Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.
Identifieur interne : 002D38 ( Main/Exploration ); précédent : 002D37; suivant : 002D39Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.
Auteurs : Trevor Addington [Espagne] ; Barbara Calisto ; Mercedes Alfonso-Prieto ; Carme Rovira ; Ignasi Fita ; Antoni PlanasSource :
- Proteins [ 1097-0134 ] ; 2011.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Bacillus (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Dosages enzymatiques (MeSH), Glucanes (composition chimique), Glycosidases (génétique), Glycosyltransferase (génétique), Ingénierie des protéines (MeSH), Liaison aux protéines (MeSH), Motifs d'acides aminés (MeSH), Mutagenèse dirigée (MeSH), Populus (MeSH), Protéines de fusion recombinantes (biosynthèse), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Similitude structurale de protéines (MeSH), Simulation de dynamique moléculaire (MeSH), Spécificité du substrat (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Xylanes (composition chimique), bêta-Glucanes (composition chimique).
- MESH :
- biosynthèse : Protéines de fusion recombinantes.
- composition chimique : Glucanes, Protéines de fusion recombinantes, Xylanes, bêta-Glucanes.
- génétique : Glycosidases, Glycosyltransferase, Protéines de fusion recombinantes.
- Alignement de séquences, Bacillus, Cristallographie aux rayons X, Données de séquences moléculaires, Dosages enzymatiques, Ingénierie des protéines, Liaison aux protéines, Motifs d'acides aminés, Mutagenèse dirigée, Populus, Similitude structurale de protéines, Simulation de dynamique moléculaire, Spécificité du substrat, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Bacillus (MeSH), Crystallography, X-Ray (MeSH), Enzyme Assays (MeSH), Glucans (chemistry), Glycoside Hydrolases (genetics), Glycosyltransferases (genetics), Molecular Dynamics Simulation (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Populus (MeSH), Protein Binding (MeSH), Protein Engineering (MeSH), Protein Structure, Tertiary (MeSH), Recombinant Fusion Proteins (biosynthesis), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Sequence Alignment (MeSH), Structural Homology, Protein (MeSH), Substrate Specificity (MeSH), Xylans (chemistry), beta-Glucans (chemistry).
- MESH :
- chemical , biosynthesis : Recombinant Fusion Proteins.
- chemical , chemistry : Glucans, Recombinant Fusion Proteins, Xylans, beta-Glucans.
- chemical , genetics : Glycoside Hydrolases, Glycosyltransferases, Recombinant Fusion Proteins.
- Amino Acid Motifs, Amino Acid Sequence, Bacillus, Crystallography, X-Ray, Enzyme Assays, Molecular Dynamics Simulation, Molecular Sequence Data, Mutagenesis, Site-Directed, Populus, Protein Binding, Protein Engineering, Protein Structure, Tertiary, Sequence Alignment, Structural Homology, Protein, Substrate Specificity.
Abstract
Family 16 carbohydrate active enzyme members Bacillus licheniformis 1,3-1,4-β-glucanase and Populus tremula x tremuloides xyloglucan endotransglycosylase (XET16-34) are highly structurally related but display different substrate specificities. Although the first binds linear gluco-oligosaccharides, the second binds branched xylogluco-oligosaccharides. Prior engineered nucleophile mutants of both enzymes are glycosynthases that catalyze the condensation between a glycosyl fluoride donor and a glycoside acceptor. With the aim of expanding the glycosynthase technology to produce designer oligosaccharides consisting of hybrids between branched xylogluco- and linear gluco-oligosaccharides, enzyme engineering on the negative subsites of 1,3-1,4-β-glucanase to accept branched substrates has been undertaken. Removal of the 1,3-1,4-β-glucanase major loop and replacement with that of XET16-34 to open the binding cleft resulted in a folded protein, which still maintained some β-glucan hydrolase activity, but the corresponding nucleophile mutant did not display glycosynthase activity with either linear or branched glycosyl donors. Next, point mutations of the 1,3-1,4-β-glucanase β-sheets forming the binding site cleft were mutated to resemble XET16-34 residues. The final chimeric protein acquired binding affinity for xyloglucan and did not bind β-glucan. Therefore, binding specificity has been re-engineered, but affinity was low and the nucleophile mutant of the chimeric enzyme did not show glycosynthase activity to produce the target hybrid oligosaccharides. Structural analysis by X-ray crystallography explains these results in terms of changes in the protein structure and highlights further engineering approaches toward introducing the desired activity.
