Identification of activity related amino acid mutations of a GH9 termite cellulase
Site-directed mutagenesis of the endo-β-1,4-glucanase (EG) gene from the termite Reticulitermes speratus EG (RsEG) was performed to gain a better understanding of the role of certain amino acid residues in the activity of the enzyme. Three mutants, G91A, Y97W and K429A had higher activities towards...
Gespeichert in:
| Veröffentlicht in: | Bioresource technology 2010-08, Vol.101 (16), p.6438-6443 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6443 |
|---|---|
| container_issue | 16 |
| container_start_page | 6438 |
| container_title | Bioresource technology |
| container_volume | 101 |
| creator | Ni, Jinfeng Takehara, Motomi Watanabe, Hirofumi |
| description | Site-directed mutagenesis of the endo-β-1,4-glucanase (EG) gene from the termite
Reticulitermes speratus EG (RsEG) was performed to gain a better understanding of the role of certain amino acid residues in the activity of the enzyme. Three mutants, G91A, Y97W and K429A had higher activities towards carboxymethyl cellulose than the wild type. The mutations had synergistic effects since each single mutant exhibited about 3–4-fold of wild type activity, but the corresponding activities for double and triple mutants were 7–13-fold. Mutant G147R lost the enzymatic activity completely, suggesting G147 plays a significant role in maintaining enzyme activity. The predicted roles of Asp53, Asp56 and Glu411 in enzymatic catalysis were experimentally verified since the resultant mutants lost the enzyme activities. This study presents the first report on the relationship between amino acid residues and enzyme activity of termite EG, and the information will potentially be useful for industrial application of termite-origin cellulase. |
| doi_str_mv | 10.1016/j.biortech.2010.03.045 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_746009148</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0960852410005225</els_id><sourcerecordid>746009148</sourcerecordid><originalsourceid>FETCH-LOGICAL-c486t-93160b4ccc511c2a6f0488efd1815ceb08d4302c6af56b2f43b9dbd8283715193</originalsourceid><addsrcrecordid>eNqF0E1v1DAQBmALgehS-AslFwSXLOOPOM4NVEFbqRIS0LPl2GPwKomL7VTqv8fb3cINTpZGz3hevYScUdhSoPL9bjuGmAran1sGdQh8C6J7QjZU9bxlQy-fkg0MElrVMXFCXuS8AwBOe_acnDDgkgnONuTrlcOlBB-sKSEuTfSNsSXchXLfJJxMQdeYOSyxjoNr5rU8uPwAm4vLoSmY5lCwsThN62QyviTPvJkyvjq-p-Tm86fv55ft9ZeLq_OP160VSpZ24FTCKKy1HaWWGelBKIXeUUU7iyMoJzgwK43v5Mi84OPgRqeY4j3t6MBPydvDv7cp_loxFz2HvE9hFoxr1r2QAAMVqsp3_5RU9pRTJruuUnmgNsWcE3p9m8Js0r2moPfN651-bF7vm9fAdW2-Lp4db6zjjO7P2mPVFbw5ApOtmXwyiw35r2MKZKf2YV8fnDdRmx-pmptv9RIHqgQFwav4cBBY270LmHS2AReLLiS0RbsY_pf2N-PkrQk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1671312655</pqid></control><display><type>article</type><title>Identification of activity related amino acid mutations of a GH9 termite cellulase</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Ni, Jinfeng ; Takehara, Motomi ; Watanabe, Hirofumi</creator><creatorcontrib>Ni, Jinfeng ; Takehara, Motomi ; Watanabe, Hirofumi</creatorcontrib><description>Site-directed mutagenesis of the endo-β-1,4-glucanase (EG) gene from the termite
Reticulitermes speratus EG (RsEG) was performed to gain a better understanding of the role of certain amino acid residues in the activity of the enzyme. Three mutants, G91A, Y97W and K429A had higher activities towards carboxymethyl cellulose than the wild type. The mutations had synergistic effects since each single mutant exhibited about 3–4-fold of wild type activity, but the corresponding activities for double and triple mutants were 7–13-fold. Mutant G147R lost the enzymatic activity completely, suggesting G147 plays a significant role in maintaining enzyme activity. The predicted roles of Asp53, Asp56 and Glu411 in enzymatic catalysis were experimentally verified since the resultant mutants lost the enzyme activities. This study presents the first report on the relationship between amino acid residues and enzyme activity of termite EG, and the information will potentially be useful for industrial application of termite-origin cellulase.