Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">CelI, a Noncellulosomal Family 9 Enzyme from <italic>Clostridium thermocellum</italic>, Is a Processive Endoglucanase That Degrades Crystalline Cellulose</title><author><name sortKey="Gilad, Rachel" sort="Gilad, Rachel" uniqKey="Gilad R" first="Rachel" last="Gilad">Rachel Gilad</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Rabinovich, Larisa" sort="Rabinovich, Larisa" uniqKey="Rabinovich L" first="Larisa" last="Rabinovich">Larisa Rabinovich</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Yaron, Sima" sort="Yaron, Sima" uniqKey="Yaron S" first="Sima" last="Yaron">Sima Yaron</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Bayer, Edward A" sort="Bayer, Edward A" uniqKey="Bayer E" first="Edward A." last="Bayer">Edward A. Bayer</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lamed, Raphael" sort="Lamed, Raphael" uniqKey="Lamed R" first="Raphael" last="Lamed">Raphael Lamed</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Gilbert, Harry J" sort="Gilbert, Harry J" uniqKey="Gilbert H" first="Harry J." last="Gilbert">Harry J. Gilbert</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Shoham, Yuval" sort="Shoham, Yuval" uniqKey="Shoham Y" first="Yuval" last="Shoham">Yuval Shoham</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12511483</idno><idno type="pmc">145334</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC145334</idno><idno type="RBID">PMC:145334</idno><idno type="doi">10.1128/JB.185.2.391-398.2003</idno><date when="2003">2003</date><idno type="wicri:Area/Pmc/Corpus">000770</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">CelI, a Noncellulosomal Family 9 Enzyme from <italic>Clostridium thermocellum</italic>, Is a Processive Endoglucanase That Degrades Crystalline Cellulose</title><author><name sortKey="Gilad, Rachel" sort="Gilad, Rachel" uniqKey="Gilad R" first="Rachel" last="Gilad">Rachel Gilad</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Rabinovich, Larisa" sort="Rabinovich, Larisa" uniqKey="Rabinovich L" first="Larisa" last="Rabinovich">Larisa Rabinovich</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Yaron, Sima" sort="Yaron, Sima" uniqKey="Yaron S" first="Sima" last="Yaron">Sima Yaron</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Bayer, Edward A" sort="Bayer, Edward A" uniqKey="Bayer E" first="Edward A." last="Bayer">Edward A. Bayer</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Lamed, Raphael" sort="Lamed, Raphael" uniqKey="Lamed R" first="Raphael" last="Lamed">Raphael Lamed</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Gilbert, Harry J" sort="Gilbert, Harry J" uniqKey="Gilbert H" first="Harry J." last="Gilbert">Harry J. Gilbert</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Shoham, Yuval" sort="Shoham, Yuval" uniqKey="Shoham Y" first="Yuval" last="Shoham">Yuval Shoham</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The family 9 cellulase gene <italic>celI</italic> of <italic>Clostridium thermocellum</italic>, was previously cloned, expressed, and characterized (G. P. Hazlewood, K. Davidson, J. I. Laurie, N. S. Huskisson, and H. J. Gilbert, J. Gen. Microbiol. 139:307-316, 1993). We have recloned and sequenced the entire <italic>celI</italic> gene and found that the published sequence contained a 53-bp deletion that generated a frameshift mutation, resulting in a truncated and modified C-terminal segment of the protein. The enzymatic properties of the wild-type protein were characterized and found to conform to those of other family 9 glycoside hydrolases with a so-called theme B architecture, where the catalytic module is fused to a family 3c carbohydrate-binding module (CBM3c); CelI also contains a C-terminal CBM3b. The intact recombinant CelI exhibited high levels of activity on all cellulosic substrates tested, with pH and temperature optima of 5.5 and 70°C, respectively, using carboxymethylcellulose as a substrate. Native CelI was capable of solubilizing filter paper, and the distribution of reducing sugar between the soluble and insoluble fractions suggests that the enzyme acts as a processive cellulase. A truncated form of the enzyme, lacking the C terminal CBM3b, failed to bind to crystalline cellulose and displayed reduced activity toward insoluble substrates. A truncated form of the enzyme, in which both the cellulose-binding CBM3b and the fused CBM3c were removed, failed to exhibit significant levels of activity on any of the substrates examined. This study underscores the general nature of this type of enzymatic theme, whereby the fused CBM3c plays a critical accessory role for the family 9 catalytic domain and changes its character to facilitate processive cleavage of recalcitrant cellulose substrates.