Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning
Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazino...
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| Veröffentlicht in: | Journal of Pesticide Science 2020/11/20, Vol.45(4), pp.238-240 |
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| container_title | Journal of Pesticide Science |
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| creator | Yamamoto, Kohji Yamaguchi, Misuzu Yamada, Naotaka |
| description | Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity. |
| doi_str_mv | 10.1584/jpestics.D20-036 |
| format | Article |
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Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.</description><identifier>ISSN: 1348-589X</identifier><identifier>EISSN: 1349-0923</identifier><identifier>DOI: 10.1584/jpestics.D20-036</identifier><identifier>PMID: 33304193</identifier><language>eng</language><publisher>Tokyo: Pesticide Science Society of Japan</publisher><subject>Alanine ; Amino acids ; Bombyx mori ; Catalytic activity ; Detoxification ; Diazinon ; Fungicides ; Glutathione ; Glutathione transferase ; Hydrogen bonding ; Insecticides ; Lepidoptera ; Oxidative stress ; Residues ; Site-directed mutagenesis ; Xenobiotics</subject><ispartof>Journal of Pesticide Science, 2020/11/20, Vol.45(4), pp.238-240</ispartof><rights>Pesticide Science Society of Japan 2020. 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Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 Pesticide Science Society of Japan 2020 Pesticide Science Society of Japan</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c722t-68675a7b36992fde9ac528cc27c3578b0182170906cce9ed4f75f7d7789bd0963</citedby><cites>FETCH-LOGICAL-c722t-68675a7b36992fde9ac528cc27c3578b0182170906cce9ed4f75f7d7789bd0963</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/PMC7691559/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7691559/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,1876,27903,27904,53769,53771</link.rule.ids></links><search><creatorcontrib>Yamamoto, Kohji</creatorcontrib><creatorcontrib>Yamaguchi, Misuzu</creatorcontrib><creatorcontrib>Yamada, Naotaka</creatorcontrib><creatorcontrib>Department of Bioscience and Biotechnology</creatorcontrib><creatorcontrib>Kyushu University Graduate School</creatorcontrib><title>Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning</title><title>Journal of Pesticide Science</title><addtitle>J. Pestic. Sci.</addtitle><description>Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.</description><subject>Alanine</subject><subject>Amino acids</subject><subject>Bombyx mori</subject><subject>Catalytic activity</subject><subject>Detoxification</subject><subject>Diazinon</subject><subject>Fungicides</subject><subject>Glutathione</subject><subject>Glutathione transferase</subject><subject>Hydrogen bonding</subject><subject>Insecticides</subject><subject>Lepidoptera</subject><subject>Oxidative stress</subject><subject>Residues</subject><subject>Site-directed mutagenesis</subject><subject>Xenobiotics</subject><issn>1348-589X</issn><issn>1349-0923</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNpdUU1v1DAUjBCIVqV3jpa4cEl5tuOvCxIUWipV4gISN8txnKxXib3YyYr99zjsshVcni17Zt68N1X1GsMNZrJ5t925PHubbz4RqIHyZ9Ulpo2qQRH6_M9d1kyqHxfVdc5bAMCCCqX4y-qCUgoNVvSyCg9hv8oMZvYxoNijeeOQsbPfO5T97NYnE9AS7Ghy9r13HRrGZTbzphAcmpMJuXfJZId8QB_j1B5-oSkmj9oDMqMJvqCyNaFchlfVi96M2V2fzqvq-93nb7df6sev9w-3Hx5rKwiZay65YEa0lCtF-s4pYxmR1hJhKROyBSwJFqCAW-uU65pesF50QkjVdqA4vareH3V3Szu5zrpQfI56l_xk0kFH4_W_P8Fv9BD3WnCFGVNF4O1JIMWfS9mQnny2bizzuLhkTRpJG-CMywJ98x90G5cUyngFxTkIkAQKCo4om2LOyfVnMxj0mqf-m6cueeqSZ6HcHynFp7dmjGEsu3xStwe6cqwmsDKgYUA1YKaBUFlKU0QEU3xVujsqbfNsBndubVJpOLqn1g3TzVpOFs4AuzFJu0B_A1-3xd4</recordid><startdate>20201120</startdate><enddate>20201120</enddate><creator>Yamamoto, Kohji</creator><creator>Yamaguchi, Misuzu</creator><creator>Yamada, Naotaka</creator><general>Pesticide Science Society of Japan</general><general>Japan Science and Technology Agency</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SS</scope><scope>7ST</scope><scope>7TK</scope><scope>7U7</scope><scope>C1K</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20201120</creationdate><title>Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning</title><author>Yamamoto, Kohji ; Yamaguchi, Misuzu ; Yamada, Naotaka</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c722t-68675a7b36992fde9ac528cc27c3578b0182170906cce9ed4f75f7d7789bd0963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Alanine</topic><topic>Amino acids</topic><topic>Bombyx mori</topic><topic>Catalytic activity</topic><topic>Detoxification</topic><topic>Diazinon</topic><topic>Fungicides</topic><topic>Glutathione</topic><topic>Glutathione transferase</topic><topic>Hydrogen bonding</topic><topic>Insecticides</topic><topic>Lepidoptera</topic><topic>Oxidative stress</topic><topic>Residues</topic><topic>Site-directed mutagenesis</topic><topic>Xenobiotics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamamoto, Kohji</creatorcontrib><creatorcontrib>Yamaguchi, Misuzu</creatorcontrib><creatorcontrib>Yamada, Naotaka</creatorcontrib><creatorcontrib>Department of Bioscience and Biotechnology</creatorcontrib><creatorcontrib>Kyushu University Graduate School</creatorcontrib><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Pesticide Science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yamamoto, Kohji</au><au>Yamaguchi, Misuzu</au><au>Yamada, Naotaka</au><aucorp>Department of Bioscience and Biotechnology</aucorp><aucorp>Kyushu University Graduate School</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning</atitle><jtitle>Journal of Pesticide Science</jtitle><addtitle>J. Pestic. Sci.</addtitle><date>2020-11-20</date><risdate>2020</risdate><volume>45</volume><issue>4</issue><spage>238</spage><epage>240</epage><pages>238-240</pages><issn>1348-589X</issn><eissn>1349-0923</eissn><abstract>Glutathione transferase (GST) is an important class of detoxification enzymes that are vital for defense against various xenobiotics and cellular oxidative stress. Previously, we had reported an unclassified glutathione transferase 2 in Bombyx mori (bmGSTu2) to be responsible for detoxifying diazinon. In this study, we aimed to identify the amino acid residues that constitute a hydrogen-bonding network important for GST activity. Site-directed mutagenesis of bmGSTu2 suggested that residues Asn102, Pro162, and Ser166 contribute to its catalytic activity.</abstract><cop>Tokyo</cop><pub>Pesticide Science Society of Japan</pub><pmid>33304193</pmid><doi>10.1584/jpestics.D20-036</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| source | DOAJ Directory of Open Access Journals; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; PubMed Central |
| subjects | Alanine Amino acids Bombyx mori Catalytic activity Detoxification Diazinon Fungicides Glutathione Glutathione transferase Hydrogen bonding Insecticides Lepidoptera Oxidative stress Residues Site-directed mutagenesis Xenobiotics |
| title | Investigation of the active site of an unclassified glutathione transferase in Bombyx mori by alanine scanning |
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