His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases
Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between...
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| Veröffentlicht in: | Journal of enzyme inhibition and medicinal chemistry 2009-02, Vol.24 (1), p.38-46 |
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| creator | Rombouts, Sigrid Fierens, Ellen Vandermarliere, Elien Voet, Arnout Gebruers, Kurt Beaugrand, Johnny Courtin, Christophe M. Delcour, Jan A. de Maeyer, Marc Rabijns, Anja Van Campenhout, Steven Volckaert, Guido |
| description | Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed. |
| doi_str_mv | 10.1080/14756360701841913 |
| format | Article |
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It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.</description><identifier>ISSN: 1475-6366</identifier><identifier>EISSN: 1475-6374</identifier><identifier>DOI: 10.1080/14756360701841913</identifier><identifier>PMID: 18608747</identifier><language>eng</language><publisher>England: Informa UK Ltd</publisher><subject>Cloning, Molecular ; Endo-1,4-beta Xylanases - antagonists & inhibitors ; Glycoside Hydrolases - antagonists & inhibitors ; Histidine ; Models, Molecular ; Mutagenesis, Site-Directed ; Pichia pastoris ; Plant Proteins - genetics ; Plant Proteins - physiology ; Protein Binding ; protein-protein interaction ; site-directed mutagenesis ; Thaumatin-like protein ; Triticum ; Triticum aestivum ; xylanase inhibitor</subject><ispartof>Journal of enzyme inhibition and medicinal chemistry, 2009-02, Vol.24 (1), p.38-46</ispartof><rights>2009 Informa UK Ltd 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-f4a735aa5891f1dbd310819106112e5cfcca23b3e305c43d7cd67e27d307486c3</citedby><cites>FETCH-LOGICAL-c478t-f4a735aa5891f1dbd310819106112e5cfcca23b3e305c43d7cd67e27d307486c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.tandfonline.com/doi/pdf/10.1080/14756360701841913$$EPDF$$P50$$Ginformaworld$$H</linktopdf><linktohtml>$$Uhttps://www.tandfonline.com/doi/full/10.1080/14756360701841913$$EHTML$$P50$$Ginformaworld$$H</linktohtml><link.rule.ids>315,782,786,27931,27932,59654,60443,61228,61409</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18608747$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Fierens, Ellen</creatorcontrib><creatorcontrib>Vandermarliere, Elien</creatorcontrib><creatorcontrib>Voet, Arnout</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>Beaugrand, Johnny</creatorcontrib><creatorcontrib>Courtin, Christophe M.</creatorcontrib><creatorcontrib>Delcour, Jan A.</creatorcontrib><creatorcontrib>de Maeyer, Marc</creatorcontrib><creatorcontrib>Rabijns, Anja</creatorcontrib><creatorcontrib>Van Campenhout, Steven</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><title>His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases</title><title>Journal of enzyme inhibition and medicinal chemistry</title><addtitle>J Enzyme Inhib Med Chem</addtitle><description>Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.</description><subject>Cloning, Molecular</subject><subject>Endo-1,4-beta Xylanases - antagonists & inhibitors</subject><subject>Glycoside Hydrolases - antagonists & inhibitors</subject><subject>Histidine</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Pichia pastoris</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - physiology</subject><subject>Protein Binding</subject><subject>protein-protein interaction</subject><subject>site-directed mutagenesis</subject><subject>Thaumatin-like protein</subject><subject>Triticum</subject><subject>Triticum aestivum</subject><subject>xylanase inhibitor</subject><issn>1475-6366</issn><issn>1475-6374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9rGzEQxUVJaNK0H6CXoFNubjUrrbShuQTTNgFDLgn0po71p6ugXbnSmnS_fWRsGkohpxkev_eYeYR8BPYJWMc-g1Ct5JIpBp2AS-BvyOlOW0iuxNHfXcoT8q6UR8YaaEC8JSfQSdYpoU7Jz5tQmoYmT-9XP27pJuJcKFKTwxQMRppTdDSMdOp3ow_rqqdxx_-Ks0klWEf72VYMi6MehxBnCkD_zBHHKpX35NhjLO7DYZ6Rh29f75c3i9Xd99vl9WphhOqmhReoeIvYdpfgwa4trx_Wl5gEaFxrvDHY8DV3nLVGcKuMlco1ynKmRCcNPyMX-9xNTr-3rkx6CMW4WM9waVt0w6RUgvMKwh40OZWSndebHAbMswamd7Xq_2qtnvND-HY9OPviOPRYgas9EEaf8oBPKUerJ5xjyj7jaELR_LX8L__Ye4dx6g1mpx_TNo-1uFeuewZj4pa_</recordid><startdate>200902</startdate><enddate>200902</enddate><creator>Rombouts, Sigrid</creator><creator>Fierens, Ellen</creator><creator>Vandermarliere, Elien</creator><creator>Voet, Arnout</creator><creator>Gebruers, Kurt</creator><creator>Beaugrand, Johnny</creator><creator>Courtin, Christophe M.