DOI: 10.1002/prot.22884
PubMed: 21069723
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.</title><author><name sortKey="Addington, Trevor" sort="Addington, Trevor" uniqKey="Addington T" first="Trevor" last="Addington">Trevor Addington</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biochemistry, Bioengineering Department, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Laboratory of Biochemistry, Bioengineering Department, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Calisto, Barbara" sort="Calisto, Barbara" uniqKey="Calisto B" first="Barbara" last="Calisto">Barbara Calisto</name></author><author><name sortKey="Alfonso Prieto, Mercedes" sort="Alfonso Prieto, Mercedes" uniqKey="Alfonso Prieto M" first="Mercedes" last="Alfonso-Prieto">Mercedes Alfonso-Prieto</name></author><author><name sortKey="Rovira, Carme" sort="Rovira, Carme" uniqKey="Rovira C" first="Carme" last="Rovira">Carme Rovira</name></author><author><name sortKey="Fita, Ignasi" sort="Fita, Ignasi" uniqKey="Fita I" first="Ignasi" last="Fita">Ignasi Fita</name></author><author><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21069723</idno><idno type="pmid">21069723</idno><idno type="doi">10.1002/prot.22884</idno><idno type="wicri:Area/Main/Corpus">003017</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003017</idno><idno type="wicri:Area/Main/Curation">003017</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003017</idno><idno type="wicri:Area/Main/Exploration">003017</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.</title><author><name sortKey="Addington, Trevor" sort="Addington, Trevor" uniqKey="Addington T" first="Trevor" last="Addington">Trevor Addington</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Biochemistry, Bioengineering Department, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Laboratory of Biochemistry, Bioengineering Department, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Calisto, Barbara" sort="Calisto, Barbara" uniqKey="Calisto B" first="Barbara" last="Calisto">Barbara Calisto</name></author><author><name sortKey="Alfonso Prieto, Mercedes" sort="Alfonso Prieto, Mercedes" uniqKey="Alfonso Prieto M" first="Mercedes" last="Alfonso-Prieto">Mercedes Alfonso-Prieto</name></author><author><name sortKey="Rovira, Carme" sort="Rovira, Carme" uniqKey="Rovira C" first="Carme" last="Rovira">Carme Rovira</name></author><author><name sortKey="Fita, Ignasi" sort="Fita, Ignasi" uniqKey="Fita I" first="Ignasi" last="Fita">Ignasi Fita</name></author><author><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name></author></analytic><series><title level="j">Proteins</title><idno type="eISSN">1097-0134</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Bacillus (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Enzyme Assays (MeSH)</term><term>Glucans (chemistry)</term><term>Glycoside Hydrolases (genetics)</term><term>Glycosyltransferases (genetics)</term><term>Molecular Dynamics Simulation (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Populus (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Engineering (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Recombinant Fusion Proteins (biosynthesis)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Sequence Alignment (MeSH)</term><term>Structural Homology, Protein (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Xylans (chemistry)</term><term>beta-Glucans (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Bacillus (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Dosages enzymatiques (MeSH)</term><term>Glucanes (composition chimique)</term><term>Glycosidases (génétique)</term><term>Glycosyltransferase (génétique)</term><term>Ingénierie des protéines (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Populus (MeSH)</term><term>Protéines de fusion recombinantes (biosynthèse)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Similitude structurale de protéines (MeSH)</term><term>Simulation de dynamique moléculaire (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Xylanes (composition chimique)</term><term>bêta-Glucanes (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glucans</term><term>Recombinant Fusion Proteins</term><term>Xylans</term><term>beta-Glucans</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycoside Hydrolases</term><term>Glycosyltransferases</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glucanes</term><term>Protéines de fusion recombinantes</term><term>Xylanes</term><term>bêta-Glucanes</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycosidases</term><term>Glycosyltransferase</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Bacillus</term><term>Crystallography, X-Ray</term><term>Enzyme Assays</term><term>Molecular Dynamics Simulation</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Populus</term><term>Protein Binding</term><term>Protein Engineering</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Structural Homology, Protein</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Bacillus</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Dosages enzymatiques</term><term>Ingénierie des protéines</term><term>Liaison aux protéines</term><term>Motifs d'acides aminés</term><term>Mutagenèse dirigée</term><term>Populus</term><term>Similitude structurale de protéines</term><term>Simulation de dynamique moléculaire</term><term>Spécificité du substrat</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Family 16 carbohydrate active enzyme members Bacillus licheniformis 1,3-1,4-β-glucanase and Populus tremula x tremuloides xyloglucan endotransglycosylase (XET16-34) are highly structurally related but display different substrate specificities. Although the first binds linear gluco-oligosaccharides, the second binds branched xylogluco-oligosaccharides. Prior engineered nucleophile mutants of both enzymes are glycosynthases that catalyze the condensation between a glycosyl fluoride donor and a glycoside acceptor. With the aim of expanding the glycosynthase technology to produce designer oligosaccharides consisting of hybrids between branched xylogluco- and linear gluco-oligosaccharides, enzyme engineering on the negative subsites of 1,3-1,4-β-glucanase to accept branched substrates has been undertaken. Removal of the 1,3-1,4-β-glucanase major loop and replacement with that of XET16-34 to open the binding cleft resulted in a folded protein, which still maintained some β-glucan hydrolase activity, but the corresponding nucleophile mutant did not display