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id><journal-id journal-id-type="publisher-id">jb</journal-id><journal-title>Journal of Bacteriology</journal-title><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12511483</article-id><article-id pub-id-type="pmc">145334</article-id><article-id pub-id-type="publisher-id">0983</article-id><article-id pub-id-type="doi">10.1128/JB.185.2.391-398.2003</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymes and Proteins</subject></subj-group></article-categories><title-group><article-title>CelI, a Noncellulosomal Family 9 Enzyme from <italic>Clostridium thermocellum</italic>, Is a Processive Endoglucanase That Degrades Crystalline Cellulose</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Gilad</surname><given-names>Rachel</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Rabinovich</surname><given-names>Larisa</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Yaron</surname><given-names>Sima</given-names></name><xref ref-type="aff" rid="aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Bayer</surname><given-names>Edward A.</given-names></name><xref ref-type="aff" rid="aff1">2</xref></contrib><contrib contrib-type="author"><name><surname>Lamed</surname><given-names>Raphael</given-names></name><xref ref-type="aff" rid="aff1">3</xref></contrib><contrib contrib-type="author"><name><surname>Gilbert</surname><given-names>Harry J.</given-names></name><xref ref-type="aff" rid="aff1">4</xref></contrib><contrib contrib-type="author"><name><surname>Shoham</surname><given-names>Yuval</given-names></name><xref ref-type="aff" rid="aff1">1</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="aff1">Department of Food Engineering and Biotechnology and Institute of Catalysis Science and Technology, Technion—Israel Institute of Technology, Haifa 32000,<label>1</label> Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100,<label>2</label> Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv 69978, Israel,<label>3</label> Department of Biological and Nutritional Sciences, University of Newcastle-upon-Tyne, Newcastle-upon-Tyne NE1 7RU, United Kingdom<label>4</label></aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address: Department of Food Engineering and Biotechnology, Technion—Israel Institute of Technology, Haifa 32000, Israel. Phone: (972) 4-829-3072. Fax: (972) 4-832-0742. E-mail: <email>yshoham@tx.chnion.ac.il</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>1</month><year>2003</year></pub-date><volume>185</volume><issue>2</issue><fpage>391</fpage><lpage>398</lpage><history><date date-type="received"><day>5</day><month>8</month><year>2002</year></date><date date-type="accepted"><day>21</day><month>10</month><year>2002</year></date></history><copyright-statement>Copyright © 2003, American Society for Microbiology</copyright-statement><copyright-year>2003</copyright-year><abstract><p>The family 9 cellulase gene <italic>celI</italic> of <italic>Clostridium thermocellum</italic>, was previously cloned, expressed, and characterized (G. P. Hazlewood, K. Davidson, J. I. Laurie, N. S. Huskisson, and H. J. Gilbert, J. Gen. Microbiol. 139:307-316, 1993). We have recloned and sequenced the entire <italic>celI</italic> gene and found that the published sequence contained a 53-bp deletion that generated a frameshift mutation, resulting in a truncated and modified C-terminal segment of the protein. The enzymatic properties of the wild-type protein were characterized and found to conform to those of other family 9 glycoside hydrolases with a so-called theme B architecture, where the catalytic module is fused to a family 3c carbohydrate-binding module (CBM3c); CelI also contains a C-terminal CBM3b. The intact recombinant CelI exhibited high levels of activity on all cellulosic substrates tested, with pH and temperature optima of 5.5 and 70°C, respectively, using carboxymethylcellulose as a substrate. Native CelI was capable of solubilizing filter paper, and the distribution of reducing sugar between the soluble and insoluble fractions suggests that the enzyme acts as a processive cellulase. A truncated form of the enzyme, lacking the C terminal CBM3b, failed to bind to crystalline cellulose and displayed reduced activity toward insoluble substrates. A truncated form of the enzyme, in which both the cellulose-binding CBM3b and the fused CBM3c were removed, failed to exhibit significant levels of activity on any of the substrates examined. This study underscores the general nature of this type of enzymatic theme, whereby the fused CBM3c plays a critical accessory role for the family 9 catalytic domain and changes its character to facilitate processive cleavage of recalcitrant cellulose substrates.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Bois/explor/OrangerV1/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000770 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 000770 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Bois
|area= OrangerV1
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.25. |  |