</creator><creator>Delcour, Jan A.</creator><creator>de Maeyer, Marc</creator><creator>Rabijns, Anja</creator><creator>Van Campenhout, Steven</creator><creator>Volckaert, Guido</creator><general>Informa UK Ltd</general><general>Taylor & Francis</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>200902</creationdate><title>His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases</title><author>Rombouts, Sigrid ; Fierens, Ellen ; Vandermarliere, Elien ; Voet, Arnout ; Gebruers, Kurt ; Beaugrand, Johnny ; Courtin, Christophe M. ; Delcour, Jan A. ; de Maeyer, Marc ; Rabijns, Anja ; Van Campenhout, Steven ; Volckaert, Guido</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-f4a735aa5891f1dbd310819106112e5cfcca23b3e305c43d7cd67e27d307486c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Cloning, Molecular</topic><topic>Endo-1,4-beta Xylanases - antagonists & inhibitors</topic><topic>Glycoside Hydrolases - antagonists & inhibitors</topic><topic>Histidine</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed</topic><topic>Pichia pastoris</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - physiology</topic><topic>Protein Binding</topic><topic>protein-protein interaction</topic><topic>site-directed mutagenesis</topic><topic>Thaumatin-like protein</topic><topic>Triticum</topic><topic>Triticum aestivum</topic><topic>xylanase inhibitor</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Fierens, Ellen</creatorcontrib><creatorcontrib>Vandermarliere, Elien</creatorcontrib><creatorcontrib>Voet, Arnout</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>Beaugrand, Johnny</creatorcontrib><creatorcontrib>Courtin, Christophe M.</creatorcontrib><creatorcontrib>Delcour, Jan A.</creatorcontrib><creatorcontrib>de Maeyer, Marc</creatorcontrib><creatorcontrib>Rabijns, Anja</creatorcontrib><creatorcontrib>Van Campenhout, Steven</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of enzyme inhibition and medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rombouts, Sigrid</au><au>Fierens, Ellen</au><au>Vandermarliere, Elien</au><au>Voet, Arnout</au><au>Gebruers, Kurt</au><au>Beaugrand, Johnny</au><au>Courtin, Christophe M.</au><au>Delcour, Jan A.</au><au>de Maeyer, Marc</au><au>Rabijns, Anja</au><au>Van Campenhout, Steven</au><au>Volckaert, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases</atitle><jtitle>Journal of enzyme inhibition and medicinal chemistry</jtitle><addtitle>J Enzyme Inhib Med Chem</addtitle><date>2009-02</date><risdate>2009</risdate><volume>24</volume><issue>1</issue><spage>38</spage><epage>46</epage><pages>38-46</pages><issn>1475-6366</issn><eissn>1475-6374</eissn><abstract>Recently, a novel wheat thaumatin-like protein, TLXI, which inhibits microbial glycoside hydrolase family (GH) 11 xylanases has been identified. It is the first xylanase inhibitor that exerts its inhibition in a non-competitive way. In the present study we gained insight into the interaction between TLXI and xylanases via combined molecular modeling and mutagenic approaches. More specifically, site-specific mutation of His22, situated on a loop which distinguishes TLXI from other, non-inhibiting, thaumatin-like proteins, and subsequent expression of the mutant in Pichia pastoris resulted in a protein lacking inhibition capacity. The mutant protein was unable to form a complex with GH11 xylanases. Based on these findings, the interaction of TLXI with GH11 xylanases is discussed.</abstract><cop>England</cop><pub>Informa UK Ltd</pub><pmid>18608747</pmid><doi>10.1080/14756360701841913</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of enzyme inhibition and medicinal chemistry, 2009-02, Vol.24 (1), p.38-46 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Taylor & Francis Journals Complete |
| subjects | Cloning, Molecular Endo-1,4-beta Xylanases - antagonists & inhibitors Glycoside Hydrolases - antagonists & inhibitors Histidine Models, Molecular Mutagenesis, Site-Directed Pichia pastoris Plant Proteins - genetics Plant Proteins - physiology Protein Binding protein-protein interaction site-directed mutagenesis Thaumatin-like protein Triticum Triticum aestivum xylanase inhibitor |
| title | His22 of TLXI plays a critical role in the inhibition of glycoside hydrolase family 11 xylanases |
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