glycosynthase activity with either linear or branched glycosyl donors. Next, point mutations of the 1,3-1,4-β-glucanase β-sheets forming the binding site cleft were mutated to resemble XET16-34 residues. The final chimeric protein acquired binding affinity for xyloglucan and did not bind β-glucan. Therefore, binding specificity has been re-engineered, but affinity was low and the nucleophile mutant of the chimeric enzyme did not show glycosynthase activity to produce the target hybrid oligosaccharides. Structural analysis by X-ray crystallography explains these results in terms of changes in the protein structure and highlights further engineering approaches toward introducing the desired activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21069723</PMID><DateCompleted><Year>2011</Year><Month>05</Month><Day>27</Day></DateCompleted><DateRevised><Year>2011</Year><Month>01</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>79</Volume><Issue>2</Issue><PubDate><Year>2011</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Proteins</Title><ISOAbbreviation>Proteins</ISOAbbreviation></Journal><ArticleTitle>Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.</ArticleTitle><Pagination><MedlinePgn>365-75</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/prot.22884</ELocationID><Abstract><AbstractText>Family 16 carbohydrate active enzyme members Bacillus licheniformis 1,3-1,4-β-glucanase and Populus tremula x tremuloides xyloglucan endotransglycosylase (XET16-34) are highly structurally related but display different substrate specificities. Although the first binds linear gluco-oligosaccharides, the second binds branched xylogluco-oligosaccharides. Prior engineered nucleophile mutants of both enzymes are glycosynthases that catalyze the condensation between a glycosyl fluoride donor and a glycoside acceptor. With the aim of expanding the glycosynthase technology to produce designer oligosaccharides consisting of hybrids between branched xylogluco- and linear gluco-oligosaccharides, enzyme engineering on the negative subsites of 1,3-1,4-β-glucanase to accept branched substrates has been undertaken. Removal of the 1,3-1,4-β-glucanase major loop and replacement with that of XET16-34 to open the binding cleft resulted in a folded protein, which still maintained some β-glucan hydrolase activity, but the corresponding nucleophile mutant did not display glycosynthase activity with either linear or branched glycosyl donors. Next, point mutations of the 1,3-1,4-β-glucanase β-sheets forming the binding site cleft were mutated to resemble XET16-34 residues. The final chimeric protein acquired binding affinity for xyloglucan and did not bind β-glucan. Therefore, binding specificity has been re-engineered, but affinity was low and the nucleophile mutant of the chimeric enzyme did not show glycosynthase activity to produce the target hybrid oligosaccharides. Structural analysis by X-ray crystallography explains these results in terms of changes in the protein structure and highlights further engineering approaches toward introducing the desired activity.</AbstractText><CopyrightInformation>© 2010 Wiley-Liss, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Addington</LastName><ForeName>Trevor</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Laboratory of Biochemistry, Bioengineering Department, Institut Químic de Sarrià, Universitat Ramon Llull, 08017 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Calisto</LastName><ForeName>Barbara</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Alfonso-Prieto</LastName><ForeName>Mercedes</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rovira</LastName><ForeName>Carme</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Fita</LastName><ForeName>Ignasi</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Planas</LastName><ForeName>Antoni</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proteins</MedlineTA><NlmUniqueID>8700181</NlmUniqueID><ISSNLinking>0887-3585</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047071">beta-Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>37294-28-3</RegistryNumber><NameOfSubstance UI="C029353">xyloglucan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.-</RegistryNumber><NameOfSubstance UI="D016695">Glycosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.207</RegistryNumber><NameOfSubstance UI="C473049">xyloglucan - xyloglucosyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.73</RegistryNumber><NameOfSubstance UI="C028020">licheninase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001407" MajorTopicYN="N">Bacillus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057075" MajorTopicYN="N">Enzyme Assays</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016695" MajorTopicYN="N">Glycosyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056004" MajorTopicYN="N">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015202" MajorTopicYN="N">Protein Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D047071" MajorTopicYN="N">beta-Glucans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21069723</ArticleId><ArticleId IdType="doi">10.1002/prot.22884</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Catalogne</li></region></list><tree><noCountry><name sortKey="Alfonso Prieto, Mercedes" sort="Alfonso Prieto, Mercedes" uniqKey="Alfonso Prieto M" first="Mercedes" last="Alfonso-Prieto">Mercedes Alfonso-Prieto</name><name sortKey="Calisto, Barbara" sort="Calisto, Barbara" uniqKey="Calisto B" first="Barbara" last="Calisto">Barbara Calisto</name><name sortKey="Fita, Ignasi" sort="Fita, Ignasi" uniqKey="Fita I" first="Ignasi" last="Fita">Ignasi Fita</name><name sortKey="Planas, Antoni" sort="Planas, Antoni" uniqKey="Planas A" first="Antoni" last="Planas">Antoni Planas</name><name sortKey="Rovira, Carme" sort="Rovira, Carme" uniqKey="Rovira C" first="Carme" last="Rovira">Carme Rovira</name></noCountry><country name="Espagne"><region name="Catalogne"><name sortKey="Addington, Trevor" sort="Addington, Trevor" uniqKey="Addington T" first="Trevor" last="Addington">Trevor Addington</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002D38 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002D38 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PoplarV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:21069723
|texte= Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:21069723" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PoplarV1
| This area was generated with Dilib version V0.6.37. |  |