58721ddb4273</cites><orcidid>0000-0002-0693-7860</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431827/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431827/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids></links><search><creatorcontrib>Hayes, Robert P.</creatorcontrib><creatorcontrib>Webb, Brian N.</creatorcontrib><creatorcontrib>Subramanian, Arun Kumar</creatorcontrib><creatorcontrib>Nissen, Mark</creatorcontrib><creatorcontrib>Popchock, Andrew</creatorcontrib><creatorcontrib>Xun, Luying</creatorcontrib><creatorcontrib>Kang, ChulHee</creatorcontrib><title>Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134</title><title>International journal of molecular sciences</title><description>2,4,5-TCP 4-monooxygenase (TftD) and 2,4,6-TCP 4-monooxygenase (TcpA) have been discovered in the biodegradation of 2,4,5-trichlorophenol (2,4,5-TCP) and 2,4,6-trichlorophenol (2,4,6-TCP). TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2,4,6-TCP as a substrate; however, the two enzymes produce different end products. TftD catalyzes a typical monooxygenase reaction, while TcpA catalyzes a typical monooxygenase reaction followed by a hydrolytic dechlorination. We have previously reported the 3D structure of TftD and confirmed the catalytic residue, His289. Here we have determined the crystal structure of TcpA and investigated the apparent differences in specificity and catalysis between these two closely related monooxygenases through structural comparison. Our computational docking results suggest that Ala293 in TcpA (Ile292 in TftD) is possibly responsible for the differences in substrate specificity between the two monooxygenases. We have also identified that Arg101 in TcpA could provide inductive effects/charge stabilization during hydrolytic dechlorination. The collective information provides a fundamental understanding of the catalytic reaction mechanism and the parameters for substrate specificity. The information may provide guidance for designing bioremediation strategies for polychlorophenols, a major group of environmental pollutants.</description><subject>Biodegradation</subject><subject>Bioremediation</subject><subject>Crystal structure</subject><subject>Enzymes</subject><subject>Metabolism</subject><subject>Pollutants</subject><subject>Toxicity</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1ks9u1DAQxi0EoqVw4wEscQFpA-M_SdYckJYspaBWVGI5W449abPs2sF2WvZJeR3SdoXaA6cZaWZ-36fRR8hLBm-FUPCuX28TEzBXdaUekUMmOS8Aqvrxvf6APEtpDcAFL9VTcsC5kmrO1SH58z3H0eYxmg013tHGZLPZ5d7SZd91GNFbTLTFfI3o6eo60OPF8oQXSxzQO_SZngUfwu_dBXqTML2nfCZnZbFqzqksHszo61WXl29oF8OWfhzjz8uwcRh7Qy0Oxk510TAGcOvjhlL9h2KHxZ7SjMN0f9W7MVGP1uQQ6dezcybkc_KkM5uEL_b1iPw4_rRqTorTb5-_NIvTwnJgqpCtFLYVtauMciWTratlKaAz1rZQOVGVANJYyVjJy5Yz5UznynnNmXOt5LU4Ih_uuMPYbtHZ6SPTK_Vka2viTgfT64cT31_qi3ClhRRsfgt4tQfE8GvElPU6jNFPnvWkWQEHVYtpa3a3ZWNIKWL3T4GBvomBvh8D8RdryqPI</recordid><startdate>20120806</startdate><enddate>20120806</enddate><creator>Hayes, Robert P.</creator><creator>Webb, Brian N.</creator><creator>Subramanian, Arun Kumar</creator><creator>Nissen, Mark</creator><creator>Popchock, Andrew</creator><creator>Xun, Luying</creator><creator>Kang, ChulHee</creator><general>MDPI AG</general><general>Molecular Diversity Preservation International (MDPI)</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0693-7860</orcidid></search><sort><creationdate>20120806</creationdate><title>Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134</title><author>Hayes, Robert P. ; Webb, Brian N. ; Subramanian, Arun Kumar ; Nissen, Mark ; Popchock, Andrew ; Xun, Luying ; Kang, ChulHee</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2019-4b43cb37d6a9d514bd74530faccb06d365004ac411525b219dafd58721ddb4273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Biodegradation</topic><topic>Bioremediation</topic><topic>Crystal structure</topic><topic>Enzymes</topic><topic>Metabolism</topic><topic>Pollutants</topic><topic>Toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hayes, Robert P.</creatorcontrib><creatorcontrib>Webb, Brian N.</creatorcontrib><creatorcontrib>Subramanian, Arun Kumar</creatorcontrib><creatorcontrib>Nissen, Mark</creatorcontrib><creatorcontrib>Popchock, Andrew</creatorcontrib><creatorcontrib>Xun, Luying</creatorcontrib><creatorcontrib>Kang, ChulHee</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hayes, Robert P.</au><au>Webb, Brian N.</au><au>Subramanian, Arun Kumar</au><au>Nissen, Mark</au><au>Popchock, Andrew</au><au>Xun, Luying</au><au>Kang, ChulHee</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134</atitle><jtitle>International journal of molecular sciences</jtitle><date>2012-08-06</date><risdate>2012</risdate><volume>13</volume><issue>8</issue><spage>9769</spage><epage>9784</epage><pages>9769-9784</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>2,4,5-TCP 4-monooxygenase (TftD) and 2,4,6-TCP 4-monooxygenase (TcpA) have been discovered in the biodegradation of 2,4,5-trichlorophenol (2,4,5-TCP) and 2,4,6-trichlorophenol (2,4,6-TCP). TcpA and TftD belong to the reduced flavin adenine dinucleotide (FADH2)-dependent monooxygenases and both use 2,4,6-TCP as a substrate; however, the two enzymes produce different end products. TftD catalyzes a typical monooxygenase reaction, while TcpA catalyzes a typical monooxygenase reaction followed by a hydrolytic dechlorination. We have previously reported the 3D structure of TftD and confirmed the catalytic residue, His289. Here we have determined the crystal structure of TcpA and investigated the apparent differences in specificity and catalysis between these two closely related monooxygenases through structural comparison. Our computational docking results suggest that Ala293 in TcpA (Ile292 in TftD) is possibly responsible for the differences in substrate specificity between the two monooxygenases. We have also identified that Arg101 in TcpA could provide inductive effects/charge stabilization during hydrolytic dechlorination. The collective information provides a fundamental understanding of the catalytic reaction mechanism and the parameters for substrate specificity. The information may provide guidance for designing bioremediation strategies for polychlorophenols, a major group of environmental pollutants.</abstract><cop>Basel</cop><pub>MDPI AG</pub><pmid>22949829</pmid><doi>10.3390/ijms13089769</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0002-0693-7860</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Biodegradation Bioremediation Crystal structure Enzymes Metabolism Pollutants Toxicity |
title | Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134 |
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