</description><identifier>ISSN: 0960-8524</identifier><identifier>EISSN: 1873-2976</identifier><identifier>DOI: 10.1016/j.biortech.2010.03.045</identifier><identifier>PMID: 20362432</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Activity ; Amino Acid Sequence ; Amino acids ; Amino Acids - genetics ; Animals ; Biocatalysis ; Biological and medical sciences ; Catalytic Domain ; Cellulase ; Cellulase - chemistry ; Cellulase - genetics ; Cellulase - metabolism ; Enzyme activity ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gain ; Genes ; Isoptera ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutations ; Residues ; Resultants ; Reticulitermes speratus ; Sequence Homology, Amino Acid ; Site-directed mutagenesis ; Termite</subject><ispartof>Bioresource technology, 2010-08, Vol.101 (16), p.6438-6443</ispartof><rights>2010 Elsevier Ltd</rights><rights>2015 INIST-CNRS</rights><rights>Copyright 2010 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c486t-93160b4ccc511c2a6f0488efd1815ceb08d4302c6af56b2f43b9dbd8283715193</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0960852410005225$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22806588$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20362432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ni, Jinfeng</creatorcontrib><creatorcontrib>Takehara, Motomi</creatorcontrib><creatorcontrib>Watanabe, Hirofumi</creatorcontrib><title>Identification of activity related amino acid mutations of a GH9 termite cellulase</title><title>Bioresource technology</title><addtitle>Bioresour Technol</addtitle><description>Site-directed mutagenesis of the endo-β-1,4-glucanase (EG) gene from the termite
Reticulitermes speratus EG (RsEG) was performed to gain a better understanding of the role of certain amino acid residues in the activity of the enzyme. Three mutants, G91A, Y97W and K429A had higher activities towards carboxymethyl cellulose than the wild type. The mutations had synergistic effects since each single mutant exhibited about 3–4-fold of wild type activity, but the corresponding activities for double and triple mutants were 7–13-fold. Mutant G147R lost the enzymatic activity completely, suggesting G147 plays a significant role in maintaining enzyme activity. The predicted roles of Asp53, Asp56 and Glu411 in enzymatic catalysis were experimentally verified since the resultant mutants lost the enzyme activities. This study presents the first report on the relationship between amino acid residues and enzyme activity of termite EG, and the information will potentially be useful for industrial application of termite-origin cellulase.</description><subject>Activity</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Amino Acids - genetics</subject><subject>Animals</subject><subject>Biocatalysis</subject><subject>Biological and medical sciences</subject><subject>Catalytic Domain</subject><subject>Cellulase</subject><subject>Cellulase - chemistry</subject><subject>Cellulase - genetics</subject><subject>Cellulase - metabolism</subject><subject>Enzyme activity</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gain</subject><subject>Genes</subject><subject>Isoptera</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutations</subject><subject>Residues</subject><subject>Resultants</subject><subject>Reticulitermes speratus</subject><subject>Sequence Homology, Amino Acid</subject><subject>Site-directed mutagenesis</subject><subject>Termite</subject><issn>0960-8524</issn><issn>1873-2976</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1v1DAQBmALgehS-AslFwSXLOOPOM4NVEFbqRIS0LPl2GPwKomL7VTqv8fb3cINTpZGz3hevYScUdhSoPL9bjuGmAran1sGdQh8C6J7QjZU9bxlQy-fkg0MElrVMXFCXuS8AwBOe_acnDDgkgnONuTrlcOlBB-sKSEuTfSNsSXchXLfJJxMQdeYOSyxjoNr5rU8uPwAm4vLoSmY5lCwsThN62QyviTPvJkyvjq-p-Tm86fv55ft9ZeLq_OP160VSpZ24FTCKKy1HaWWGelBKIXeUUU7iyMoJzgwK43v5Mi84OPgRqeY4j3t6MBPydvDv7cp_loxFz2HvE9hFoxr1r2QAAMVqsp3_5RU9pRTJruuUnmgNsWcE3p9m8Js0r2moPfN651-bF7vm9fAdW2-Lp4db6zjjO7P2mPVFbw5ApOtmXwyiw35r2MKZKf2YV8fnDdRmx-pmptv9RIHqgQFwav4cBBY270LmHS2AReLLiS0RbsY_pf2N-PkrQk</recordid><startdate>20100801</startdate><enddate>20100801</enddate><creator>Ni, Jinfeng</creator><creator>Takehara, Motomi</creator><creator>Watanabe, Hirofumi</creator><general>Elsevier Ltd</general><general>[New York, NY]: Elsevier Ltd</general><general>Elsevier</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>7SU</scope><scope>7TB</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>KR7</scope><scope>7QO</scope><scope>7SS</scope><scope>7ST</scope><scope>P64</scope><scope>SOI</scope></search><sort><creationdate>20100801</creationdate><title>Identification of activity related amino acid mutations of a GH9 termite cellulase</title><author>Ni, Jinfeng ; Takehara, Motomi ; Watanabe, Hirofumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c486t-93160b4ccc511c2a6f0488efd1815ceb08d4302c6af56b2f43b9dbd8283715193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Activity</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Amino Acids - genetics</topic><topic>Animals</topic><topic>Biocatalysis</topic><topic>Biological and medical sciences</topic><topic>Catalytic Domain</topic><topic>Cellulase</topic><topic>Cellulase - chemistry</topic><topic>Cellulase - genetics</topic><topic>Cellulase - metabolism</topic><topic>Enzyme activity</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gain</topic><topic>Genes</topic><topic>Isoptera</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutations</topic><topic>Residues</topic><topic>Resultants</topic><topic>Reticulitermes speratus</topic><topic>Sequence Homology, Amino Acid</topic><topic>Site-directed mutagenesis</topic><topic>Termite</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ni, Jinfeng</creatorcontrib><creatorcontrib>Takehara, Motomi</creatorcontrib><creatorcontrib>Watanabe, Hirofumi</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>Environmental Engineering Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Civil Engineering Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><jtitle>Bioresource technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ni, Jinfeng</au><au>Takehara, Motomi</au><au>Watanabe, Hirofumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of activity related amino acid mutations of a GH9 termite cellulase</atitle><jtitle>Bioresource technology</jtitle><addtitle>Bioresour Technol</addtitle><date>2010-08-01</date><risdate>2010</risdate><volume>101</volume><issue>16</issue><spage>6438</spage><epage>6443</epage><pages>6438-6443</pages><issn>0960-8524</issn><eissn>1873-2976</eissn><abstract>Site-directed mutagenesis of the endo-β-1,4-glucanase (EG) gene from the termite
Reticulitermes speratus EG (RsEG) was performed to gain a better understanding of the role of certain amino acid residues in the activity of the enzyme. Three mutants, G91A, Y97W and K429A had higher activities towards carboxymethyl cellulose than the wild type. The mutations had synergistic effects since each single mutant exhibited about 3–4-fold of wild type activity, but the corresponding activities for double and triple mutants were 7–13-fold. Mutant G147R lost the enzymatic activity completely, suggesting G147 plays a significant role in maintaining enzyme activity. The predicted roles of Asp53, Asp56 and Glu411 in enzymatic catalysis were experimentally verified since the resultant mutants lost the enzyme activities. This study presents the first report on the relationship between amino acid residues and enzyme activity of termite EG, and the information will potentially be useful for industrial application of termite-origin cellulase.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>20362432</pmid><doi>10.1016/j.biortech.2010.03.045</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-8524 |
| ispartof | Bioresource technology, 2010-08, Vol.101 (16), p.6438-6443 |
| issn | 0960-8524 1873-2976 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_746009148 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Activity Amino Acid Sequence Amino acids Amino Acids - genetics Animals Biocatalysis Biological and medical sciences Catalytic Domain Cellulase Cellulase - chemistry Cellulase - genetics Cellulase - metabolism Enzyme activity Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gain Genes Isoptera Molecular Sequence Data Mutagenesis, Site-Directed Mutations Residues Resultants Reticulitermes speratus Sequence Homology, Amino Acid Site-directed mutagenesis Termite |
| title | Identification of activity related amino acid mutations of a GH9 termite cellulase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T19%3A16%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Identification%20of%20activity%20related%20amino%20acid%20mutations%20of%20a%20GH9%20termite%20cellulase&rft.jtitle=Bioresource%20technology&rft.au=Ni,%20Jinfeng&rft.date=2010-08-01&rft.volume=101&rft.issue=16&rft.spage=6438&rft.epage=6443&rft.pages=6438-6443&rft.issn=0960-8524&rft.eissn=1873-2976&rft_id=info:doi/10.1016/j.biortech.2010.03.045&rft_dat=%3Cproquest_cross%3E746009148%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1671312655&rft_id=info:pmid/20362432&rft_els_id=S0960852410005225&rfr_iscdi=true |